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Article

Electron-proton coupling in cytochrome c studied using protein variants.

European journal of biochemistry - 15 Feb 1992

Gao Y, McLendon G, Pielak G J, Williams R J

Abstract excerpt

An NMR study of the cytochrome c variant Asn52Ile is used to show how the redox state change in native cytochrome c is coupled to a rearrangement of a proton network which runs through the cytochrome c molecule. The substitution breaks the H-bond network and removes the coupling. The uncovering of this putative proton channel and the connection of changes to it with redox state changes of the iron centre of the...

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Identifiers

PMID: 1371254
DOI: 10.1111/j.1432-1033.1992.tb16642.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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