Probing the ubiquinone reduction site in bovine mitochondrial complex I using a series of synthetic ubiquinones and inhibitors (Q34429389)

2 August 2017

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title

Probing the ubiquinone reduction site in bovine mitochondrial complex I using a series of synthetic ubiquinones and inhibitors (English)

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2 August 2017

Miyoshi H

1

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2 August 2017

1 June 2001

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Journal of Bioenergetics and Biomembranes

2 August 2017

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2 August 2017

33

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2 August 2017

3

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2 August 2017

223-231

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https://scigraph.springernature.com/pub.10.1023/a:1010735019982

2 August 2017

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The quinohemoprotein alcohol dehydrogenase of Gluconobacter suboxydans has ubiquinol oxidation activity at a site different from the ubiquinone reduction site

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Inhibition by capsaicin of NADH-quinone oxidoreductases is correlated with the presence of energy-coupling site 1 in various organisms

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Assay conditions for the mitochondrial NADH:coenzyme Q oxidoreductase

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The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I.

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12 December 2020

Steady-state kinetics of the reduction of coenzyme Q analogs by complex I (NADH:ubiquinone oxidoreductase) in bovine heart mitochondria and submitochondrial particles.

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12 December 2020

Probing the ubiquinone reduction site of mitochondrial complex I using novel cationic inhibitors

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12 December 2020

Identifiers

DOI

10.1023/A:1010735019982

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PubMed ID

11695832

Dimensions Publication ID

2 August 2017

0 references

1 reference

PubMed ID

11695832