The Involvement of the nif-Associated Ferredoxin-Like Genes fdxA and fdxN of Herbaspirillum seropedicae in Nitrogen Fixation

The pathway of electron transport to nitrogenase in the endophytic β-Proteobacterium Herbaspirillum seropedicae has not been characterized. We have generated mutants in two nif-associated genes encoding putative ferredoxins, fdxA and fdxN. The fdxA gene is part of the operon nifHDKENXorf1orf2fdxAnif...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	The journal of microbiology Jg. 48; H. 1; S. 77 - 83
Hauptverfasser:	Souza, Andre L.F., Universidade Federal do Parana, CP, Brazil, Invitti, Adriana L., Universidade Federal do Parana, CP, Brazil, Rego, Fabiane G.M., Universidade Federal do Parana, CP, Brazil, Monteiro, Rose A., Universidade Federal do Parana, CP, Brazil, Klassen, Giseli, Universidade Federal do Parana, CP, Brazil, Souza, Emanuel M., Universidade Federal do Parana, CP, Brazil, Chubatsu, Leda S., Universidade Federal do Parana, CP, Brazil, Pedrosa, Fabio O., Universidade Federal do Parana, CP, Brazil, Rigo, Liu U., Universidade Federal do Parana, CP, Brazil
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	Heidelberg The Microbiological Society of Korea 01.02.2010 Springer Nature B.V 한국미생물학회
Schlagworte:	Ammonium Antibiotics Bacterial Proteins - genetics Bacterial Proteins - metabolism Biomedical and Life Sciences Cloning DNA Mutational Analysis fdxA fdxN ferredoxin Ferredoxins - genetics Ferredoxins - metabolism Genes H. seropedicae Herbaspirillum - genetics Herbaspirillum - metabolism Life Sciences Microbiology Molecular biology Mutation Nitrogen Nitrogen fixation Nitrogen Fixation - genetics NITROGENASA NITROGENASE Nitrogenase - metabolism Phenotype Plasmids Promoter Regions, Genetic Proteins Transcription, Genetic 생물학 Brazil ferredoxin nitrogenase
ISSN:	1225-8873, 1976-3794, 1976-3794
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Abstract	The pathway of electron transport to nitrogenase in the endophytic β-Proteobacterium Herbaspirillum seropedicae has not been characterized. We have generated mutants in two nif-associated genes encoding putative ferredoxins, fdxA and fdxN. The fdxA gene is part of the operon nifHDKENXorf1orf2fdxAnifQmodABC and is transcribed from the nifH promoter, as revealed by lacZ gene fusion. The fdxN gene is probably co-transcribed with the nifB gene. Mutational analysis suggests that the FdxA protein is essential for maximum nitrogenase activity, since the nitrogenase activity of the fdxA mutant strain was reduced to about 30% of that of the wild-type strain. In addition, the fdxA mutation had no effect on the nitrogenase switch-off in response to ammonium. Nitrogenase activity of a mutant strain lacking the fdxN gene was completely abolished. This phenotype was reverted by complementation with fdxN expressed under lacZ promoter control. The results suggest that the products of both the fdxA and fdxN genes are probably involved in electron transfer during nitrogen fixation.
AbstractList	The pathway of electron transport to nitrogenase in the endophytic β-Proteobacterium Herbaspirillum seropedicae has not been characterized. We have generated mutants in two nif-associated genes encoding putative ferredoxins, fdxA and fdxN. The fdxA gene is part of the operon nifHDKENXorf1orf2fdxAnifQmodABC and is transcribed from the nifH promoter, as revealed by lacZ gene fusion. The fdxN gene is probably cotranscribed with the nifB gene. Mutational analysis suggests that the FdxA protein is essential for maximum nitrogenase activity, since the nitrogenase activity of the fdxA mutant strain was reduced to about 30% of that of the wild-type strain. In addition, the fdxA mutation had no effect on the nitrogenase switch-off in response to ammonium. Nitrogenase activity of a mutant strain lacking the fdxN gene was completely abolished. This phenotype was reverted by complementation with fdxN expressed under lacZ promoter control. The results suggest that the products of both the fdxA and fdxN genes are probably involved in electron transfer during nitrogen fixation. KCI Citation Count: 8 The pathway of electron transport to nitrogenase in the endophytic β-Proteobacterium Herbaspirillum seropedicae has not been characterized. We have generated mutants in two nif-associated genes encoding putative ferredoxins, fdxA and fdxN. The fdxA gene is part of the operon nifHDKENXorf1orf2fdxAnifQmodABC and is transcribed from the nifH promoter, as revealed by lacZ gene fusion. The fdxN gene is probably co-transcribed with the nifB gene. Mutational analysis suggests that the FdxA protein is essential for maximum nitrogenase activity, since the nitrogenase activity of the fdxA mutant strain was reduced to about 30% of that of the wild-type strain. In addition, the fdxA mutation had no effect on the nitrogenase switch-off in response to ammonium. Nitrogenase activity of a mutant strain lacking the fdxN gene was completely abolished. This phenotype was reverted by complementation with fdxN expressed under lacZ promoter control. The results suggest that the products of both the fdxA and fdxN genes are probably involved in electron transfer during nitrogen fixation. The pathway of electron transport to nitrogenase in the endophytic β-Proteobacterium Herbaspirillum seropedicae has not been characterized. We have generated mutants in two nif-associated genes encoding putative ferredoxins, fdxA and fdxN. The fdxA gene is part of the operon nifHDKENXorf1orf2fdxAnifQmodABC and is transcribed from the nifH promoter, as revealed by lacZ gene fusion. The fdxN gene is probably cotranscribed with the nifB gene. Mutational analysis suggests that the FdxA protein is essential for maximum nitrogenase activity, since the nitrogenase activity of the fdxA mutant strain was reduced to about 30% of that of the wild-type strain. In addition, the fdxA mutation had no effect on the nitrogenase switch-off in response to ammonium. Nitrogenase activity of a mutant strain lacking the fdxN gene was completely abolished. This phenotype was reverted by complementation with fdxN expressed under lacZ promoter control. The results suggest that the products of both the fdxA and fdxN genes are probably involved in electron transfer during nitrogen fixation.[PUBLICATION ABSTRACT] The pathway of electron transport to nitrogenase in the endophytic beta-Proteobacterium Herbaspirillum seropedicae has not been characterized. We have generated mutants in two nif-associated genes encoding putative ferredoxins, fdxA and fdxN. The fdxA gene is part of the operon nifHDKENXorf1orf2fdxAnifQmodABC and is transcribed from the nifH promoter, as revealed by lacZ gene fusion. The fdxN gene is probably cotranscribed with the nifB gene. Mutational analysis suggests that the FdxA protein is essential for maximum nitrogenase activity, since the nitrogenase activity of the fdxA mutant strain was reduced to about 30% of that of the wild-type strain. In addition, the fdxA mutation had no effect on the nitrogenase switch-off in response to ammonium. Nitrogenase activity of a mutant strain lacking the fdxN gene was completely abolished. This phenotype was reverted by complementation with fdxN expressed under lacZ promoter control. The results suggest that the products of both the fdxA and fdxN genes are probably involved in electron transfer during nitrogen fixation. The pathway of electron transport to nitrogenase in the endophytic β-Proteobacterium Herbaspirillum seropedicae has not been characterized. We have generated mutants in two nif -associated genes encoding putative ferredoxins, fdxA and fdxN . The fdxA gene is part of the operon nifHDKENXorf1orf2fdxAnifQmodABC and is transcribed from the nifH promoter, as revealed by lacZ gene fusion. The fdxN gene is probably cotranscribed with the nifB gene. Mutational analysis suggests that the FdxA protein is essential for maximum nitrogenase activity, since the nitrogenase activity of the fdxA mutant strain was reduced to about 30% of that of the wild-type strain. In addition, the fdxA mutation had no effect on the nitrogenase switch-off in response to ammonium. Nitrogenase activity of a mutant strain lacking the fdxN gene was completely abolished. This phenotype was reverted by complementation with fdxN expressed under lacZ promoter control. The results suggest that the products of both the fdxA and fdxN genes are probably involved in electron transfer during nitrogen fixation. The pathway of electron transport to nitrogenase in the endophytic beta-Proteobacterium Herbaspirillum seropedicae has not been characterized. We have generated mutants in two nif-associated genes encoding putative ferredoxins, fdxA and fdxN. The fdxA gene is part of the operon nifHDKENXorf1orf2fdxAnifQmodABC and is transcribed from the nifH promoter, as revealed by lacZ gene fusion. The fdxN gene is probably cotranscribed with the nifB gene. Mutational analysis suggests that the FdxA protein is essential for maximum nitrogenase activity, since the nitrogenase activity of the fdxA mutant strain was reduced to about 30% of that of the wild-type strain. In addition, the fdxA mutation had no effect on the nitrogenase switch-off in response to ammonium. Nitrogenase activity of a mutant strain lacking the fdxN gene was completely abolished. This phenotype was reverted by complementation with fdxN expressed under lacZ promoter control. The results suggest that the products of both the fdxA and fdxN genes are probably involved in electron transfer during nitrogen fixation.The pathway of electron transport to nitrogenase in the endophytic beta-Proteobacterium Herbaspirillum seropedicae has not been characterized. We have generated mutants in two nif-associated genes encoding putative ferredoxins, fdxA and fdxN. The fdxA gene is part of the operon nifHDKENXorf1orf2fdxAnifQmodABC and is transcribed from the nifH promoter, as revealed by lacZ gene fusion. The fdxN gene is probably cotranscribed with the nifB gene. Mutational analysis suggests that the FdxA protein is essential for maximum nitrogenase activity, since the nitrogenase activity of the fdxA mutant strain was reduced to about 30% of that of the wild-type strain. In addition, the fdxA mutation had no effect on the nitrogenase switch-off in response to ammonium. Nitrogenase activity of a mutant strain lacking the fdxN gene was completely abolished. This phenotype was reverted by complementation with fdxN expressed under lacZ promoter control. The results suggest that the products of both the fdxA and fdxN genes are probably involved in electron transfer during nitrogen fixation.
