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
Hauptverfasser: Elmore, Bradley O., Bergmann, David J., Klotz, Martin G., Hooper, Alan B.
Format: Journal Article
Sprache:Englisch
Veröffentlicht: England 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
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  organization: Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, St. Paul, MN, United States
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  givenname: David J.
  surname: Bergmann
  fullname: Bergmann, David J.
  organization: Department of Biology, Black Hills State University, Spearfish, SD, United States
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  givenname: Martin G.
  surname: Klotz
  fullname: Klotz, Martin G.
  organization: Departments of Biology and Microbiology and Immunology, University of Louisville, Louisville, KY, United States
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  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
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Issue 5
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
URI https://dx.doi.org/10.1016/j.febslet.2007.01.068
https://onlinelibrary.wiley.com/doi/abs/10.1016%2Fj.febslet.2007.01.068
https://www.ncbi.nlm.nih.gov/pubmed/17292891
https://www.proquest.com/docview/20130965
https://www.proquest.com/docview/70212575
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