6533b81ffe1ef96bd1278fb3

RESEARCH PRODUCT

Membrane D-lactate oxidase in Zymomonas mobilis: evidence for a branched respiratory chain.

Uldis KalnenieksRobert K. PooleStefanie Bringer-meyerNina Galinina

subject

StereochemistryChlorpromazineMicrobiologyMixed Function OxygenasesElectron Transportchemistry.chemical_compoundOxygen ConsumptionCytochrome C1Multienzyme ComplexesGeneticsCytochrome c oxidaseNADH NADPH OxidoreductasesLactic AcidMolecular BiologyZymomonasbiologyMyxothiazolCytochrome b6f complexCytochrome bCytochrome cCytochrome dNADAerobiosisThiazolesBiochemistrychemistrySpectrophotometryCoenzyme Q – cytochrome c reductasebiology.proteinCytochromesMethacrylatesOxidation-Reduction

description

Respiratory chain composition of the ethanol-producing bacterium Zymomonas mobilis was studied. Its membrane D-lactate oxidase was characterised. With NADH, but not D-lactate as substrate, a cytochrome o-like component was seen in CO difference spectra. Chlorpromazine specifically inhibited reduction of cytochrome d, while myxothiazol eliminated the cytochrome o-like features in CO difference spectra. It is suggested that electrons from NADH are distributed between branches terminated by the cytochrome o-like component, cytochrome a, and cytochrome d. With D-lactate, electrons are transported to cytochrome a, or an unidentified CN(-)-sensitive oxidase, and cytochrome d.

yearjournalcountryeditionlanguage
1998-11-01FEMS microbiology letters
10.1111/j.1574-6968.1998.tb13260.xhttps://pubmed.ncbi.nlm.nih.gov/9812368