The disulfide bridge in the head domain of rhodobacter sphaeroides cytochrome c1 is needed to maintain its structural integrity.

doi:10.1021/bi0522246

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Article

The disulfide bridge in the head domain of rhodobacter sphaeroides cytochrome c1 is needed to maintain its structural integrity.

Biochemistry - 18 Apr 2006

Elberry Maria, Yu Linda, Yu Chang-An

Abstract excerpt

Cytochrome c(1) of Rhodobacter sphaeroides ubiquinol-cytochrome c oxidoreductase contains several insertions and deletions that distinguish it from the complex of other higher organisms. Additionally, this bacterial cytochrome c(1) contains two nonconserved cysteines, C145 and C169, with the latter included in the second long insertion located upstream of the sixth heme ligand, M185. The orientation of the...

Topics

Animals
Blotting, Western
Catalysis
Cysteine
Cytochromes c1
Disulfides
Electrophoresis, Polyacrylamide Gel
Horses
Models, Molecular
Mutation
Oxidation-Reduction
Protein Structure, Tertiary
Rhodobacter sphaeroides
Structure-Activity Relationship

Source

Open in PubMed

Identifiers

PMID: 16605267
DOI: 10.1021/bi0522246

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