(Q35082932)

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The structure of Wolinella succinogenes quinol: fumarate reductase and its relevance to the superfamily of succinate: quinone oxidoreductases

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Europe PubMed Central

PubMed publication ID

6 August 2017

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Europe PubMed Central

The structure of Wolinella succinogenes quinol: fumarate reductase and its relevance to the superfamily of succinate: quinone oxidoreductases (English)

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Europe PubMed Central

PubMed publication ID

6 August 2017

author name string

C Roy D Lancaster

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Europe PubMed Central

PubMed publication ID

6 August 2017

publication date

1 January 2003

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Europe PubMed Central

PubMed publication ID

6 August 2017

Advances in Protein Chemistry

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Europe PubMed Central

PubMed publication ID

6 August 2017

63

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Europe PubMed Central

PubMed publication ID

6 August 2017

131-149

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Sequence analysis of subunits of the membrane-bound nitrate reductase from a denitrifying bacterium: the integral membrane subunit provides a prototype for the dihaem electron-carrying arm of a redox loop

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Reconstitution of coupled fumarate respiration in liposomes by incorporating the electron transport enzymes isolated from Wolinella succinogenes

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The unusual iron sulfur composition of the Acidianus ambivalens succinate dehydrogenase complex

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Identification of histidine residues in Wolinella succinogenes hydrogenase that are essential for menaquinone reduction by H2.

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Succinate: quinone oxidoreductases. Variations on a conserved theme

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A structural model for the membrane-integral domain of succinate: quinone oxidoreductases.

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The trinuclear iron-sulfur cluster S3 in Bacillus subtilis succinate:menaquinone reductase; effects of a mutation in the putative cluster ligation motif on enzyme activity and EPR properties.

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Respiration without O2

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Structure of the Escherichia coli fumarate reductase respiratory complex

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Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site

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Molecular basis of proton motive force generation: structure of formate dehydrogenase-N

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The covalently bound flavin ofVibrio succinogenessuccinate dehydrogenase

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Wolinella succinogenes fumarate reductase contains a dihaem cytochrome b.

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Fumarate as terminal acceptor of phosphorylative electron transport

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Fumarate respiration of Wolinella succinogenes: enzymology, energetics and coupling mechanism

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Succinate:quinone oxidoreductases--what can we learn from Wolinella succinogenes quinol:fumarate reductase?

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Succinate:quinone oxidoreductases: an overview

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Wolinella succinogenes quinol:fumarate reductase-2.2-A resolution crystal structure and the E-pathway hypothesis of coupled transmembrane proton and electron transfer

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Succinate: quinone oxidoreductases: new insights from X-ray crystal structures

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The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB

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Succinate:quinone oxidoreductases from epsilon-proteobacteria.

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Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution

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A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction

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The fumarate reductase operon of Wolinella succinogenes. Sequence and expression of the frdA and frdB genes

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Reactivity of the Bacillus subtilis succinate dehydrogenase complex with quinones.

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Quinol:fumarate oxidoreductases and succinate:quinone oxidoreductases: phylogenetic relationships, metal centres and membrane attachment

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Identifiers

10.1016/S0065-3233(03)63006-8

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

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