Author	Monteiro, Rose A., Universidade Federal do Parana, CP, Brazil Souza, Andre L.F., Universidade Federal do Parana, CP, Brazil Invitti, Adriana L., Universidade Federal do Parana, CP, Brazil Souza, Emanuel M., Universidade Federal do Parana, CP, Brazil Klassen, Giseli, Universidade Federal do Parana, CP, Brazil Pedrosa, Fabio O., Universidade Federal do Parana, CP, Brazil Rego, Fabiane G.M., Universidade Federal do Parana, CP, Brazil Chubatsu, Leda S., Universidade Federal do Parana, CP, Brazil Rigo, Liu U., Universidade Federal do Parana, CP, Brazil
Author_xml	– sequence: 1 fullname: Souza, Andre L.F., Universidade Federal do Parana, CP, Brazil – sequence: 2 fullname: Invitti, Adriana L., Universidade Federal do Parana, CP, Brazil – sequence: 3 fullname: Rego, Fabiane G.M., Universidade Federal do Parana, CP, Brazil – sequence: 4 fullname: Monteiro, Rose A., Universidade Federal do Parana, CP, Brazil – sequence: 5 fullname: Klassen, Giseli, Universidade Federal do Parana, CP, Brazil – sequence: 6 fullname: Souza, Emanuel M., Universidade Federal do Parana, CP, Brazil – sequence: 7 fullname: Chubatsu, Leda S., Universidade Federal do Parana, CP, Brazil – sequence: 8 fullname: Pedrosa, Fabio O., Universidade Federal do Parana, CP, Brazil – sequence: 9 fullname: Rigo, Liu U., Universidade Federal do Parana, CP, Brazil
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/20221733$$D View this record in MEDLINE/PubMed https://www.kci.go.kr/kciportal/ci/sereArticleSearch/ciSereArtiView.kci?sereArticleSearchBean.artiId=ART001425543$$DAccess content in National Research Foundation of Korea (NRF)
BookMark	eNp9kctuEzEUhi1URC_wACxAFhvYDPiW8cwyqkgbERWpCmvL4zkObiZ2sGeqROLh8XQKSF10YZ8j6_vPxf85OvHBA0JvKflMCZFfEmVMzgpC6nykLI4v0BmtZVlwWYuTnDM2K6pK8lN0ntIdISXlgr1Cp4wwRiXnZ-j3-ifgpb8P3T3swPc4WNznJ-9sMU8pGKd7aPECYoQ2HJwvVm4L-Ao8JGzbwxxr347Jzai8htjotHfRdd2wwwli2EPrjAbsPL5xfQwb8HjhDrp3wb9GL63uErx5jBfox-Lr-vK6WH2_Wl7OV4URbNYXlFVNI2swrajKllmwJSvBMl1KyRstDLFMCoC8kLCC14aXQCTlbcO1pJXgF-jTVNdHq7bGqaDdQ9wEtY1qfrteqorKGWcZ_Tih-xh-DZB6tXPJQNdpD2FIauwhWSVoJj88Ie_CEH3eQzFWE5GnJhl6_wgNzQ5atY9up-NR_TUgA3QCTAwpRbD_EErUaLKaTFbZZDWarI5ZI59ojOsfPrSP2nXPKtmkTLmL30D8P_NzoneTyOqg9Ca6pL7dMkIzzvPN_wCfAMOR
CitedBy_id	crossref_primary_10_1128_JB_00757_17 crossref_primary_10_1007_s00203_011_0732_7 crossref_primary_10_1038_s41598_019_45866_w crossref_primary_10_1016_j_syapm_2022_126377 crossref_primary_10_3389_fmicb_2019_01457 crossref_primary_10_1007_s11104_011_0819_6
Cites_doi	10.1016/0378-1119(89)90522-2 10.1128/JB.183.12.3752-3760.2001 10.1111/j.1574-6968.1988.tb02741.x 10.1007/s00438-002-0715-0 10.1038/nbt923 10.1016/0014-5793(72)80410-1 10.1073/pnas.58.1.213 10.1128/JB.183.4.1405-1412.2001 10.1111/j.1574-6968.2006.00297.x 10.1139/m97-129 10.1007/s00438-007-0246-9 10.1073/pnas.87.12.4645 10.1093/nar/gkl825 10.1111/j.1365-2958.1989.tb01803.x 10.1016/j.femsle.2005.03.024 10.1111/j.1574-6968.1999.tb08840.x 10.1128/AEM.67.5.2375-2379.2001 10.1016/S0168-1656(01)00343-1 10.1111/j.1462-2920.2007.01240.x 10.1007/s00203-005-0066-4 10.1099/00207713-36-1-86 10.1016/0003-2697(76)90527-3 10.1038/nbt1183-784 10.1007/BF00017984 10.1128/JB.184.8.2251-2259.2002 10.1139/W06-085 10.1042/bj2390069 10.1016/0005-2728(95)00106-X 10.1128/jb.171.5.2591-2598.1989 10.1590/S0100-879X2001001100003 10.1016/S0021-9258(17)44340-7 10.1139/w06-085 10.1128/JB.181.2.681-684.1999 10.1128/jb.170.4.1999-2001.1988 10.1128/jb.179.10.3304-3309.1997 10.1016/0304-4165(66)90383-7 10.1042/bj2310743
ContentType	Journal Article
Copyright	The Microbiological Society of Korea and Springer-Verlag Berlin Heidelberg 2010
Copyright_xml	– notice: The Microbiological Society of Korea and Springer-Verlag Berlin Heidelberg 2010
DBID	FBQ AAYXX CITATION CGR CUY CVF ECM EIF NPM 3V. 7QL 7T7 7TM 7TN 7U9 7X7 7XB 88A 88E 8AO 8FD 8FE 8FH 8FI 8FJ 8FK ABUWG AEUYN AFKRA AZQEC BBNVY BENPR BHPHI BKSAR C1K CCPQU DWQXO F1W FR3 FYUFA GHDGH GNUQQ H94 H95 HCIFZ K9. L.G LK8 M0S M1P M7N M7P P64 PCBAR PHGZM PHGZT PJZUB PKEHL PPXIY PQEST PQGLB PQQKQ PQUKI PRINS 7X8 ACYCR
DOI	10.1007/s12275-009-0077-y
DatabaseName	AGRIS CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed ProQuest Central (Corporate) Bacteriology Abstracts (Microbiology B) Industrial and Applied Microbiology Abstracts (Microbiology A) Nucleic Acids Abstracts Oceanic Abstracts Virology and AIDS Abstracts Health & Medical Collection (Proquest) ProQuest Central (purchase pre-March 2016) Biology Database (Alumni Edition) Medical Database (Alumni Edition) ProQuest Pharma Collection Technology Research Database ProQuest SciTech Collection ProQuest Natural Science Collection ProQuest Hospital Collection Hospital Premium Collection (Alumni Edition) ProQuest Central (Alumni) (purchase pre-March 2016) ProQuest Central (Alumni) ProQuest One Sustainability (subscription) ProQuest Central UK/Ireland ProQuest Central Essentials Biological Science Collection ProQuest Central Natural Science Collection Earth, Atmospheric & Aquatic Science Collection Environmental Sciences and Pollution Management ProQuest One Community College ProQuest Central ASFA: Aquatic Sciences and Fisheries Abstracts Engineering Research Database Health Research Premium Collection Health Research Premium Collection (Alumni) ProQuest Central Student AIDS and Cancer Research Abstracts Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources SciTech Premium Collection ProQuest Health & Medical Complete (Alumni) Aquatic Science & Fisheries Abstracts (ASFA) Professional Biological Sciences ProQuest Health & Medical Collection Medical Database Algology Mycology and Protozoology Abstracts (Microbiology C) Biological Science Database Biotechnology and BioEngineering Abstracts Earth, Atmospheric & Aquatic Science Database ProQuest Central Premium ProQuest One Academic (New) ProQuest Health & Medical Research Collection ProQuest One Academic Middle East (New) ProQuest One Health & Nursing ProQuest One Academic Eastern Edition (DO NOT USE) One Applied & Life Sciences ProQuest One Academic (retired) ProQuest One Academic UKI Edition ProQuest Central China MEDLINE - Academic Korean Citation Index
