Preparation and characterization of the water-soluble heme-binding domain of cytochrome c1 from the Rhodobacter sphaeroides bc1 complex.

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Article

Preparation and characterization of the water-soluble heme-binding domain of cytochrome c1 from the Rhodobacter sphaeroides bc1 complex.

The Journal of biological chemistry - 5 Aug 1991

Konishi K, Van Doren S R, Kramer D M, Crofts A R, Gennis R B

Abstract excerpt

The ubiquinol:cytochrome c2 oxidoreductase (bc1 complex) of Rhodobacter sphaeroides consists of four subunits. One of these subunits, cytochrome c1, is the site of interaction with cytochrome c2, a periplasmic protein. In addition, the sequences of the fbcC gene and of the cytochrome c1 subunit t...

Topics

Amino Acid Sequence
Amino Acids
Base Sequence
Carrier Proteins
Chromatography, High Pressure Liquid
Cytochromes c1
Electron Transport Complex III
Electrophoresis, Polyacrylamide Gel
Heme-Binding Proteins
Hemeproteins
Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutagenesis, Site-Directed

Mutation

Operon

Plasmids

Rhodobacter sphaeroides

Sequence Alignment

Source

Open in PubMed

Identifiers

PMID: 1650353

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1650353-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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