Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coli.

doi:10.1021/bi00041a029

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Article

Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coli.

Biochemistry - 17 Oct 1995

Kaysser T M, Ghaim J B, Georgiou C, Gennis R B

Abstract excerpt

The cytochrome bd oxidase is one of two terminal oxidases in the aerobic respiratory chain of Escherichia coli. The complex is composed of two subunits (I and II) and three heme prosthetic groups (heme b558, heme b595, and a chlorin, called heme d). Both subunits are located within the bacterial cytoplasmic membrane, and each has multiple putative transmembrane helices. Heme b558 is a six-coordinate, low-spin...

Topics

Amino Acid Sequence
Base Sequence
Cytochrome b Group
Cytochromes
Dithionite
Electron Transport Chain Complex Proteins
Escherichia coli
Escherichia coli Proteins
Genotype
Heme
Histidine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Leucine

Ligands

Macromolecular Substances

Methionine

Molecular Sequence Data

Mutagenesis, Site-Directed

NADPH Oxidases

Source

Open in PubMed

Identifiers

PMID: 7577938
DOI: 10.1021/bi00041a029

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7577938-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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