DatabaseTitle	CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) ProQuest Central Student ProQuest Central Essentials Nucleic Acids Abstracts SciTech Premium Collection ProQuest Central China Environmental Sciences and Pollution Management ProQuest One Applied & Life Sciences ProQuest One Sustainability Health Research Premium Collection Natural Science Collection Health & Medical Research Collection Biological Science Collection Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources Industrial and Applied Microbiology Abstracts (Microbiology A) ProQuest Central (New) ProQuest Medical Library (Alumni) Virology and AIDS Abstracts ProQuest Biological Science Collection ProQuest One Academic Eastern Edition Earth, Atmospheric & Aquatic Science Database ProQuest Hospital Collection Health Research Premium Collection (Alumni) Biological Science Database ProQuest Hospital Collection (Alumni) Biotechnology and BioEngineering Abstracts ProQuest Health & Medical Complete ProQuest One Academic UKI Edition Engineering Research Database ProQuest One Academic ProQuest One Academic (New) Aquatic Science & Fisheries Abstracts (ASFA) Professional Technology Research Database ProQuest One Academic Middle East (New) ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) ProQuest One Community College ProQuest One Health & Nursing ProQuest Natural Science Collection ProQuest Pharma Collection ProQuest Biology Journals (Alumni Edition) ProQuest Central Earth, Atmospheric & Aquatic Science Collection ProQuest Health & Medical Research Collection Oceanic Abstracts Health and Medicine Complete (Alumni Edition) ProQuest Central Korea Bacteriology Abstracts (Microbiology B) Algology Mycology and Protozoology Abstracts (Microbiology C) AIDS and Cancer Research Abstracts ProQuest SciTech Collection ProQuest Medical Library ASFA: Aquatic Sciences and Fisheries Abstracts ProQuest Central (Alumni) MEDLINE - Academic
DatabaseTitleList	ProQuest Central Student MEDLINE MEDLINE - Academic
Database_xml	– sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: BENPR name: ProQuest Central url: https://www.proquest.com/central sourceTypes: Aggregation Database
DeliveryMethod	fulltext_linktorsrc
Discipline	Biology
EISSN	1976-3794
EndPage	83
ExternalDocumentID	oai_kci_go_kr_ARTI_817532 1981512591 20221733 10_1007_s12275_009_0077_y KR2011003011
Genre	Research Support, Non-U.S. Gov't Journal Article
GeographicLocations	Brazil
GeographicLocations_xml	– name: Brazil
GroupedDBID	--- -Y2 .86 .VR 06C 06D 0R~ 0VY 123 1N0 203 29L 29~ 2J2 2JN 2JY 2KG 2KM 2LR 2VQ 2~H 30V 4.4 406 408 40D 40E 53G 5VS 67N 6NX 7X7 88E 8AO 8CJ 8FE 8FH 8FI 8FJ 8TC 8UJ 95- 95. 95~ 96X 9ZL A8Z AAAVM AABHQ AACDK AAHBH AAHNG AAIAL AAJBT AAJKR AANXM AANZL AAPKM AARHV AARTL AATNV AATVU AAUYE AAWCG AAYIU AAYQN AAYTO AAYZH ABDZT ABECU ABFTV ABHLI ABHQN ABJNI ABJOX ABKCH ABMNI ABMQK ABNWP ABPLI ABQBU ABSXP ABTEG ABTHY ABTKH ABTMW ABUWG ABWNU ABXPI ACGFS ACHSB ACHXU ACKNC ACMDZ ACMLO ACOKC ACOMO ACPIV ACPRK ACSNA ACZOJ ADBBV ADHHG ADHIR ADKNI ADKPE ADRFC ADTPH ADURQ ADYFF ADZKW AEBTG AEGAL AEGNC AEJHL AEJRE AEKMD AEMSY AENEX AEOHA AEPYU AESKC AETLH AEUYN AEVLU AEXYK AFBBN AFGCZ AFKRA AFLOW AFQWF AFRAH AFWTZ AFZKB AGAYW AGDGC AGJBK AGMZJ AGQEE AGQMX AGRTI AGWIL AGWZB AGYKE AHAVH AHBYD AHKAY AHMBA AHPBZ AHSBF AHYZX AIAKS AIIXL AILAN AITGF AJBLW AJRNO AKMHD ALIPV ALMA_UNASSIGNED_HOLDINGS ALWAN AMKLP AMXSW AMYLF AMYQR AOCGG ARMRJ ASPBG AVWKF AXYYD AZFZN B-. BA0 BAWUL BBNVY BDATZ BENPR BGNMA BHPHI BKSAR BPHCQ BSONS BVXVI CAG CCPQU COF CS3 CSCUP D1J DBRKI DDRTE DNIVK DPUIP DU5 EBD EBLON EBS EIOEI EJD EMOBN ESBYG F5P FBQ FEDTE FERAY FFXSO FIGPU FINBP FNLPD FRRFC FSGXE FWDCC FYUFA G-Y G-Z GGCAI GGRSB GJIRD GNWQR GQ7 GW5 H13 HCIFZ HF~ HG6 HLICF HMCUK HMJXF HRMNR HVGLF HZ~ IJ- IKXTQ IWAJR IXC IXD I~X I~Z J-C J0Z JBSCW JZLTJ KOV KQ8 KVFHK LK8 LLZTM M1P M4Y M7P MA- MM. N9A NPVJJ NQJWS NU0 O9- O9J OK1 P2P PCBAR PF0 PHGZT PQQKQ PROAC PSQYO PT4 Q2X QOR QOS R89 R9I ROL RPX RSV S16 S1Z S27 S3A S3B SAP SBL SDH SHX SISQX SJN SJYHP SNE SNPRN SNX SOHCF SOJ SPISZ SRMVM SSLCW SSXJD STPWE SV3 SZN T13 TDB TSG TUC TUS U2A U9L UG4 UKHRP UOJIU UTJUX UZXMN VC2 VFIZW W48 WK8 YLTOR Z45 ZMTXR ZOVNA ~A9 -56 -5G -BR -EM -~C .UV 3V. 88A AASML ABAKF ACAOD ADINQ AEFQL AIGIU GQ6 M0L Z7U Z7W AAYXX ABFSG ACSTC AEZWR AFFHD AFHIU AFOHR AHWEU AIXLP ATHPR CITATION PHGZM PJZUB PPXIY PQGLB CGR CUY CVF ECM EIF NPM 7QL 7T7 7TM 7TN 7U9 7XB 8FD 8FK AZQEC C1K DWQXO F1W FR3 GNUQQ H94 H95 K9. L.G M7N P64 PKEHL PQEST PQUKI PRINS 7X8 ACYCR
ID	FETCH-LOGICAL-c425t-128bb79ecd486d2fef626ef2a6773ba4c0f274ee7334f439c36e0713db3a71843
IEDL.DBID	M7P
ISICitedReferencesCount	9
ISICitedReferencesURI	http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000275135800012&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN	1225-8873 1976-3794
IngestDate	Sun Mar 09 07:52:30 EDT 2025 Sun Nov 09 10:57:43 EST 2025 Sun Oct 26 04:42:03 EDT 2025 Wed Feb 19 01:51:49 EST 2025 Sat Nov 29 02:14:06 EST 2025 Tue Nov 18 22:18:34 EST 2025 Fri Feb 21 02:35:16 EST 2025 Thu Apr 03 09:44:05 EDT 2025
IsPeerReviewed	true
IsScholarly	true
Issue	1
Keywords	ferredoxin nitrogenase
Language	English
License	http://www.springer.com/tdm
LinkModel	DirectLink
MergedId	FETCHMERGED-LOGICAL-c425t-128bb79ecd486d2fef626ef2a6773ba4c0f274ee7334f439c36e0713db3a71843
Notes	A50 2011003011 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 G704-000121.2010.48.1.007
PMID	20221733
PQID	229041280
PQPubID	54654
PageCount	7
ParticipantIDs	nrf_kci_oai_kci_go_kr_ARTI_817532 proquest_miscellaneous_733472841 proquest_journals_229041280 pubmed_primary_20221733 crossref_primary_10_1007_s12275_009_0077_y crossref_citationtrail_10_1007_s12275_009_0077_y springer_journals_10_1007_s12275_009_0077_y fao_agris_KR2011003011
