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Article

Suppression of axial methionine fluxion in Hydrogenobacter thermophilus Gln64Asn cytochrome c552.

Biochemistry - 5 Apr 2005

Wen Xin, Bren Kara L

Abstract excerpt

Proteins in the cytochrome c (cyt c) family with His-Met heme axial ligation display diverse heme electronic structures as revealed by the NMR spectra of their oxidized (paramagnetic) forms. These variations in electronic structure are thought to result primarily from differences in heme axial Met orientation among cyt c species. The factors determining Met orientation in cyts c, however, remain poorly...

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PMID: 15794659
DOI: 10.1021/bi047556+

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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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Suppression of axial methionine fluxion in Hydrogenobacter thermophilus Gln64Asn cytochrome c552.PMID 15794659Read ↗

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Inversion of the stereochemistry around the sulfur atom of the axial methionine side chain through alteration of amino acid side chain packing in Hydrogenobacter thermophilus cytochrome C552 and its functional consequences.Semantic proximity Read ↗

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