Literature DB >> 11712120

Flavin and ubiquinone of mitochondrial NADH dehydrogenase are not involved in the electron transfer to artificial acceptors.

A S Lomtev1, I V Sharova, N L Vekshin.   

Abstract

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Year:  2001        PMID： 11712120     DOI： 10.1023/a:1018879521780

Source DB:  PubMed          Journal:  Dokl Biochem Biophys        ISSN： 1607-6729            Impact factor:   0.788


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  8 in total

1.  [Light-dependent phosphorylation in mitochondria].

Authors:  I L Vekshin
Journal:  Mol Biol (Mosk)       Date:  1991 Jan-Feb

Review 2.  Catalytic properties of the mitochondrial NADH-ubiquinone oxidoreductase (complex I) and the pseudo-reversible active/inactive enzyme transition.

Authors:  A D Vinogradov
Journal:  Biochim Biophys Acta       Date:  1998-05-06

Review 3.  Proton-translocation by membrane-bound NADH:ubiquinone-oxidoreductase (complex I) through redox-gated ligand conduction.

Authors:  U Brandt
Journal:  Biochim Biophys Acta       Date:  1997-01-16

4.  Chaotropic resolution of high molecular weight (type I) NADH dehydrogenase, and reassociation of flavin-rich (type II) and flavin-poor subunits.

Authors:  G Dooijewaard; E C Slater; P J van Dijk; G J de Bruin
Journal:  Biochim Biophys Acta       Date:  1978-09-07

5.  [Spectrophotometric determination of the quantity of protein in standard biological suspensions].

Authors:  N L Vekshin
Journal:  Nauchnye Doki Vyss Shkoly Biol Nauki       Date:  1988

Review 6.  The mitochondrial electron transport and oxidative phosphorylation system.

Authors:  Y Hatefi
Journal:  Annu Rev Biochem       Date:  1985       Impact factor: 23.643

7.  Structural analysis of NADH: ubiquinone oxidoreductase from bovine heart mitochondria.

Authors:  J E Walker; J M Skehel; S K Buchanan
Journal:  Methods Enzymol       Date:  1995       Impact factor: 1.600

8.  Reductive inactivation of the mitochondrial three subunit NADH dehydrogenase.

Authors:  V D Sled; A D Vinogradov
Journal:  Biochim Biophys Acta       Date:  1993-07-05
  8 in total

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