Distinct forms of the haem o-Cu binuclear site of oxidised cytochrome bo from Escherichia coli. Evidence from optical and EPR spectroscopy. (Q54660570)

2 June 2018

title

Distinct forms of the haem o-Cu binuclear site of oxidised cytochrome bo from Escherichia coli. Evidence from optical and EPR spectroscopy. (English)

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2 June 2018

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N J Watmough

1

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M R Cheesman

2

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R B Gennis

3

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C Greenwood

4

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A J Thomson

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language of work or name

English

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publication date

1 March 1993

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2 June 2018

published in

FEBS Letters

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volume

319

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issue

1-2

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2 June 2018

page(s)

151-154

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2 June 2018

Potentiometric titration of cytochrome-bo type quinol oxidase of Escherichia coli: evidence for heme-heme and copper-heme interaction.

cites work

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Cloning of the cyo locus encoding the cytochrome o terminal oxidase complex of Escherichia coli

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Cytochrome bo from Escherichia coli: identification of haem ligands and reaction of the reduced enzyme with carbon monoxide

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Properties of a copper-containing cytochrome c1aa3 complex: a terminal oxidase of the extreme thermophile Thermus thermophilus HB8

21 January 2018

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Effect of high pH on the spectral and catalytic properties of beef heart cytochrome oxidase

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Conformational substates of bovine heart cytochrome c oxidase: the modified Volpe-Caughey variant

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The formate complex of the cytochrome bo quinol oxidase of Escherichia coli exhibits a 'g = 12' EPR feature analogous to that of 'slow' cytochrome oxidase

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21 January 2018

Identifiers

DOI

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2 June 2018

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2 June 2018