X-ray emission spectroscopy evidences a central carbon in the nitrogenase iron-molybdenum cofactor

Nitrogenase is a complex enzyme that catalyzes the reduction of dinitrogen to ammonia. Despite insight from structural and biochemical studies, its structure and mechanism await full characterization. An iron-molybdenum cofactor (FeMoco) is thought to be the site of dinitrogen reduction, but the ide...

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Vydáno v:	Science (American Association for the Advancement of Science) Ročník 334; číslo 6058; s. 974
Hlavní autoři:	Lancaster, Kyle M, Roemelt, Michael, Ettenhuber, Patrick, Hu, Yilin, Ribbe, Markus W, Neese, Frank, Bergmann, Uwe, DeBeer, Serena
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States 18.11.2011
Témata:	Azotobacter vinelandii - chemistry Biocatalysis Carbon - chemistry Ligands Models, Molecular Molecular Structure Molybdoferredoxin - chemistry Molybdoferredoxin - metabolism Nitrogen - chemistry Oxidation-Reduction Oxygen - chemistry Spectrometry, X-Ray Emission
ISSN:	1095-9203, 1095-9203
On-line přístup:	Zjistit podrobnosti o přístupu
Tagy:	Přidat tag Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!

Abstract	Nitrogenase is a complex enzyme that catalyzes the reduction of dinitrogen to ammonia. Despite insight from structural and biochemical studies, its structure and mechanism await full characterization. An iron-molybdenum cofactor (FeMoco) is thought to be the site of dinitrogen reduction, but the identity of a central atom in this cofactor remains unknown. Fe Kβ x-ray emission spectroscopy (XES) of intact nitrogenase MoFe protein, isolated FeMoco, and the FeMoco-deficient nifB protein indicates that among the candidate atoms oxygen, nitrogen, and carbon, it is carbon that best fits the XES data. The experimental XES is supported by computational efforts, which show that oxidation and spin states do not affect the assignment of the central atom to C(4-). Identification of the central atom will drive further studies on its role in catalysis.
AbstractList	Nitrogenase is a complex enzyme that catalyzes the reduction of dinitrogen to ammonia. Despite insight from structural and biochemical studies, its structure and mechanism await full characterization. An iron-molybdenum cofactor (FeMoco) is thought to be the site of dinitrogen reduction, but the identity of a central atom in this cofactor remains unknown. Fe Kβ x-ray emission spectroscopy (XES) of intact nitrogenase MoFe protein, isolated FeMoco, and the FeMoco-deficient nifB protein indicates that among the candidate atoms oxygen, nitrogen, and carbon, it is carbon that best fits the XES data. The experimental XES is supported by computational efforts, which show that oxidation and spin states do not affect the assignment of the central atom to C(4-). Identification of the central atom will drive further studies on its role in catalysis.Nitrogenase is a complex enzyme that catalyzes the reduction of dinitrogen to ammonia. Despite insight from structural and biochemical studies, its structure and mechanism await full characterization. An iron-molybdenum cofactor (FeMoco) is thought to be the site of dinitrogen reduction, but the identity of a central atom in this cofactor remains unknown. Fe Kβ x-ray emission spectroscopy (XES) of intact nitrogenase MoFe protein, isolated FeMoco, and the FeMoco-deficient nifB protein indicates that among the candidate atoms oxygen, nitrogen, and carbon, it is carbon that best fits the XES data. The experimental XES is supported by computational efforts, which show that oxidation and spin states do not affect the assignment of the central atom to C(4-). Identification of the central atom will drive further studies on its role in catalysis. Nitrogenase is a complex enzyme that catalyzes the reduction of dinitrogen to ammonia. Despite insight from structural and biochemical studies, its structure and mechanism await full characterization. An iron-molybdenum cofactor (FeMoco) is thought to be the site of dinitrogen reduction, but the identity of a central atom in this cofactor remains unknown. Fe Kβ x-ray emission spectroscopy (XES) of intact nitrogenase MoFe protein, isolated FeMoco, and the FeMoco-deficient nifB protein indicates that among the candidate atoms oxygen, nitrogen, and carbon, it is carbon that best fits the XES data. The experimental XES is supported by computational efforts, which show that oxidation and spin states do not affect the assignment of the central atom to C(4-). Identification of the central atom will drive further studies on its role in catalysis.
Author	Roemelt, Michael Ettenhuber, Patrick Lancaster, Kyle M Bergmann, Uwe Neese, Frank DeBeer, Serena Hu, Yilin Ribbe, Markus W
Author_xml	– sequence: 1 givenname: Kyle M surname: Lancaster fullname: Lancaster, Kyle M organization: Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA – sequence: 2 givenname: Michael surname: Roemelt fullname: Roemelt, Michael – sequence: 3 givenname: Patrick surname: Ettenhuber fullname: Ettenhuber, Patrick – sequence: 4 givenname: Yilin surname: Hu fullname: Hu, Yilin – sequence: 5 givenname: Markus W surname: Ribbe fullname: Ribbe, Markus W – sequence: 6 givenname: Frank surname: Neese fullname: Neese, Frank – sequence: 7 givenname: Uwe surname: Bergmann fullname: Bergmann, Uwe – sequence: 8 givenname: Serena surname: DeBeer fullname: DeBeer, Serena
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/22096198$$D View this record in MEDLINE/PubMed
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Snippet	Nitrogenase is a complex enzyme that catalyzes the reduction of dinitrogen to ammonia. Despite insight from structural and biochemical studies, its structure...
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SubjectTerms	Azotobacter vinelandii - chemistry Biocatalysis Carbon - chemistry Ligands Models, Molecular Molecular Structure Molybdoferredoxin - chemistry Molybdoferredoxin - metabolism Nitrogen - chemistry Oxidation-Reduction Oxygen - chemistry Spectrometry, X-Ray Emission
Title	X-ray emission spectroscopy evidences a central carbon in the nitrogenase iron-molybdenum cofactor
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