关于 NADH-醌氧化还原酶（复合物 I）中质子泵的直接和间接机制的新假说。
A new hypothesis on the simultaneous direct and indirect proton pump mechanisms in NADH-quinone oxidoreductase (complex I).
机构信息
Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA.
出版信息
FEBS Lett. 2010 Oct 8;584(19):4131-7. doi: 10.1016/j.febslet.2010.08.039. Epub 2010 Sep 15.
Abstract
Recently, Sazanov's group reported the X-ray structure of whole complex I [Nature, 465, 441 (2010)], which presented a strong clue for a "piston-like" structure as a key element in an "indirect" proton pump. We have studied the NuoL subunit which has a high sequence similarity to Na(+)/H(+) antiporters, as do the NuoM and N subunits. We constructed 27 site-directed NuoL mutants. Our data suggest that the H(+)/e(-) stoichiometry seems to have decreased from (4H(+)/2e(-)) in the wild-type to approximately (3H(+)/2e(-)) in NuoL mutants. We propose a revised hypothesis that each of the "direct" and the "indirect" proton pumps transports 2H(+) per 2e(-).
摘要
最近，Sazanov 小组报道了完整的复合物 I 的 X 射线结构[《自然》，465，441（2010）]，这为“活塞样”结构作为“间接”质子泵的关键元件提供了一个强有力的线索。我们研究了 NuoL 亚基，它与 Na(+)/H(+)反向转运蛋白具有很高的序列相似性，NuoM 和 N 亚基也是如此。我们构建了 27 个定点 NuoL 突变体。我们的数据表明，H(+)/e(-)的比例似乎从野生型的（4H(+)/2e(-)）降低到 NuoL 突变体的约（3H(+)/2e(-)）。我们提出了一个修正的假说，即“直接”和“间接”质子泵每 2e(-)转运 2H(+)。
相似文献
1
A new hypothesis on the simultaneous direct and indirect proton pump mechanisms in NADH-quinone oxidoreductase (complex I).
FEBS Lett. 2010 Oct 8;584(19):4131-7. doi: 10.1016/j.febslet.2010.08.039. Epub 2010 Sep 15.
2
Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH:ubiquinone oxidoreductase (Complex I).
Biochim Biophys Acta. 2008 Sep;1777(9):1166-72. doi: 10.1016/j.bbabio.2008.06.001. Epub 2008 Jun 9.
3
The membrane subunit NuoL(ND5) is involved in the indirect proton pumping mechanism of Escherichia coli complex I.
J Biol Chem. 2010 Dec 10;285(50):39070-8. doi: 10.1074/jbc.M110.157826. Epub 2010 Sep 7.
4
Asp563 of the horizontal helix of subunit NuoL is involved in proton translocation by the respiratory complex I.
FEBS Lett. 2012 Mar 23;586(6):699-704. doi: 10.1016/j.febslet.2012.01.056. Epub 2012 Feb 3.
5
The C-terminally truncated NuoL subunit (ND5 homologue) of the Na+-dependent complex I from Escherichia coli transports Na+.
J Biol Chem. 2003 Jul 18;278(29):26817-22. doi: 10.1074/jbc.M301682200. Epub 2003 May 10.
6
The location of NuoL and NuoM subunits in the membrane domain of the Escherichia coli complex I: implications for the mechanism of proton pumping.
J Biol Chem. 2003 Oct 31;278(44):43114-20. doi: 10.1074/jbc.M308247200. Epub 2003 Aug 15.
7
Roles of subunit NuoL in the proton pumping coupling mechanism of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli.
J Biochem. 2016 Oct;160(4):205-215. doi: 10.1093/jb/mvw027. Epub 2016 Apr 26.
8
Probing the mechanistic role of the long α-helix in subunit L of respiratory Complex I from Escherichia coli by site-directed mutagenesis.
Mol Microbiol. 2011 Dec;82(5):1086-95. doi: 10.1111/j.1365-2958.2011.07883.x. Epub 2011 Nov 7.
9
Constraining the Lateral Helix of Respiratory Complex I by Cross-linking Does Not Impair Enzyme Activity or Proton Translocation.
J Biol Chem. 2015 Aug 21;290(34):20761-20773. doi: 10.1074/jbc.M115.660381. Epub 2015 Jul 1.
10
Cation transport by the respiratory NADH:quinone oxidoreductase (complex I): facts and hypotheses.
Biochem Soc Trans. 2013 Oct;41(5):1280-7. doi: 10.1042/BST20130024.
引用本文的文献
1
Molecular Dynamics Simulation of T10609C and C10676G Mutations of Mitochondrial Gene Associated With Proton Translocation in Type 2 Diabetes Mellitus and Cataract Patients.
