Literature DB >> 11860176

Steady-state kinetics of NADH:coenzyme Q oxidoreductase isolated from bovine heart mitochondria.

Yumiko Nakashima1, Kyoko Shinzawa-Itoh, Kenji Watanabe, Kazuki Naoki, Nobuko Hano, Shinya Yoshikawa.   

Abstract

Steady-state kinetics of the bovine heart NADH:coenzyme Q oxidoreductase reaction were analyzed in the presence of various concentrations of NADH and coenzyme Q with one isoprenoid unit (Q1). Product inhibitions by NAD+ and reduced coenzyme Q1 were also determined. These results show an ordered sequential mechanism in which the order of substrate binding and product release is Q1-NADH-NAD+-Q1H2. It has been widely accepted that the NADH binding site is likely to be on the top of a large extramembrane portion protruding to the matrix space while the Q1 binding site is near the transmembrane moiety. The rigorous controls for substrate binding and product release are indicative of a strong, long range interaction between NADH and Q1 binding sites.

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Year:  2002        PMID： 11860176     DOI： 10.1023/a:1013862502185

Source DB:  PubMed          Journal:  J Bioenerg Biomembr        ISSN： 0145-479X            Impact factor:   2.945


  34 in total

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  18 in total

1.  The second coenzyme Q1 binding site of bovine heart NADH: coenzyme Q oxidoreductase.

Authors:  Yumiko Nakashima; Kyoko Shinzawa-Itoh; Kenji Watanabe; Kazuki Naoki; Nobuko Hano; Shinya Yoshikawa
Journal:  J Bioenerg Biomembr       Date:  2002-04       Impact factor: 2.945

2.  Kinetics and regulation of mammalian NADH-ubiquinone oxidoreductase (Complex I).

Authors:  Xuewen Chen; Feng Qi; Ranjan K Dash; Daniel A Beard
Journal:  Biophys J       Date:  2010-09-08       Impact factor: 4.033

3.  Specific modification of a Na+ binding site in NADH:quinone oxidoreductase from Klebsiella pneumoniae with dicyclohexylcarbodiimide.

Authors:  Irini Vgenopoulou; Anja C Gemperli; Julia Steuber
Journal:  J Bacteriol       Date:  2006-05       Impact factor: 3.490

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

Authors:  Vera G Grivennikova; Alexander B Kotlyar; Joel S Karliner; Gary Cecchini; Andrei D Vinogradov
Journal:  Biochemistry       Date:  2007-08-31       Impact factor: 3.162

Review 5.  Mammalian NADH:ubiquinone oxidoreductase (Complex I) and nicotinamide nucleotide transhydrogenase (Nnt) together regulate the mitochondrial production of H₂O₂--implications for their role in disease, especially cancer.

Authors:  Simon P J Albracht; Alfred J Meijer; Jan Rydström
Journal:  J Bioenerg Biomembr       Date:  2011-09-01       Impact factor: 2.945

6.  Isoflurane selectively inhibits distal mitochondrial complex I in Caenorhabditis elegans.

Authors:  Ernst-Bernhard Kayser; Wichit Suthammarak; Phil G Morgan; Margaret M Sedensky
Journal:  Anesth Analg       Date:  2011-04-05       Impact factor: 5.108

7.  Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli.

Authors:  Michael A Moxley; John J Tanner; Donald F Becker
Journal:  Arch Biochem Biophys       Date:  2011-10-25       Impact factor: 4.013

8.  Functional role of coenzyme Q in the energy coupling of NADH-CoQ oxidoreductase (Complex I): stabilization of the semiquinone state with the application of inside-positive membrane potential to proteoliposomes.

Authors:  Tomoko Ohnishi; S Tsuyoshi Ohnishi; Kyoko Shinzawa-Ito; Shinya Yoshikawa
Journal:  Biofactors       Date:  2008       Impact factor: 6.113

Review 9.  NADH/NAD+ interaction with NADH: ubiquinone oxidoreductase (complex I).

Authors:  Andrei D Vinogradov
Journal:  Biochim Biophys Acta       Date:  2008-04-18

10.  Effect of the side chain structure of coenzyme Q on the steady state kinetics of bovine heart NADH: coenzyme Q oxidoreductase.

Authors:  Nobuko Hano; Yumiko Nakashima; Kyoko Shinzawa-Itoh; Shinya Yoshikawa
Journal:  J Bioenerg Biomembr       Date:  2003-06       Impact factor: 2.945
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