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Redox-linked proton translocation by NADH-ubiquinone reductase (complex I).

作者信息

Weiss H, Friedrich T

机构信息

Institut für Biochemie der Universität Düsseldorf, Germany.

出版信息

J Bioenerg Biomembr. 1991 Oct;23(5):743-54. doi: 10.1007/BF00785999.

DOI:10.1007/BF00785999

PMID:1660872

Abstract

摘要

相似文献

Redox-linked proton translocation by NADH-ubiquinone reductase (complex I).

J Bioenerg Biomembr. 1991 Oct;23(5):743-54. doi: 10.1007/BF00785999.

Search for novel redox groups in mitochondrial NADH:ubiquinone oxidoreductase (complex I) by diode array UV/VIS spectroscopy.

Biofactors. 1998;8(3-4):177-86. doi: 10.1002/biof.5520080303.

Characterization of a membrane fragment of respiratory chain complex I from Neurospora crassa. Insights on the topology of the ubiquinone-binding site.

Int J Biochem. 1994 Apr;26(4):505-10. doi: 10.1016/0020-711x(94)90007-8.

From NADH to ubiquinone in Neurospora mitochondria.

Biochim Biophys Acta. 2002 Sep 10;1555(1-3):187-91. doi: 10.1016/s0005-2728(02)00276-1.

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

Biochim Biophys Acta. 1997 Jan 16;1318(1-2):79-91. doi: 10.1016/s0005-2728(96)00141-7.

Complex I from the fungus Neurospora crassa.

Biochim Biophys Acta. 1998 May 6;1364(2):89-100. doi: 10.1016/s0005-2728(98)00020-6.

Identification of the ubiquinone-binding site of NADH:ubiquinone oxidoreductase (complex I) from Neurospora crassa.

Biochemistry. 1992 Nov 24;31(46):11413-9. doi: 10.1021/bi00161a020.

Proton translocation in the respiratory chain involving ubiquinone--a hypothetical semiquinone switch mechanism for complex I.

Biofactors. 1999;9(2-4):95-101. doi: 10.1002/biof.5520090203.

Assembly of NADH: ubiquinone reductase (complex I) in Neurospora mitochondria. Independent pathways of nuclear-encoded and mitochondrially encoded subunits.

J Mol Biol. 1990 Jun 20;213(4):845-57. doi: 10.1016/S0022-2836(05)80268-2.

Kinetics, control, and mechanism of ubiquinone reduction by the mammalian respiratory chain-linked NADH-ubiquinone reductase.

J Bioenerg Biomembr. 1993 Aug;25(4):367-75. doi: 10.1007/BF00762462.

引用本文的文献

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

Biochim Biophys Acta. 2008 Jul-Aug;1777(7-8):729-34. doi: 10.1016/j.bbabio.2008.04.014. Epub 2008 Apr 18.

EPR characterization of ubisemiquinones and iron-sulfur cluster N2, central components of the energy coupling in the NADH-ubiquinone oxidoreductase (complex I) in situ.

J Bioenerg Biomembr. 2002 Jun;34(3):193-208. doi: 10.1023/a:1016083419979.

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

J Bioenerg Biomembr. 2002 Apr;34(2):89-94. doi: 10.1023/a:1015119808009.

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

J Bioenerg Biomembr. 2002 Feb;34(1):11-9. doi: 10.1023/a:1013862502185.

Structure-activity analysis of fluorinated 1-N-arylamino-1-arylmethanephosphonic acid esters as inhibitors of the NADH:ubiquinone oxidoreductase (complex I).

J Comput Aided Mol Des. 1996 Apr;10(2):100-6. doi: 10.1007/BF00402818.

The specificity of mitochondrial complex I for ubiquinones.

Biochem J. 1996 Jan 1;313 ( Pt 1)(Pt 1):327-34. doi: 10.1042/bj3130327.

Kinetics, control, and mechanism of ubiquinone reduction by the mammalian respiratory chain-linked NADH-ubiquinone reductase.

J Bioenerg Biomembr. 1993 Aug;25(4):367-75. doi: 10.1007/BF00762462.