PublicationCentury	2000
PublicationDate	2010-02-01
PublicationDateYYYYMMDD	2010-02-01
PublicationDate_xml	– month: 02 year: 2010 text: 2010-02-01 day: 01
PublicationDecade	2010
PublicationPlace	Heidelberg
PublicationPlace_xml	– name: Heidelberg – name: Korea (South) – name: Seoul
PublicationTitle	The journal of microbiology
PublicationTitleAbbrev	J Microbiol
PublicationTitleAlternate	J Microbiol
PublicationYear	2010
Publisher	The Microbiological Society of Korea Springer Nature B.V 한국미생물학회
Publisher_xml	– name: The Microbiological Society of Korea – name: Springer Nature B.V – name: 한국미생물학회
References	Schollhorn, Burris (CR33) 1967; 58 Edgren, Nordlund (CR11) 2005; 245 Noindorf, Rego, Baura, Monteiro, Wassem, Cruz, Rigo, Souza, Steffens, Pedrosa, Chubatsu (CR28) 2006; 185 Spaink, Okker, Wijffelman, Pees, Lugtenberg (CR37) 1987; 9 Deistung, Cannon, Cannon, Hill, Thorneley (CR6) 1985; 231 Young, Stacey, Burris, Evans (CR40) 1992 Armengaud, Meyer, Jouanneau (CR1) 1997; 179 Menard, Monnez, Estrada de Los Santos, Segonds, Caballero-Mellado, Lipuma, Chabanon, Cournoyer (CR25) 2007; 9 Cruz, Souza, Weber, Baldani, Dobereiner, Pedrosa (CR5) 2001; 67 Ebeling, Noti, Hennecke (CR10) 1988; 170 Miller (CR26) 1992 Sambrook, Fritsch, Maniatis (CR32) 1989 Potrich, Bressel, Schrank, Passaglia (CR30) 2001; 34 Egener, Martin, Sarkar, Reinhold-Hurek (CR13) 2001; 183 Rego, Pedrosa, Chubatsu, Yates, Wassem, Steffens, Rigo, Souza (CR31) 2006; 52 Shah, Stacey, Brill (CR34) 1983; 258 Gubler, Zürcher, Hennecke (CR16) 1989; 3 Edgren, Nordlund (CR12) 2006; 260 Simon, Priefer, Puhler (CR35) 1983; 1 Baldani, Baldani, Seldin, Dobereiner (CR2) 1986; 36 Deistung, Thorneley (CR7) 1986; 239 Hauser, Pessi, Friberg, Weber, Rusca, Lindemann, Fischer, Hennecke (CR17) 2007; 278 Gottfert, Rothlisberger, Kundig, Beck, Marty, Hennecke (CR14) 2001; 183 Dilworth (CR8) 1966; 127 Martin, Reinhold-Hurek (CR24) 2002; 184 Klassen, Pedrosa, Souza, Funayama, Rigo (CR19) 1997; 43 von Mering, Jensen, Kuhn, Chaffron, Doerks, Krüger, Snel, Bork (CR38) 2007; 35 Grant, Jessee, Bloom, Hanahan (CR15) 1990; 87 Pedrosa, Benelli, Yates, Wassem, Monteiro, Klassen, Steffens, Souza, Chubatsu, Rigo (CR29) 2001; 91 Machado, Yates, Machado, Souza, Pedrosa (CR23) 1996; 29 Dombrecht, Tesfay, Verreth, Heusdens, Nápoles, Vanderleyden, Michiels (CR9) 2002; 267 Bruschi, Guerlesquin (CR4) 1988; 54 Klassen, Pedrosa, Souza, Yates, Rigo (CR20) 1999; 181 Jouanneau, Meyer, Naud, Klipp (CR18) 1995; 1232 Bradford (CR3) 1976; 72 Kokotek, Lotz (CR21) 1989; 84 Yates (CR39) 1972; 27 Larimer, Chain, Hauser, Lamerdin, Malfatti, Do, Land, Pelletier, Beatty, Lang, Tabita, Gibson, Hanson, Bobst, Torres, Peres, Harrison, Gibson, Harwood (CR22) 2004; 22 Souza, Pedrosa, Drummond, Rigo, Yates (CR36) 1999; 181 Moreno-Vivian, Hennecke, Puhler, Klipp (CR27) 1989; 171 M. Bruschi (77_CR4) 1988; 54 H.P. Spaink (77_CR37) 1987; 9 F.G. Rego (77_CR31) 2006; 52 J. Deistung (77_CR7) 1986; 239 E.M. Souza (77_CR36) 1999; 181 R. Simon (77_CR35) 1983; 1 I.J. Baldani (77_CR2) 1986; 36 M. Gubler (77_CR16) 1989; 3 L.M. Cruz (77_CR5) 2001; 67 L. Noindorf (77_CR28) 2006; 185 M.J. Dilworth (77_CR8) 1966; 127 C. Mering von (77_CR38) 2007; 35 F.W. Larimer (77_CR22) 2004; 22 M.M. Bradford (77_CR3) 1976; 72 D.P. Potrich (77_CR30) 2001; 34 T. Edgren (77_CR12) 2006; 260 C. Moreno-Vivian (77_CR27) 1989; 171 F.O. Pedrosa (77_CR29) 2001; 91 J. Deistung (77_CR6) 1985; 231 J. Armengaud (77_CR1) 1997; 179 A. Menard (77_CR25) 2007; 9 G. Klassen (77_CR19) 1997; 43 S. Grant (77_CR15) 1990; 87 Y. Jouanneau (77_CR18) 1995; 1232 R. Schollhorn (77_CR33) 1967; 58 M. Gottfert (77_CR14) 2001; 183 G. Klassen (77_CR20) 1999; 181 T. Egener (77_CR13) 2001; 183 J.P.W. Young (77_CR40) 1992 B. Dombrecht (77_CR9) 2002; 267 I.M.P. Machado (77_CR23) 1996; 29 F. Hauser (77_CR17) 2007; 278 D.E. Martin (77_CR24) 2002; 184 W. Kokotek (77_CR21) 1989; 84 V.K. Shah (77_CR34) 1983; 258 M.G. Yates (77_CR39) 1972; 27 T. Edgren (77_CR11) 2005; 245 S. Ebeling (77_CR10) 1988; 170 J.H. Miller (77_CR26) 1992 J. Sambrook (77_CR32) 1989 9222418 - Braz J Med Biol Res. 1996 Dec;29(12):1599-602 5231601 - Proc Natl Acad Sci U S A. 1967 Jul;58(1):213-6 24276795 - Plant Mol Biol. 1987 Jan;9(1):27-39 11914357 - J Bacteriol. 2002 Apr;184(8):2251-9 11157954 - J Bacteriol. 2001 Feb;183(4):1405-12 11566390 - J Biotechnol. 2001 Oct 4;91(2-3):189-95 10564803 - FEMS Microbiol Lett. 1999 Dec 1;181(1):165-70 2503674 - Mol Microbiol. 1989 Feb;3(2):141-8 3907625 - Biochem J. 1985 Nov 1;231(3):743-53 2708314 - J Bacteriol. 1989 May;171(5):2591-8 12207230 - Mol Genet Genomics. 2002 Aug;267(6):820-8 11668346 - Braz J Med Biol Res. 2001 Nov;34(11):1379-95 3078742 - FEMS Microbiol Rev. 1988 Apr-Jun;4(2):155-75 6352705 - J Biol Chem. 1983 Oct 10;258(19):12064-8 942051 - Anal Biochem. 1976 May 7;72:248-54 2515118 - Gene. 1989 Dec 14;84(2):467-71 11946808 - FEBS Lett. 1972 Oct 15;27(1):63-67 7495836 - Biochim Biophys Acta. 1995 Nov 21;1232(1-2):33-42 16790015 - FEMS Microbiol Lett. 2006 Jul;260(1):30-5 3541922 - Biochem J. 1986 Oct 1;239(1):69-75 17472633 - Environ Microbiol. 2007 May;9(5):1176-85 17098935 - Nucleic Acids Res. 2007 Jan;35(Database issue):D358-62 17569992 - Mol Genet Genomics. 2007 Sep;278(3):255-71 11371540 - J Bacteriol. 2001 Jun;183(12):3752-60 9882688 - J Bacteriol. 1999 Jan;181(2):681-4 14704707 - Nat Biotechnol. 2004 Jan;22(1):55-61 11319127 - Appl Environ Microbiol. 2001 May;67(5):2375-9 9150228 - J Bacteriol. 1997 May;179(10):3304-9 17473889 - Can J Microbiol. 2006 Dec;52(12):1199-207 5964974 - Biochim Biophys Acta. 1966 Oct 31;127(2):285-94 2162051 - Proc Natl Acad Sci U S A. 1990 Jun;87(12):4645-9 16331441 - Arch Microbiol. 2006 Mar;185(1):55-62 15837392 - FEMS Microbiol Lett. 2005 Apr 15;245(2):345-51 3350797 - J Bacteriol. 1988 Apr;170(4):1999-2001
