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

Uldis Kalnenieks; Nina Galinina; Stefanie Bringer-Meyer; Robert K. Poole

doi:10.1016/S0378-1097(98)00424-8

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

Uldis Kalnenieks
, Nina Galinina
, Stefanie Bringer-Meyer
, Robert K. Poole^*

^*Corresponding author for this work

Jülich Research Centre
University of Sheffield

Research output: Contribution to journal › Article › peer-review

51 Citations (Scopus)

Abstract

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. Copyright (C) 1998 Federation of European Microbiological Societies.

Original language	English
Pages (from-to)	91-97
Number of pages	7
Journal	FEMS Microbiology Letters
Volume	168
Issue number	1
DOIs	https://doi.org/10.1016/S0378-1097(98)00424-8
Publication status	Published - 1 Nov 1998

Keywords

Chlorpromazine
Cytochrome d
Cytochrome o
D-Lactate oxidase
Electron transport chain
Myxothiazol
Zymomonas mobilis

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10.1016/S0378-1097(98)00424-8

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title = "Membrane D-lactate oxidase in Zymomonas mobilis: Evidence for a branched respiratory chain",

abstract = "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. Copyright (C) 1998 Federation of European Microbiological Societies.",

keywords = "Chlorpromazine, Cytochrome d, Cytochrome o, D-Lactate oxidase, Electron transport chain, Myxothiazol, Zymomonas mobilis",

author = "Uldis Kalnenieks and Nina Galinina and Stefanie Bringer-Meyer and Poole, \{Robert K.\}",

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doi = "10.1016/S0378-1097(98)00424-8",

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TY - JOUR

T1 - Membrane D-lactate oxidase in Zymomonas mobilis

T2 - Evidence for a branched respiratory chain

AU - Kalnenieks, Uldis

AU - Galinina, Nina

AU - Bringer-Meyer, Stefanie

AU - Poole, Robert K.

PY - 1998/11/1

Y1 - 1998/11/1

N2 - 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. Copyright (C) 1998 Federation of European Microbiological Societies.

AB - 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. Copyright (C) 1998 Federation of European Microbiological Societies.

KW - Chlorpromazine

KW - Cytochrome d

KW - Cytochrome o

KW - D-Lactate oxidase

KW - Electron transport chain

KW - Myxothiazol

KW - Zymomonas mobilis

UR - https://www.scopus.com/pages/publications/0032213815

U2 - 10.1016/S0378-1097(98)00424-8

DO - 10.1016/S0378-1097(98)00424-8

M3 - Article

C2 - 9812368

AN - SCOPUS:0032213815

SN - 0378-1097

VL - 168

SP - 91

EP - 97

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

IS - 1

ER -

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

Abstract

Keywords

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