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Article

Characterization of the ubiquinol oxidation sites in cytochromes bo and bd from Escherichia coli using aurachin C analogues.

Journal of biochemistry - 1 Jan 1999

Miyoshi H, Takegami K, Sakamoto K, Mogi T, Iwamura H

Abstract excerpt

Natural aurachin C is the most potent inhibitor of oxidation of ubiquinols by cytochromes bo and bd from Escherichia coli. To probe the structural properties of the substrate oxidation site in the ubiquinol oxidases, we synthesized a systematic set of aurachin C analogues (N-hydroxy-4-quinolone d...

Topics

Binding Sites
Cytochrome b Group
Cytochromes
Electron Transport Chain Complex Proteins
Enzyme Inhibitors
Escherichia coli
Escherichia coli Proteins
Mutation
Oxidation-Reduction
Oxidoreductases
Quinolones

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Structure-Activity Relationship

Ubiquinone

Source

Identifiers

PMID: 9880809
DOI: 10.1093/oxfordjournals.jbchem.a022250

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9880809-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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