Functional role of heme ligation in cytochrome c. Effects of replacement of methionine 80 with natural and non-natural residues by semisynthesis.

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Article

Functional role of heme ligation in cytochrome c. Effects of replacement of methionine 80 with natural and non-natural residues by semisynthesis.

The Journal of biological chemistry - 25 Feb 1992

Wallace C J, Clark-Lewis I

Abstract excerpt

The nature of the axial ligation to heme iron has been suggested to be the major determinant of the oxidation-reduction potential of a particular cytochrome, but natural cytochromes that vary significantly in E'm invariably differ from one another in many ways. We proposed to clarify this issue b...

Topics

Amino Acids
Animals
Catalysis
Cations
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Cytochrome c Group
Heme
Horses
Iron
Methionine
Mutation
Myocardium
Oxidation-Reduction
Oxygen
Spectrophotometry, Ultraviolet

Source

Open in PubMed

Identifiers

PMID: 1310985

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1310985-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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