Controlling the functionality of cytochrome c(1) redox potentials in the Rhodobacter capsulatus bc(1) complex through disulfide anchoring of a loop and a beta-branched amino acid near the heme-ligating methionine.

doi:10.1021/bi011630w

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Article

Controlling the functionality of cytochrome c(1) redox potentials in the Rhodobacter capsulatus bc(1) complex through disulfide anchoring of a loop and a beta-branched amino acid near the heme-ligating methionine.

Biochemistry - 4 Dec 2001

Osyczka A, Dutton P L, Moser C C, Darrouzet E, Daldal F

Abstract excerpt

The cytochrome c(1) subunit of the ubihydroquinone:cytochrome c oxidoreductase (bc(1) complex) contains a single heme group covalently attached to the polypeptide via thioether bonds of two conserved cysteine residues. In the photosynthetic bacterium Rhodobacter (Rba.) capsulatus, cytochrome c(1) contains two additional cysteines, C144 and C167. Site-directed mutagenesis reveals a disulfide bond (rare in monoheme...

Topics

Amino Acid Sequence
Binding Sites
Cytochromes c1
Disulfides
Electron Transport
Electron Transport Complex III
Electrophoresis, Polyacrylamide Gel
Factor Xa
Heme
Methionine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutagenesis, Site-Directed

Mutation

Oxidation-Reduction

Plasmids

Protein Folding

Rhodobacter capsulatus

Sequence Homology, Amino Acid

Source

Open in PubMed

Identifiers

PMID: 11724568
DOI: 10.1021/bi011630w

Provenance

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