Bacterial NADH-quinone oxidoreductases: Iron-sulfur clusters and related problems

Vladimir D. Sled'; Thorsten Friedrich; Hans Leif; Hanns Weiss; Steven W. Meinhardt; Yoshihiro Fukumori; Melissa W. Calhoun; Robert B. Gennis; Tomoko Ohnishi

doi:10.1007/BF00762460

Bacterial NADH-quinone oxidoreductases: Iron-sulfur clusters and related problems

Vladimir D. Sled', Thorsten Friedrich, Hans Leif, Hanns Weiss, Steven W. Meinhardt, Yoshihiro Fukumori, Melissa W. Calhoun, Robert B. Gennis, Tomoko Ohnishi

Biochemistry

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

Abstract

Many bacteria contain proton-translocating membrane-bound NADH-quinone oxidoreductases (NDH-1), which demonstrate significant genetic, spectral, and kinetic similarity with their mitochondrial counterparts. This review is devoted to the comparative aspects of the ironsulfur cluster composition of NDH-1 from the most well-studied bacterial systems to date.:Paracoccus denitrificans, Rhodobacter sphaeroides, Escherichia coli, and Thermus thermophilus. These bacterial systems provide useful models for the study of coupling Site I and contain all the essential parts of the electron-transfer and proton-translocating machinery of their eukaryotic counterparts.

Original language	English (US)
Pages (from-to)	347-356
Number of pages	10
Journal	Journal of Bioenergetics and Biomembranes
Volume	25
Issue number	4
DOIs	https://doi.org/10.1007/BF00762460
State	Published - Aug 1993

Keywords

Escherichia coli
NADH-quinone oxidoreductase: NDH-1
Paracoccus denitrificans
Rhodobacter sphaeroides
Thermus thermophilus
iron-sulfur cluster

ASJC Scopus subject areas

Physiology
Cell Biology

Online availability

10.1007/BF00762460

Library availability

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abstract = "Many bacteria contain proton-translocating membrane-bound NADH-quinone oxidoreductases (NDH-1), which demonstrate significant genetic, spectral, and kinetic similarity with their mitochondrial counterparts. This review is devoted to the comparative aspects of the ironsulfur cluster composition of NDH-1 from the most well-studied bacterial systems to date.:Paracoccus denitrificans, Rhodobacter sphaeroides, Escherichia coli, and Thermus thermophilus. These bacterial systems provide useful models for the study of coupling Site I and contain all the essential parts of the electron-transfer and proton-translocating machinery of their eukaryotic counterparts.",

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AU - Sled', Vladimir D.

AU - Friedrich, Thorsten

AU - Leif, Hans

AU - Weiss, Hanns

AU - Meinhardt, Steven W.

AU - Fukumori, Yoshihiro

AU - Calhoun, Melissa W.

AU - Gennis, Robert B.

AU - Ohnishi, Tomoko

PY - 1993/8

Y1 - 1993/8

N2 - Many bacteria contain proton-translocating membrane-bound NADH-quinone oxidoreductases (NDH-1), which demonstrate significant genetic, spectral, and kinetic similarity with their mitochondrial counterparts. This review is devoted to the comparative aspects of the ironsulfur cluster composition of NDH-1 from the most well-studied bacterial systems to date.:Paracoccus denitrificans, Rhodobacter sphaeroides, Escherichia coli, and Thermus thermophilus. These bacterial systems provide useful models for the study of coupling Site I and contain all the essential parts of the electron-transfer and proton-translocating machinery of their eukaryotic counterparts.

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KW - Escherichia coli

KW - NADH-quinone oxidoreductase: NDH-1

KW - Paracoccus denitrificans

KW - Rhodobacter sphaeroides

KW - Thermus thermophilus

KW - iron-sulfur cluster

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Bacterial NADH-quinone oxidoreductases: Iron-sulfur clusters and related problems

Abstract

Keywords

ASJC Scopus subject areas

Online availability

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