References_xml	– volume: 84 start-page: 467 year: 1989 end-page: 471 ident: CR21 article-title: Construction of a -kanamycinresistance cassette, useful for site-directed mutagenesis and as a promoter probe publication-title: Gene doi: 10.1016/0378-1119(89)90522-2 – volume: 29 start-page: 1599 year: 1996 end-page: 1602 ident: CR23 article-title: Cloning and sequencing of the nitrogenase structural genes of publication-title: Braz. J. Med. Biol. Res. – start-page: 456 year: 1992 ident: CR26 publication-title: A short course in bacterial genetics: a laboratory manual and handbook for and related bacteria – volume: 1232 start-page: 33 issue: 1–2 year: 1995 end-page: 42 ident: CR18 article-title: Characterization of an mutant of indicates that ferredoxin I serves as electron donor to nitrogenase publication-title: Biochim. Biophys. Acta. – volume: 183 start-page: 3752 year: 2001 end-page: 3760 ident: CR13 article-title: Role of a ferredoxin gene cotranscribed with the operon in N fixation and nitrogenase “switch-off” of sp. strain BH72 publication-title: J. Bacteriol. doi: 10.1128/JB.183.12.3752-3760.2001 – volume: 54 start-page: 155 year: 1988 end-page: 176 ident: CR4 article-title: Structure, function and evolution of bacterial ferredoxins publication-title: FEMS Microbiol. Rev. doi: 10.1111/j.1574-6968.1988.tb02741.x – start-page: 43 year: 1992 end-page: 86 ident: CR40 article-title: Phylogenetic classification of nitrogen-fixing organisms publication-title: Biological Nitrogen Fixation – volume: 267 start-page: 820 year: 2002 end-page: 828 ident: CR9 article-title: The gene is highly expressed in bacteroids and required for nitrogen fixation publication-title: Mol. Genet. Genomics doi: 10.1007/s00438-002-0715-0 – volume: 22 start-page: 55 year: 2004 end-page: 61 ident: CR22 article-title: Complete genome sequence of the metabolically versatile photosynthetic bacterium publication-title: Nat. Biotechnol. doi: 10.1038/nbt923 – volume: 181 start-page: 681 year: 1999 end-page: 684 ident: CR36 article-title: Control of NifA activity by ammonium ions and oxygen publication-title: J. Bacteriol. – volume: 27 start-page: 63 year: 1972 end-page: 67 ident: CR39 article-title: Electron transport to nitrogenase in : flavodoxin hydroquinone as an electron donor publication-title: FEBS Lett. doi: 10.1016/0014-5793(72)80410-1 – volume: 127 start-page: 285 year: 1966 end-page: 294 ident: CR8 article-title: Acetylene reduction by nitrogen-fixing preparations from publication-title: Bioch. Biophys. Acta. – volume: 58 start-page: 213 year: 1967 end-page: 216 ident: CR33 article-title: Acetylene as a competitive inhibitor of N fixation publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.58.1.213 – volume: 258 start-page: 12064 year: 1983 end-page: 12068 ident: CR34 article-title: Electron transport to nitrogenase. Purification and characterization of pyruvate: flavodoxin oxidoreductase. The gene product publication-title: J. Biol. Chem. – volume: 183 start-page: 1405 year: 2001 end-page: 1412 ident: CR14 article-title: Potential symbiosis-specific genes uncovered by sequencing a 410-kilobase DNA region of the chromosome publication-title: J. Bacteriol. doi: 10.1128/JB.183.4.1405-1412.2001 – volume: 260 start-page: 30 year: 2006 end-page: 35 ident: CR12 article-title: Two pathways of electron transport to nitrogenase in : the major pathway is dependent on the gene products publication-title: FEMS Microbiol. Lett. doi: 10.1111/j.1574-6968.2006.00297.x – volume: 43 start-page: 887 year: 1997 end-page: 891 ident: CR19 article-title: Effect of nitrogen compounds on nitrogenase activity in SMR1 publication-title: Can. J. Microbiol. doi: 10.1139/m97-129 – volume: 278 start-page: 255 year: 2007 end-page: 271 ident: CR17 article-title: Dissection of the NifA+sigma(54) regulon, and identification of a ferredoxin gene ( ) for symbiotic nitrogen fixation publication-title: Mol. Genet. Genomics doi: 10.1007/s00438-007-0246-9 – volume: 231 start-page: 743 year: 1985 end-page: 753 ident: CR6 article-title: Electron transfer to nitrogenase in publication-title: Biochem. J. – volume: 87 start-page: 4645 year: 1990 end-page: 4649 ident: CR15 article-title: Differential plasmid rescue from transgenic mouse DNAs into methylation-restriction mutants publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.87.12.4645 – volume: 35 start-page: 358 year: 2007 end-page: 362 ident: CR38 article-title: STRING 7—recent developments in the integration and prediction of protein interactions publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkl825 – volume: 3 start-page: 141 year: 1989 end-page: 148 ident: CR16 article-title: The operon: identification of and of a 5′ mRNA region affecting the level of the transcript publication-title: Mol. Microbiol. doi: 10.1111/j.1365-2958.1989.tb01803.x – year: 1989 ident: CR32 publication-title: Molecular cloning a laboratory manual – volume: 245 start-page: 345 year: 2005 end-page: 351 ident: CR11 article-title: Electron transport to nitrogenase in : identification of a new gene encoding the primary electron donor to nitrogenase publication-title: FEMS Microbiol. Lett. doi: 10.1016/j.femsle.2005.03.024 – volume: 170 start-page: 1999 year: 1988 end-page: 2001 ident: CR10 article-title: Identification of a new gene ( ) encoding a ferredoxin-like protein publication-title: J. Bacteriol. – volume: 181 start-page: 165 year: 1999 end-page: 170 ident: CR20 article-title: Sequencing and functional analysis of the gene cluster of publication-title: FEMS Microbiol. Lett. doi: 10.1111/j.1574-6968.1999.tb08840.x – volume: 67 start-page: 2375 year: 2001 end-page: 2379 ident: CR5 article-title: 16S Ribosomal DNA characterization of nitrogen-fixing bacteria isolated from Banana ( spp.) and Pineapple ( (L) Merril) publication-title: Appl. Environ. Microbiol. doi: 10.1128/AEM.67.5.2375-2379.2001 – volume: 91 start-page: 189 year: 2001 end-page: 195 ident: CR29 article-title: Recent developments in the structural