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Article

Characterization of mutant Met100Lys of cytochrome c-550 from Thiobacillus versutus with lysine-histidine heme ligation.

Biochemistry - 23 Aug 1994

Ubbink M, Campos A P, Teixeira M, Hunt N I, Hill H A, Canters G W

Abstract excerpt

The heme iron in cytochrome c-550 from Thiobacillus versutus has a methionine and a histidine as axial ligands. In order to study the characteristics of a possible lysine-histidine ligation in a heme protein, the methionine has been replaced by a lysine. This residue acts as a ligand between pH 3 and 12. The midpoint potential of the mutant has shifted -329 mV compared to wild type, but apart from this shift the...

Topics

Cytochrome c Group
Electron Spin Resonance Spectroscopy
Heme
Histidine
Hydrogen-Ion Concentration
Lysine
Magnetic Resonance Spectroscopy
Methionine
Models, Molecular
Mutation
Spectrophotometry

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Structure-Activity Relationship

Thiobacillus

Source

Identifiers

PMID: 8060974
DOI: 10.1021/bi00199a032

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8060974-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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