Attempts to define distinct parts of NADH:ubiquinone oxidoreductase (complex I).

J Bioenerg Biomembr. 1993 Aug;25(4):331-7. doi: 10.1007/BF00762458.

本文引用的文献

Studies on the interaction of arylazido-beta-alanyl NAD+ with the mitochondrial NADH dehydrogenase.

J Biol Chem. 1981 Aug 25;256(16):8318-23.

The ATP-to-oxygen stoichiometries of oxidative phosphorylation by rat liver mitochondria. An analysis of ADP-induced oxygen jumps by linear nonequilibrium thermodynamics.

J Biol Chem. 1984 Nov 10;259(21):13123-30.

Activation of site I redox-driven H+ pump by exogenous quinones in intact mitochondria.

J Biol Chem. 1982 Apr 25;257(8):4106-13.

Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone.

FEBS Lett. 1984 Apr 24;169(2):300-4. doi: 10.1016/0014-5793(84)80338-5.

Thermodynamic limits to the ATP/site stoichiometries of oxidative phosphorylation by rat liver mitochondria.

J Biol Chem. 1984 Mar 10;259(5):3058-63.

New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria.

Biochim Biophys Acta. 1982 Dec 31;683(3-4):245-77. doi: 10.1016/0304-4173(82)90003-9.

Evidence of an ubisemiquinone radical(s) from the NADH-ubiquinone reductase of the mitochondrial respiratory chain.

J Biol Chem. 1983 Jan 10;258(1):352-8.

Proton electrochemical gradients and energy-transduction processes.

Annu Rev Biochem. 1982;51:185-217. doi: 10.1146/annurev.bi.51.070182.001153.

An analysis of some thermodynamic properties of iron-sulphur centres in site I of mitochondria.

Biochem J. 1980 Jan 15;186(1):111-7. doi: 10.1042/bj1860111.

Energetics of ATP-driven reverse electron transfer from cytochrome c to fumarate and from succinate to NAD in submitochondrial particles.

Biochemistry. 1984 Jul 3;23(14):3341-5. doi: 10.1021/bi00309a035.

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Redox-linked proton translocation by NADH-ubiquinone reductase (complex I).

作者信息

Weiss H, Friedrich T

机构信息

Institut für Biochemie der Universität Düsseldorf, Germany.

出版信息

J Bioenerg Biomembr. 1991 Oct;23(5):743-54. doi: 10.1007/BF00785999.

DOI:10.1007/BF00785999

PMID:1660872

Abstract

摘要

相似文献

Redox-linked proton translocation by NADH-ubiquinone reductase (complex I).

J Bioenerg Biomembr. 1991 Oct;23(5):743-54. doi: 10.1007/BF00785999.

Search for novel redox groups in mitochondrial NADH:ubiquinone oxidoreductase (complex I) by diode array UV/VIS spectroscopy.

Biofactors. 1998;8(3-4):177-86. doi: 10.1002/biof.5520080303.

Characterization of a membrane fragment of respiratory chain complex I from Neurospora crassa. Insights on the topology of the ubiquinone-binding site.

Int J Biochem. 1994 Apr;26(4):505-10. doi: 10.1016/0020-711x(94)90007-8.

From NADH to ubiquinone in Neurospora mitochondria.

Biochim Biophys Acta. 2002 Sep 10;1555(1-3):187-91. doi: 10.1016/s0005-2728(02)00276-1.

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

Biochim Biophys Acta. 1997 Jan 16;1318(1-2):79-91. doi: 10.1016/s0005-2728(96)00141-7.

Complex I from the fungus Neurospora crassa.

Biochim Biophys Acta. 1998 May 6;1364(2):89-100. doi: 10.1016/s0005-2728(98)00020-6.

Identification of the ubiquinone-binding site of NADH:ubiquinone oxidoreductase (complex I) from Neurospora crassa.

Biochemistry. 1992 Nov 24;31(46):11413-9. doi: 10.1021/bi00161a020.

Proton translocation in the respiratory chain involving ubiquinone--a hypothetical semiquinone switch mechanism for complex I.

Biofactors. 1999;9(2-4):95-101. doi: 10.1002/biof.5520090203.