organization and regulation of nitrogen fixation genes in publication-title: J. Biotechnol. doi: 10.1016/S0168-1656(01)00343-1 – volume: 239 start-page: 69 year: 1986 end-page: 75 ident: CR7 article-title: Electron transfer to nitrogenase. Characterization of flavodoxin from and comparison of its redox potentials with those of flavodoxins from and ( -gene product) publication-title: Biochem. J. – volume: 9 start-page: 1176 year: 2007 end-page: 1185 ident: CR25 article-title: Selection of nitrogen-fixing deficient strains by cystic fibrosis patients: involvement of gene deletions and auxotrophic mutations publication-title: Environ. Microbiol. doi: 10.1111/j.1462-2920.2007.01240.x – volume: 185 start-page: 55 year: 2006 end-page: 62 ident: CR28 article-title: Characterization of the operon of publication-title: Arch. Microbiol. doi: 10.1007/s00203-005-0066-4 – volume: 36 start-page: 86 year: 1986 end-page: 93 ident: CR2 article-title: Characterization of gen. nov., sp. nov., a root-associated nitrogen-fixing bacterium publication-title: Int. J. Syst. Bacteriol. doi: 10.1099/00207713-36-1-86 – volume: 72 start-page: 248 year: 1976 end-page: 254 ident: CR3 article-title: A rapid and sensitive method for the quantification of microgram quantities of protein utilization: the principle of protein-dye binding publication-title: Anal. Biochem. doi: 10.1016/0003-2697(76)90527-3 – volume: 1 start-page: 784 year: 1983 end-page: 791 ident: CR35 article-title: A broad host range mobilization system for genetic engineering: transposon mutagenesis in Gram-negative bacteria publication-title: BioTechnology doi: 10.1038/nbt1183-784 – volume: 9 start-page: 27 year: 1987 end-page: 39 ident: CR37 article-title: Promoters in the nodulation region of Sym plasmid pRL1JI publication-title: Plant Mol. Biol. doi: 10.1007/BF00017984 – volume: 184 start-page: 2251 year: 2002 end-page: 2259 ident: CR24 article-title: Distinct roles of PII-like signal transmitter proteins and in regulation of gene expression, nitrogenase activity, and posttranslational modification of NifH in sp. strain BH72 publication-title: J. Bacteriol. doi: 10.1128/JB.184.8.2251-2259.2002 – volume: 171 start-page: 2591 year: 1989 end-page: 2598 ident: CR27 article-title: Open reading frame 5 (ORF5), encoding a ferredoxinlike protein, and are cotranscribed with , and in publication-title: J. Bacteriol. – volume: 52 start-page: 1199 year: 2006 end-page: 1207 ident: CR31 article-title: The expression of gene from is dependent upon the NifA and RpoN proteins publication-title: Can J. Microbiol. doi: 10.1139/W06-085 – volume: 179 start-page: 3304 year: 1997 end-page: 3309 ident: CR1 article-title: A [2Fe-2S] ferredoxin (FdVI) is essential for growth of the photosynthetic bacterium publication-title: J. Bacteriol. – volume: 34 start-page: 1379 year: 2001 end-page: 1395 ident: CR30 article-title: Sequencing and promoter analysis of the operon from Sp7 publication-title: Braz. J. Med. Biol. Res. – volume: 87 start-page: 4645 year: 1990 ident: 77_CR15 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.87.12.4645 – volume: 267 start-page: 820 year: 2002 ident: 77_CR9 publication-title: Mol. Genet. Genomics doi: 10.1007/s00438-002-0715-0 – volume: 185 start-page: 55 year: 2006 ident: 77_CR28 publication-title: Arch. Microbiol. doi: 10.1007/s00203-005-0066-4 – volume: 54 start-page: 155 year: 1988 ident: 77_CR4 publication-title: FEMS Microbiol. Rev. doi: 10.1111/j.1574-6968.1988.tb02741.x – volume: 278 start-page: 255 year: 2007 ident: 77_CR17 publication-title: Mol. Genet. Genomics doi: 10.1007/s00438-007-0246-9 – volume: 239 start-page: 69 year: 1986 ident: 77_CR7 publication-title: Biochem. J. doi: 10.1042/bj2390069 – volume: 1 start-page: 784 year: 1983 ident: 77_CR35 publication-title: BioTechnology doi: 10.1038/nbt1183-784 – volume: 43 start-page: 887 year: 1997 ident: 77_CR19 publication-title: Can. J. Microbiol. doi: 10.1139/m97-129 – volume: 1232 start-page: 33 issue: 1–2 year: 1995 ident: 77_CR18 publication-title: Biochim. Biophys. Acta. doi: 10.1016/0005-2728(95)00106-X – volume: 171 start-page: 2591 year: 1989 ident: 77_CR27 publication-title: J. Bacteriol. doi: 10.1128/jb.171.5.2591-2598.1989 – volume: 91 start-page: 189 year: 2001 ident: 77_CR29 publication-title: J. Biotechnol. doi: 10.1016/S0168-1656(01)00343-1 – volume: 36 start-page: 86 year: 1986 ident: 77_CR2 publication-title: Int. J. Syst. Bacteriol. doi: 10.1099/00207713-36-1-86 – volume: 184 start-page: 2251 year: 2002 ident: 77_CR24 publication-title: J. Bacteriol. doi: 10.1128/JB.184.8.2251-2259.2002 – volume-title: Molecular cloning a laboratory manual year: 1989 ident: 77_CR32 – volume: 67 start-page: 2375 year: 2001 ident: 77_CR5 publication-title: Appl. Environ. Microbiol. doi: 10.1128/AEM.67.5.2375-2379.2001 – volume: 3 start-page: 141 year: 1989 ident: 77_CR16 publication-title: Mol. Microbiol. doi: 10.1111/j.1365-2958.1989.tb01803.x – start-page: 456 volume-title: A short course in bacterial genetics: a laboratory manual and handbook for Escherichia coli and related bacteria year: 1992 ident: 77_CR26 – volume: 34 start-page: 1379 year: 2001 ident: 77_CR30 publication-title: Braz. J. Med. Biol. Res. doi: 10.1590/S0100-879X2001001100003 – start-page: 43 volume-title: Biological Nitrogen Fixation year: 1992 ident: 77_CR40 – volume: 258 start-page: 12064 year: 1983 ident: 77_CR34 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)44340-7 – volume: 52 start-page: 1199 year: 2006 ident: 77_CR31 publication-title: Can J. Microbiol. doi: 10.1139/w06-085 – volume: 35 start-page: 358 year: 2007 ident: 77_CR38 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkl825 – volume: 245 start-page: 345 year: 2005 ident: 77_CR11 publication-title: FEMS Microbiol. Lett. doi: 10.1016/j.femsle.2005.03.024 – volume: 22 start-page: 55 year: 2004 ident: 77_CR22 publication-title: Nat. Biotechnol. doi: 10.1038/nbt923 – volume: 183 start-page: 3752 year: 2001 ident: 77_CR13 publication-title: J. Bacteriol. doi: 10.1128/JB.183.12.3752-3760.2001 – volume: 183 start-page: 1405 year: 2001 ident: 77_CR14 publication-title: J. Bacteriol. doi: 10.1128/JB.183.4.1405-1412.2001 – volume: 9 start-page: 1176 year: 2007 ident: 77_CR25 publication-title: Environ. Microbiol. doi: 10.1111/j.1462-2920.2007.01240.x – volume: 27 start-page: 63 year: 1972 ident: 77_CR39 publication-title: FEBS Lett. doi: 10.1016/0014-5793(72)80410-1 – volume: 181 start-page: 165 year: 1999 ident: 77_CR20 publication-title: FEMS Microbiol. Lett. doi: 10.1111/j.1574-6968.1999.tb08840.x – volume: 181 start-page: 681 year: 1999 ident: 77_CR36 publication-title: J. Bacteriol. doi: 10.1128/JB.181.2.681-684.1999 – volume: 170 start-page: 1999 year: 1988 ident: 77_CR10 publication-title: J. Bacteriol. doi: 10.1128/jb.170.4.1999-2001.1988 – volume: 260 start-page: 30 year: 2006 ident: 77_CR12 publication-title: FEMS Microbiol. Lett. doi: 10.1111/j.1574-6968.2006.00297.x – volume: 29 start-page: 1599 year: 1996 ident: 77_CR23 publication-title: Braz. J. Med. Biol. Res. – volume: 84 start-page: 467 year: 1989 ident: 77_CR21 publication-title: Gene doi: 10.1016/0378-1119(89)90522-2 – volume: 72 start-page: 248 year: 1976 ident: 77_CR3 publication-title: Anal. Biochem. doi: 10.1016/0003-2697(76)90527-3 – volume: 179 start-page: 3304 year: 1997 ident: 77_CR1 publication-title: J. Bacteriol. doi: 10.1128/jb.179.10.3304-3309.1997 – volume: 127 start-page: 285 year: 1966 ident: 77_CR8 publication-title: Bioch. Biophys. Acta. doi: 10.1016/0304-4165(66)90383-7 – volume: 58 start-page: 213 year: 1967 ident: 77_CR33 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.58.1.213 – volume: 9 start-page: 27 year: 1987 ident: 77_CR37 publication-title: Plant Mol. Biol. doi: 10.1007/BF00017984 – volume: 231 start-page: 743 year: 1985 ident: 77_CR6 publication-title: Biochem. J. doi: 10.1042/bj2310743 – reference: 11914357 - J Bacteriol. 2002 Apr;184(8):2251-9 – reference: 24276795 - Plant Mol Biol. 1987 Jan;9(1):27-39 – reference: 5964974 - Biochim Biophys Acta. 1966 Oct 31;127(2):285-94 – reference: 9882688 - J Bacteriol. 1999 Jan;181(2):681-4 – reference: 7495836 - Biochim Biophys Acta. 1995 Nov 21;1232(1-2):33-42 – reference: 2162051 - Proc Natl Acad Sci U S A. 1990 Jun;87(12):4645-9 – reference: 17473889 - Can J Microbiol. 2006 Dec;52(12):1199-207 – reference: 17098935 - Nucleic Acids Res. 2007 Jan;35(Database issue):D358-62 – reference: 16331441 - Arch Microbiol. 2006 Mar;185(1):55-62 – reference: 942051 - Anal Biochem. 1976 May 7;72:248-54 – reference: 5231601 - Proc Natl Acad Sci U S A. 1967 Jul;58(1):213-6 – reference: 2515118 - Gene. 1989 Dec 14;84(2):467-71 – reference: 3907625 - Biochem J. 1985 Nov 1;231(3):743-53 – reference: 9222418 - Braz J Med Biol Res. 1996 Dec;29(12):1599-602 – reference: 14704707 - Nat Biotechnol. 2004 Jan;22(1):55-61 – reference: 3078742 - FEMS Microbiol Rev. 1988 Apr-Jun;4(2):155-75 – reference: 11566390 - J Biotechnol. 2001 Oct 4;91(2-3):189-95 – reference: 3350797 - J Bacteriol. 1988 Apr;170(4):1999-2001 – reference: 11157954 - J Bacteriol. 2001 Feb;183(4):1405-12 – reference: 10564803 - FEMS Microbiol Lett. 1999 Dec 1;181(1):165-70 – reference: 11946808 - FEBS Lett. 1972 Oct 15;27(1):63-67 – reference: 12207230 - Mol Genet Genomics. 2002 Aug;267(6):820-8 – reference: 11319127 - Appl Environ Microbiol. 2001 May;67(5):2375-9 – reference: 17569992 - Mol Genet Genomics. 2007 Sep;278(3):255-71 – reference: 6352705 - J Biol Chem. 1983 Oct 10;258(19):12064-8 – reference: 3541922 - Biochem J. 1986 Oct 1;239(1):69-75 – reference: 11668346 - Braz J Med Biol Res. 2001 Nov;34(11):1379-95 – reference: 2503674 - Mol Microbiol. 1989 Feb;3(2):141-8 – reference: 16790015 - FEMS Microbiol Lett. 2006 Jul;260(1):30-5 – reference: 17472633 - Environ Microbiol. 2007 May;9(5):1176-85 – reference: 11371540 - J Bacteriol. 2001 Jun;183(12):3752-60 – reference: 15837392 - FEMS Microbiol Lett. 2005 Apr 15;245(2):345-51 – reference: 9150228 - J Bacteriol. 1997 May;179(10):3304-9 – reference: 2708314 - J Bacteriol. 1989 May;171(5):2591-8
SSID	ssj0061342
Score	1.8851519
Snippet	The pathway of electron transport to nitrogenase in the endophytic β-Proteobacterium Herbaspirillum seropedicae has not been characterized. We have generated... The pathway of electron transport to nitrogenase in the endophytic β-Proteobacterium Herbaspirillum seropedicae has not been characterized. We have generated... The pathway of electron transport to nitrogenase in the endophytic beta-Proteobacterium Herbaspirillum seropedicae has not been characterized. We have...
SourceID	nrf proquest pubmed crossref springer fao
SourceType	Open Website Aggregation Database Index Database Enrichment Source Publisher
StartPage	77
SubjectTerms	Ammonium Antibiotics Bacterial Proteins - genetics Bacterial Proteins - metabolism Biomedical and Life Sciences Cloning DNA Mutational Analysis fdxA fdxN ferredoxin Ferredoxins - genetics Ferredoxins - metabolism Genes H. seropedicae Herbaspirillum - genetics Herbaspirillum - metabolism Life Sciences Microbiology Molecular biology Mutation Nitrogen Nitrogen fixation Nitrogen Fixation - genetics NITROGENASA NITROGENASE Nitrogenase - metabolism Phenotype Plasmids Promoter Regions, Genetic Proteins Transcription, Genetic 생물학
SummonAdditionalLinks	– databaseName: SpringerLINK Contemporary 1997-Present dbid: RSV link: http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3da9RAEB9sVfDF72pslRV8Uhauu5fb5LGUlopySNXSt2WTzB7hSlJyqdxB__jObJI7xFbQlySQ_Uhmf_OV2cwAfFCGjFSNSE5OyiXMtJaJS3KZxT5NY0UKOnzvOPtqptPk_Dz91v_HvRh2uw8hySCpNz-7KWViGT7mj4yRqy24T9ouYW48_X42iF9ST6FiDrWOJXGQHkKZtw3xmzLa8q6mY9X426zNPyKlQQEdP_mvR38Kj3t7Uxx0AHkG97B6Dg-7CpSrF3BNMBFlRTIq5A1vRe0FmYSiKr10_cphITw2nFh0WVbyopyjmLGEFL5YHghXFXwx5Z4ntEaOQ_cl108WhO76MgSCeA4as21q6il8uQx4eAk_j49-HJ7IviCDzIm1W0m6LMtMinkxTiaF8ujJHUKv3MQYnblxPvLk5CIarceeLJ1cT5C94CLTznBhmR3YruoKX4MwHmN2VZQniy7NiwyLJEadeYIHOW0YwWhYGZv32cq5aMaF3eRZZqJaIqplotpVBB_XXS67VB1_a7xDy23djESp_XIazKDgHUbwnhBg53lpOfM2n2e1nTeW_IvPNuHEpiqC3QEftmf5heXE-WOi0CgCsb5LvMoBGFdhfbWwTBdD9gBN8qpD1fpBFdlS-3Q_gk8DhDZD3_kWb_6p9S486vY-8GacPdhumyt8Cw_yX225aN4FLroBPaUUOQ priority: 102 providerName: Springer Nature
