Redox-dependent change of nucleotide affinity to the active site of the mammalian complex I.

Redox-dependent change of nucleotide affinity to the active site of the mammalian complex I. Research Abstract Details 

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Redox-dependent change of nucleotide affinity to the active site of the mammalian complex I. Abstract Text:

Vera G Grivennikova,Alexander B Kotlyar,Joel S Karliner,Gary Cecchini,Andrei D Vinogradov,Vera G Grivennikova,Alexander B Kotlyar,Joel S Karliner,Gary Cecchini,Andrei D Vinogradov,

A very potent and specific inhibitor of mitochondrial NADH:ubiquinone oxidoreductase (complex I), a derivative of NADH (NADH-OH) has recently been discovered (Kotlyar, A. B., Karliner, J. S., and Cecchini, G. (2005) FEBS Lett. 579, 4861-4866). Here we present a quantitative analysis of the interaction of NADH-OH and other nucleotides with oxidized and reduced complex I in tightly coupled submitochondrial particles. Both the rate of the NADH-OH binding and its affinity to complex I are strongly decreased in the presence of succinate. The effect of succinate is completely reversed by rotenone, antimycin A, and uncoupler. The relative affinity of ADP-ribose, a competitive inhibitor of NADH oxidation, is also shown to be significantly affected by enzyme reduction (KD of 30 and 500 microM for oxidized and the succinate-reduced enzyme, respectively). Binding of NADH-OH is shown to abolish the succinate-supported superoxide generation by complex I. Gradual inhibition of the rotenone-sensitive uncoupled NADH oxidase and the reverse electron transfer activities by NADH-OH yield the same final titration point (approximately 0.1 nmol/mg of protein). The titration of NADH oxidase appears as a straight line, whereas the titration of the reverse reaction appears as a convex curve. Possible models to explain the different titration patterns for the forward and reverse reactions are briefly discussed.

Redox-dependent change of nucleotide affinity to the active site of the mammalian complex I. Publishing Authors By Initials

VG Grivennikova,AB Kotlyar,JS Karliner,G Cecchini,AD Vinogradov,VG Grivennikova,AB Kotlyar,JS Karliner,G Cecchini,AD Vinogradov,

For similar chemical actions and uses: pharmacologic actions: molecular mechanisms of pharmacological action: enzyme inhibitors: uncoupling agents research abstracts see: chemical actions and uses: pharmacologic actions: molecular mechanisms of pharmacological action: enzyme inhibitors: uncoupling agents research

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Redox-dependent change of nucleotide affinity to the active site of the mammalian complex I. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Biochemistry

VOLUME: 46

Page Numbers: 10971-8

Journal Abbreviation: Biochemistry

ISSN: 0006-2960

DAY: 31

MONTH: 08

YEAR: 2007

Redox-dependent change of nucleotide affinity to the active site of the mammalian complex I. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 370623

Redox-dependent change of nucleotide affinity to the active site of the mammalian complex I. Keywords Mesh Terms:

KEYWORDS: Uncoupling Agents

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Redox-dependent change of nucleotide affinity to the active site of the mammalian complex I. Information

Substance Name: Electron Transport Complex I

Registry Number: EC 1.6.5.3

Grant and Affiliation Information for Redox-dependent change of nucleotide affinity to the active site of the mammalian complex I.

AFFILIATION: Department of Biochemistry, School of Biology, Moscow State University, Moscow 119992, Russian Federation.

Country: United States

AGENCY: United States FIC

GRANT: R03 TW07825

ACRONYM: TW

MEDLINETA: Biochemistry

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