Assembly of NADH: ubiquinone reductase (complex I) in Neurospora mitochondria. Independent pathways of nuclear-encoded and mitochondrially encoded subunits.

J Mol Biol. 1990 Jun 20;213(4):845-57. doi: 10.1016/S0022-2836(05)80268-2.

Kinetics, control, and mechanism of ubiquinone reduction by the mammalian respiratory chain-linked NADH-ubiquinone reductase.

J Bioenerg Biomembr. 1993 Aug;25(4):367-75. doi: 10.1007/BF00762462.

引用本文的文献

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

Biochim Biophys Acta. 2008 Jul-Aug;1777(7-8):729-34. doi: 10.1016/j.bbabio.2008.04.014. Epub 2008 Apr 18.

EPR characterization of ubisemiquinones and iron-sulfur cluster N2, central components of the energy coupling in the NADH-ubiquinone oxidoreductase (complex I) in situ.

J Bioenerg Biomembr. 2002 Jun;34(3):193-208. doi: 10.1023/a:1016083419979.

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

J Bioenerg Biomembr. 2002 Apr;34(2):89-94. doi: 10.1023/a:1015119808009.

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

J Bioenerg Biomembr. 2002 Feb;34(1):11-9. doi: 10.1023/a:1013862502185.

Structure-activity analysis of fluorinated 1-N-arylamino-1-arylmethanephosphonic acid esters as inhibitors of the NADH:ubiquinone oxidoreductase (complex I).

J Comput Aided Mol Des. 1996 Apr;10(2):100-6. doi: 10.1007/BF00402818.

The specificity of mitochondrial complex I for ubiquinones.

Biochem J. 1996 Jan 1;313 ( Pt 1)(Pt 1):327-34. doi: 10.1042/bj3130327.

Kinetics, control, and mechanism of ubiquinone reduction by the mammalian respiratory chain-linked NADH-ubiquinone reductase.

J Bioenerg Biomembr. 1993 Aug;25(4):367-75. doi: 10.1007/BF00762462.

Attempts to define distinct parts of NADH:ubiquinone oxidoreductase (complex I).

J Bioenerg Biomembr. 1993 Aug;25(4):331-7. doi: 10.1007/BF00762458.

本文引用的文献

Studies on the interaction of arylazido-beta-alanyl NAD+ with the mitochondrial NADH dehydrogenase.

J Biol Chem. 1981 Aug 25;256(16):8318-23.

The ATP-to-oxygen stoichiometries of oxidative phosphorylation by rat liver mitochondria. An analysis of ADP-induced oxygen jumps by linear nonequilibrium thermodynamics.

J Biol Chem. 1984 Nov 10;259(21):13123-30.

Activation of site I redox-driven H+ pump by exogenous quinones in intact mitochondria.

J Biol Chem. 1982 Apr 25;257(8):4106-13.

Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone.

FEBS Lett. 1984 Apr 24;169(2):300-4. doi: 10.1016/0014-5793(84)80338-5.

Thermodynamic limits to the ATP/site stoichiometries of oxidative phosphorylation by rat liver mitochondria.

J Biol Chem. 1984 Mar 10;259(5):3058-63.

New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria.

Biochim Biophys Acta. 1982 Dec 31;683(3-4):245-77. doi: 10.1016/0304-4173(82)90003-9.

Evidence of an ubisemiquinone radical(s) from the NADH-ubiquinone reductase of the mitochondrial respiratory chain.

J Biol Chem. 1983 Jan 10;258(1):352-8.

Proton electrochemical gradients and energy-transduction processes.

Annu Rev Biochem. 1982;51:185-217. doi: 10.1146/annurev.bi.51.070182.001153.

An analysis of some thermodynamic properties of iron-sulphur centres in site I of mitochondria.

Biochem J. 1980 Jan 15;186(1):111-7. doi: 10.1042/bj1860111.

Energetics of ATP-driven reverse electron transfer from cytochrome c to fumarate and from succinate to NAD in submitochondrial particles.

Biochemistry. 1984 Jul 3;23(14):3341-5. doi: 10.1021/bi00309a035.