Bioinform Biol Insights. 2020 Dec 16;14:1177932220978672. doi: 10.1177/1177932220978672. eCollection 2020.
2
Long-range proton-coupled electron transfer in biological energy conversion: towards mechanistic understanding of respiratory complex I.
J R Soc Interface. 2018 Apr;15(141). doi: 10.1098/rsif.2017.0916.
3
Mrp Antiporters Have Important Roles in Diverse Bacteria and Archaea.
Front Microbiol. 2017 Nov 23;8:2325. doi: 10.3389/fmicb.2017.02325. eCollection 2017.
4
Symmetry-related proton transfer pathways in respiratory complex I.
Proc Natl Acad Sci U S A. 2017 Aug 1;114(31):E6314-E6321. doi: 10.1073/pnas.1706278114. Epub 2017 Jul 17.
5
A giant molecular proton pump: structure and mechanism of respiratory complex I.
Nat Rev Mol Cell Biol. 2015 Jun;16(6):375-88. doi: 10.1038/nrm3997. Epub 2015 May 20.
6
On the mechanism of respiratory complex I.
J Bioenerg Biomembr. 2014 Aug;46(4):255-68. doi: 10.1007/s10863-014-9566-8. Epub 2014 Jul 15.
7
Randomly selected suppressor mutations in genes for NADH : quinone oxidoreductase-1, which rescue motility of a Salmonella ubiquinone-biosynthesis mutant strain.
Microbiology (Reading). 2014 Jun;160(Pt 6):1075-1086. doi: 10.1099/mic.0.075945-0. Epub 2014 Apr 1.
8
Crystal structure of the entire respiratory complex I.
Nature. 2013 Feb 28;494(7438):443-8. doi: 10.1038/nature11871. Epub 2013 Feb 17.
9
Mitochondrial complex I and cell death: a semi-automatic shotgun model.
Cell Death Dis. 2011 Oct 27;2(10):e222. doi: 10.1038/cddis.2011.107.
10
Positive Darwinian selection in the piston that powers proton pumps in complex I of the mitochondria of Pacific salmon.
PLoS One. 2011;6(9):e24127. doi: 10.1371/journal.pone.0024127. Epub 2011 Sep 28.
本文引用的文献
1
Possible roles of two quinone molecules in direct and indirect proton pumps of bovine heart NADH-quinone oxidoreductase (complex I).
Biochim Biophys Acta. 2010 Dec;1797(12):1891-3. doi: 10.1016/j.bbabio.2010.06.010. Epub 2010 Jun 25.
2
The architecture of respiratory complex I.
Nature. 2010 May 27;465(7297):441-5. doi: 10.1038/nature09066.
3
Structural biology: Piston drives a proton pump.
Nature. 2010 May 27;465(7297):428-9. doi: 10.1038/465428a.
4
The ND2 subunit is labeled by a photoaffinity analogue of asimicin, a potent complex I inhibitor.
FEBS Lett. 2010 Mar 5;584(5):883-8. doi: 10.1016/j.febslet.2010.01.004. Epub 2010 Jan 13.
5
Characterization of the inhibitor binding site in mitochondrial NADH-ubiquinone oxidoreductase by photoaffinity labeling using a quinazoline-type inhibitor.
Biochemistry. 2009 Feb 3;48(4):688-98. doi: 10.1021/bi8019977.
6
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.
Biofactors. 2008;32(1-4):13-22. doi: 10.1002/biof.5520320103.
7
Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH:ubiquinone oxidoreductase (Complex I).
Biochim Biophys Acta. 2008 Sep;1777(9):1166-72. doi: 10.1016/j.bbabio.2008.06.001. Epub 2008 Jun 9.
8
Exploring the inhibitor binding pocket of respiratory complex I.
Biochim Biophys Acta. 2008 Jul-Aug;1777(7-8):660-5. doi: 10.1016/j.bbabio.2008.04.033. Epub 2008 Apr 30.
9
Were there any "misassignments" among iron-sulfur clusters N4, N5 and N6b in NADH-quinone oxidoreductase (complex I)?
Biochim Biophys Acta. 2008 Jul-Aug;1777(7-8):703-10. doi: 10.1016/j.bbabio.2008.04.032. Epub 2008 Apr 30.
10
Mitochondrial Complex I superoxide production is attenuated by uncoupling.
Int J Biochem Cell Biol. 2008;40(10):2098-109. doi: 10.1016/j.biocel.2008.02.007. Epub 2008 Feb 16.
Zotero 插件