Structure-function studies of iron-sulfur clusters and semiquinones in the NADH-Q oxidoreductase segment of the respiratory chain (Q47729468)

5 February 2018

review article

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title

Structure-function studies of iron-sulfur clusters and semiquinones in the NADH-Q oxidoreductase segment of the respiratory chain (English)

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5 February 2018

author name string

T Ohnishi

1

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5 February 2018

V D Sled

2

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5 February 2018

T Yano

3

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5 February 2018

T Yagi

4

1 reference

5 February 2018

D S Burbaev

5

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5 February 2018

A D Vinogradov

6

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5 February 2018

publication date

1 June 1998

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5 February 2018

Biochimica et Biophysica Acta

published in

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5 February 2018

volume

1365

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5 February 2018

issue

1-2

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5 February 2018

page(s)

301-308

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5 February 2018

NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain.

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Modular evolution of the respiratory NADH:ubiquinone oxidoreductase and the origin of its modules

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Q-band ENDOR spectra of the Rieske protein from Rhodobacter capsulatus ubiquinol-cytochrome c oxidoreductase show two histidines coordinated to the iron-sulfur [2Fe-2S] cluster

7 January 2021

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Electron spin echo envelope modulation spectroscopy supports the suggested coordination of two histidine ligands to the Rieske Fe-S centers of the cytochrome b6f complex of spinach and the cytochrome bc1 complexes of Rhodospirillum rubrum, Rhodobact

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7 January 2021

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10.1016/S0005-2728(98)00082-6

7 January 2021

Identifiers

DOI

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5 February 2018

release_bq6eltspencolnbr3z6zozjpqm

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5 February 2018