Title	The Involvement of the nif-Associated Ferredoxin-Like Genes fdxA and fdxN of Herbaspirillum seropedicae in Nitrogen Fixation
URI	https://link.springer.com/article/10.1007/s12275-009-0077-y https://www.ncbi.nlm.nih.gov/pubmed/20221733 https://www.proquest.com/docview/229041280 https://www.proquest.com/docview/733472841 https://www.kci.go.kr/kciportal/ci/sereArticleSearch/ciSereArtiView.kci?sereArticleSearchBean.artiId=ART001425543
Volume	48
WOSCitedRecordID	wos000275135800012&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText	1
inHoldings	1
isFullTextHit
isPrint
ispartofPNX	The Journal of Microbiology, 2010, 48(1), , pp.77-83
journalDatabaseRights	– providerCode: PRVPQU databaseName: Biological Science Database customDbUrl: eissn: 1976-3794 dateEnd: 20190131 omitProxy: false ssIdentifier: ssj0061342 issn: 1225-8873 databaseCode: M7P dateStart: 20080201 isFulltext: true titleUrlDefault: http://search.proquest.com/biologicalscijournals providerName: ProQuest – providerCode: PRVPQU databaseName: Earth, Atmospheric & Aquatic Science Database customDbUrl: eissn: 1976-3794 dateEnd: 20190131 omitProxy: false ssIdentifier: ssj0061342 issn: 1225-8873 databaseCode: PCBAR dateStart: 20080201 isFulltext: true titleUrlDefault: https://search.proquest.com/eaasdb providerName: ProQuest – providerCode: PRVPQU databaseName: Health & Medical Collection customDbUrl: eissn: 1976-3794 dateEnd: 20190131 omitProxy: false ssIdentifier: ssj0061342 issn: 1225-8873 databaseCode: 7X7 dateStart: 20080201 isFulltext: true titleUrlDefault: https://search.proquest.com/healthcomplete providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Central customDbUrl: eissn: 1976-3794 dateEnd: 20190131 omitProxy: false ssIdentifier: ssj0061342 issn: 1225-8873 databaseCode: BENPR dateStart: 20080201 isFulltext: true titleUrlDefault: https://www.proquest.com/central providerName: ProQuest – providerCode: PRVAVX databaseName: SpringerLINK Contemporary 1997-Present customDbUrl: eissn: 1976-3794 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0061342 issn: 1225-8873 databaseCode: RSV dateStart: 20080201 isFulltext: true titleUrlDefault: https://link.springer.com/search?facet-content-type=%22Journal%22 providerName: Springer Nature
link	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3fb9MwED7RDSRexs-NMKiMxBPIooubOnlC27RpCFRVBaa-WY5jV1GnpKQZaqX98dw5SScE7IUXJ1LiJM53Pt_lLt8BvA0lGqnCWnRyEiphJgSPdWx4GrkkiUJcoP33jssvcjyOZ7Nk0ubmrNq0yk4nekWdlYa-kX8gXvIhKtPBx-UPTkWjKLjaVtDowS6RJAifuTfpFDEuVL52zhGKLMe5JLqgpv9zLgxlxH1kYCAl3_y2LPWcLrEtKvc3u_OPmKlfis4f_ecgHsNea4Oy40ZonsA9WzyFB01Vys0zuEHRYXmBestzidesdAzNRFbkjusWTZsxZysiG13nBb_KF5bNSWsyl62PmS4y2hlTzwvETVM4P6eaygwlvlz64BDdA69ZVyX2ZC5fexl5Dt_Pz76dXvC2SAM3ON1rjqNJU5lYkw3jURY669BFsi7UIylFqodm4NDxtVYKMXRo_RgxsuQZZ6nQkorN7MNOURb2BTDpbETuS-jQyktMltosjqxIHYoMOnI2gEGHkTItgzkV0rhSt9zLBKtCWBXBqjYBvNt2WTb0HXedvI_AKz1H9ao-T71p5D3GAN6gLKiFyRWxcdN2XqpFpdDn-KRiIjsNAzjsIFetGlipLd4BsO1RnL8UlNGFLa9Xit6LRBsBb3LQyNf2QUO0r47weADvO4G7vfQ_R_Hyzgc5hIdN_gMl5LyCnbq6tq_hvvlZ56uqDz05k76N-7B7cjaeTPt-TmE7_Xr5C7BeIco
linkProvider	ProQuest
linkToHtml	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Lb9NAEB71AYIL74Ipj0UCDqAV6TrO2gcOoVAlSoiqqqDeFnu9G1mp7OC4kEj8Jf4jM2s7FQJ664FLHMnetb3-vnl4xjMAz4VEI9U3Bp2ciFqY-T4P41DzJLBRFAhU0O59x-exnEzCk5PocAN-tt_CUFplKxOdoE4LTe_I31Bd8i4K006TQDkyq-_oni3eDt_js3whxMGH4_0BbzoIcI1YrDgenyQyMjrthr1UWGPRfjdWxD0p_STu6o5Fr8wY6ftdi6pZ-z1Dblua-LGkTig478v5V05NqiiY23Ts2ITtsBcFSKvtw_13_aNW9KNqdN169pAkHNnrt2FU962eEDLgLhbRkZKvflOEmzYu8Dcv7d8s3T-itE75Hdz8z5btFtxorGzWr2lxGzZMfgeu1n03V3fhB5KDZTlKZlctvWKFZWgIszyzPG7walJmTUnlVJdZzk-zmWFT0gvMpss-i_OU_kxo5ACRGVPCQkZdoxlyupi78BedA-esygJHMpstHQvuwadLWY0d2MqL3DwAJq0JyEETFu3YSKeJScPA-IlFUqCrajzotJhQuqnRTq1CTtV5dWmCkUIYKYKRWnnwaj1kXhcouejgHQSaiqeoQNToyBl_zif24BliT810pqjeOG2nhZqVCr2qoQqpnKvwYLeFmGoE3UKt8eUBW-9FCUVhpzg3xdlC0bpItILwJPdrPK8vVKAFuYf7PXjdAvx86n_excMLL-QpXBscfxyr8XAy2oXrdbYHpR89gq2qPDOP4Yr-VmWL8knDXgZfLpsMvwBqbns4
linkToPdf	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3da9swED_W7oO-7LNdvXabBnvaEM0sO7IfS9vQ0hLKPkrfhGxLwaTIwXFHAvvjdyfbCWPdYOzFMViS49Pp7nc--X4A70OJIFUYg0FOShRmQvBEJznPYpumcYgO2r_vuLqQ43FyfZ1edjyn8363e5-SbL9poCpNrjmYFfZg_eFbGMqY-xf7Ayn5cgPuR8QZROH6l6veFKOr8uw52DrmuJpEn9a8a4hfHNOG1RUeXW3vQp6_ZU29Mxo9-e_HeAqPOxzKDlvFeQb3jHsOD1tmyuUL-IHqw0qHtsvXE29YZRlCReZKy3U3o6Zg1tRUcHRROn5TTg2bkOVktlgcMu0KOhlTz1OcO00p_ZJ4lRlqfTXzCSK6B47Z1BX2ZLZceD3Zhm-jk69Hp7wjauA5LvmGo4_LMpmavIiSYRFaYzFMMjbUQylFpqN8YDH4NUYKEVlEQLkYGoqOi0xoSYQzO7DpKmd2gUlrYgphQotIL82LzBRJbERmUW0wmDMBDPpZUnlXxZzING7Uuv4yCVWhUBUJVS0D-LDqMmtLePyt8Q5OvdITNLHq_LOHRz5qDOAdaoOa5qWiitz0O6nUtFYYd5yphAqehgHs9bqiOlMwV1RQP0IJDQJgq6u4hikxo52pbueK5CIRJ-BNXrYatvqjIWKsT3g9gI-9Oq2H_uNTvPqn1m_h0eXxSF2cjc_3YKvdHkH7dfZhs6lvzWt4kH9vynn9xi-un1znIAE
openUrl	ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=The+involvement+of+the+nif-associated+ferredoxin-like+genes+fdxA+and+fdxN+of+Herbaspirillum+seropedicae+in+nitrogen+fixation&rft.jtitle=The+journal+of+microbiology&rft.au=Souza%2C+Andr%C3%A9+L.+F.&rft.au=Invitti%2C+Adriana+L.&rft.au=Rego%2C+Fabiane+G.+M.&rft.au=Monteiro%2C+Rose+A.&rft.date=2010-02-01&rft.issn=1225-8873&rft.eissn=1976-3794&rft.volume=48&rft.issue=1&rft.spage=77&rft.epage=83&rft_id=info:doi/10.1007%2Fs12275-009-0077-y&rft.externalDBID=n%2Fa&rft.externalDocID=10_1007_s12275_009_0077_y
thumbnail_l	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1225-8873&client=summon
thumbnail_m	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1225-8873&client=summon
thumbnail_s	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1225-8873&client=summon