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, 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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry
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Bacterial Proteins / classification
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Circular Dichroism
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Cytochromes / chemistry*
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Cytochromes / classification
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Cytochromes / genetics
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Cytochromes / metabolism*
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Cytochromes c / chemistry*
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Cytochromes c / classification
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Cytochromes c / genetics
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Cytochromes c / metabolism*
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Cytochromes c' / chemistry*
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Cytochromes c' / classification
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Cytochromes c' / genetics
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Cytochromes c' / metabolism*
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Evolution, Molecular
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Methylococcus capsulatus / genetics
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Methylococcus capsulatus / metabolism
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Nitrosomonas europaea / genetics
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Nitrosomonas europaea / metabolism
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Phylogeny
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Protein Structure, Secondary
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Sequence Homology, Amino Acid
Substances
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Bacterial Proteins
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Cytochromes
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Cytochromes c'
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cytochrome P-460
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Cytochromes c