Cytochromes P460 and c′-beta; A new family of high-spin cytochromes c
Cytochromes-P460 of Nitrosomonas europaea and Methylococcus capsulatus (Bath), and the cytochrome c′ of M. capsulatus, believed to be involved in binding or transformation of N-oxides, are shown to represent an evolutionarily related new family of monoheme, ∼17 kDa, cytochromes c found in the genome...
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| Veröffentlicht in: | FEBS letters Jg. 581; H. 5; S. 911 - 916 |
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| Format: | Journal Article |
| Sprache: | Englisch |
| Veröffentlicht: |
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Elsevier B.V
06.03.2007
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| ISSN: | 0014-5793, 1873-3468 |
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| Abstract | Cytochromes-P460 of
Nitrosomonas europaea and
Methylococcus capsulatus (Bath), and the cytochrome
c′ of
M. capsulatus, believed to be involved in binding or transformation of N-oxides, are shown to represent an evolutionarily related new family of monoheme, ∼17
kDa, cytochromes
c found in the genomes of diverse Proteobacteria. All members of this family have a predicted secondary structure predominantly of beta-sheets in contrast to the predominantly alpha-helical cytochromes
c′ found in photoheterotrophic and denitrifying Proteobacteria. |
|---|---|
| AbstractList | Cytochromes‐P460 of
Nitrosomonas europaea
and
Methylococcus capsulatus
(Bath), and the cytochrome
c
′ of
M. capsulatus
, believed to be involved in binding or transformation of N‐oxides, are shown to represent an evolutionarily related new family of monoheme, ∼17 kDa, cytochromes
c
found in the genomes of diverse Proteobacteria. All members of this family have a predicted secondary structure predominantly of beta‐sheets in contrast to the predominantly alpha‐helical cytochromes
c
′ found in photoheterotrophic and denitrifying Proteobacteria. Cytochromes-P460 of Nitrosomonas europaea and Methylococcus capsulatus (Bath), and the cytochrome c' of M. capsulatus, believed to be involved in binding or transformation of N-oxides, are shown to represent an evolutionarily related new family of monoheme, approximately 17kDa, cytochromes c found in the genomes of diverse Proteobacteria. All members of this family have a predicted secondary structure predominantly of beta-sheets in contrast to the predominantly alpha-helical cytochromes c' found in photoheterotrophic and denitrifying Proteobacteria. Cytochromes-P460 of Nitrosomonas europaea and Methylococcus capsulatus (Bath), and the cytochrome c′ of M. capsulatus, believed to be involved in binding or transformation of N-oxides, are shown to represent an evolutionarily related new family of monoheme, ∼17 kDa, cytochromes c found in the genomes of diverse Proteobacteria. All members of this family have a predicted secondary structure predominantly of beta-sheets in contrast to the predominantly alpha-helical cytochromes c′ found in photoheterotrophic and denitrifying Proteobacteria. Cytochromes-P460 of Nitrosomonas europaea and Methylococcus capsulatus (Bath), and the cytochrome c' of M. capsulatus, believed to be involved in binding or transformation of N-oxides, are shown to represent an evolutionarily related new family of monoheme, approximately 17kDa, cytochromes c found in the genomes of diverse Proteobacteria. All members of this family have a predicted secondary structure predominantly of beta-sheets in contrast to the predominantly alpha-helical cytochromes c' found in photoheterotrophic and denitrifying Proteobacteria.Cytochromes-P460 of Nitrosomonas europaea and Methylococcus capsulatus (Bath), and the cytochrome c' of M. capsulatus, believed to be involved in binding or transformation of N-oxides, are shown to represent an evolutionarily related new family of monoheme, approximately 17kDa, cytochromes c found in the genomes of diverse Proteobacteria. All members of this family have a predicted secondary structure predominantly of beta-sheets in contrast to the predominantly alpha-helical cytochromes c' found in photoheterotrophic and denitrifying Proteobacteria. Cytochromes-P460 of Nitrosomonas europaea and Methylococcus capsulatus (Bath), and the cytochrome c' of M. capsulatus, believed to be involved in binding or transformation of N-oxides, are shown to represent an evolutionarily related new family of monoheme, ~17kDa, cytochromes c found in the genomes of diverse Proteobacteria. All members of this family have a predicted secondary structure predominantly of beta-sheets in contrast to the predominantly alpha-helical cytochromes c' found in photoheterotrophic and denitrifying Proteobacteria. Cytochromes‐P460 of Nitrosomonas europaea and Methylococcus capsulatus (Bath), and the cytochrome c′ of M. capsulatus, believed to be involved in binding or transformation of N‐oxides, are shown to represent an evolutionarily related new family of monoheme, ∼17 kDa, cytochromes c found in the genomes of diverse Proteobacteria. All members of this family have a predicted secondary structure predominantly of beta‐sheets in contrast to the predominantly alpha‐helical cytochromes c′ found in photoheterotrophic and denitrifying Proteobacteria. |
| Author | Elmore, Bradley O. Klotz, Martin G. Hooper, Alan B. Bergmann, David J. |
| Author_xml | – sequence: 1 givenname: Bradley O. surname: Elmore fullname: Elmore, Bradley O. organization: Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, St. Paul, MN, United States – sequence: 2 givenname: David J. surname: Bergmann fullname: Bergmann, David J. organization: Department of Biology, Black Hills State University, Spearfish, SD, United States – sequence: 3 givenname: Martin G. surname: Klotz fullname: Klotz, Martin G. organization: Departments of Biology and Microbiology and Immunology, University of Louisville, Louisville, KY, United States – sequence: 4 givenname: Alan B. surname: Hooper fullname: Hooper, Alan B. email: hooper@umn.edu organization: Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, St. Paul, MN, United States |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/17292891$$D View this record in MEDLINE/PubMed |
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| Keywords | Cytochrome c Denitrification Cytochrome P460 N-oxide detoxification Bacterial enzyme evolution |
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| Snippet | Cytochromes-P460 of
Nitrosomonas europaea and
Methylococcus capsulatus (Bath), and the cytochrome
c′ of
M. capsulatus, believed to be involved in binding or... Cytochromes‐P460 of Nitrosomonas europaea and Methylococcus capsulatus (Bath), and the cytochrome c′ of M. capsulatus, believed to be involved in binding or... Cytochromes‐P460 of Nitrosomonas europaea and Methylococcus capsulatus (Bath), and the cytochrome c ′ of M. capsulatus , believed to be involved in binding or... Cytochromes-P460 of Nitrosomonas europaea and Methylococcus capsulatus (Bath), and the cytochrome c' of M. capsulatus, believed to be involved in binding or... |
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| SubjectTerms | Amino Acid Sequence Bacterial enzyme evolution Bacterial Proteins - chemistry Bacterial Proteins - classification Bacterial Proteins - genetics Bacterial Proteins - metabolism Circular Dichroism Cytochrome c Cytochrome P460 Cytochromes - chemistry Cytochromes - classification Cytochromes - genetics Cytochromes - metabolism Cytochromes c - chemistry Cytochromes c - classification Cytochromes c - genetics Cytochromes c - metabolism Denitrification Evolution, Molecular Methylococcus capsulatus Methylococcus capsulatus - genetics Methylococcus capsulatus - metabolism N-oxide detoxification Nitrosomonas europaea Nitrosomonas europaea - genetics Nitrosomonas europaea - metabolism Phylogeny Protein Structure, Secondary Proteobacteria Sequence Homology, Amino Acid |
| Title | Cytochromes P460 and c′-beta; A new family of high-spin cytochromes c |
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