Dissociation of superoxide production by mitochondrial complex I from NAD(P)H redox state

被引:29
作者
Lambert, Adrian J. [1 ]
Buckingham, Julie A. [1 ]
Brand, Martin D. [1 ]
机构
[1] MRC, Dunn Human Nutr Unit, Cambridge CB2 0XY, England
基金
英国医学研究理事会; 英国惠康基金;
关键词
NADH : ubiquinone oxidoreductase; mitochondria; superoxide; NAD(P)H; hydrogen peroxide; reactive oxygen species;
D O I
10.1016/j.febslet.2008.04.030
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The relationship between the rate of superoxide production by complex I and NAD(P) H redox state was investigated in rat skeletal muscle mitochondria. A high rate of superoxide production was observed during succinate oxidation; the rate during pyruvate oxidation was over fourfold lower. However, the NAD(P) H pool was significantly less reduced during succinate oxidation than during pyruvate oxidation. We conclude that there is no unique relationship between superoxide production by complex I and the reduction state of the NAD(P) H pool. Our data suggest that less than 10% of the superoxide originates from the flavin site during reverse electron transport from succinate. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:1711 / 1714
页数:4
相关论文
共 21 条
  • [1] Mitochondrial superoxide: Production, biological effects, and activation of uncoupling proteins
    Brand, MD
    Affourtit, C
    Esteves, TC
    Green, K
    Lambert, AJ
    Miwa, S
    Pakay, JL
    Parker, N
    [J]. FREE RADICAL BIOLOGY AND MEDICINE, 2004, 37 (06) : 755 - 767
  • [2] Superoxide radical formation by pure complex I (NADH:Ubiquinone oxidoreductase) from Yarrowia lipolytica
    Galkin, A
    Brandt, U
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (34) : 30129 - 30135
  • [3] The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron-sulfur cluster N2
    Genova, ML
    Ventura, B
    Giuliano, G
    Bovina, C
    Formiggini, G
    Castelli, GP
    Lenaz, G
    [J]. FEBS LETTERS, 2001, 505 (03): : 364 - 368
  • [4] Dependence of H2O2 formation by rat heart mitochondria on substrate availability and donor age
    Hansford, RG
    Hogue, BA
    Mildaziene, V
    [J]. JOURNAL OF BIOENERGETICS AND BIOMEMBRANES, 1997, 29 (01) : 89 - 95
  • [5] RESPIRATORY CONTROL IN THE GLUCOSE PERFUSED HEART - A P-31 NMR AND NADH FLUORESCENCE STUDY
    KATZ, LA
    KORETSKY, AP
    BALABAN, RS
    [J]. FEBS LETTERS, 1987, 221 (02) : 270 - 276
  • [6] Characterization of superoxide-producing sites in isolated brain mitochondria
    Kudin, AP
    Bimpong-Buta, NYB
    Vielhaber, S
    Elger, CE
    Kunz, WS
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (06) : 4127 - 4135
  • [7] Complex I-mediated reactive oxygen species generation:: modulation by cytochrome c and NAD(P)+ oxidation-reduction state
    Kushnareva, Y
    Murphy, AN
    Andreyev, A
    [J]. BIOCHEMICAL JOURNAL, 2002, 368 : 545 - 553
  • [8] The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
    Kussmaul, Lothar
    Hirst, Judy
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (20) : 7607 - 7612
  • [9] Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    Lambert, AJ
    Brand, MD
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (38) : 39414 - 39420
  • [10] Superoxide production by NADH: ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane
    Lambert, AJ
    Brand, MD
    [J]. BIOCHEMICAL JOURNAL, 2004, 382 : 511 - 517