Conformation-specific crosslinking of mitochondrial complex I

被引:22
作者
Ciano, Margherita [1 ,4 ]
Fuszard, Matthew [2 ]
Heide, Heinrich [3 ]
Botting, Catherine H. [2 ]
Galkin, Alexander [1 ]
机构
[1] Queens Univ Belfast, Sch Biol Sci, Ctr Med Biol, Belfast BT9 7BL, Antrim, North Ireland
[2] Univ St Andrews, Sch Chem, BMS Annexe, St Andrews KY16 9ST, Fife, Scotland
[3] Goethe Univ Frankfurt, Fac Med, Mol Bioenerget Grp, D-60590 Frankfurt, Germany
[4] Univ Bologna, Dept Expt Evolutionary Biol, I-40126 Bologna, Italy
基金
英国惠康基金;
关键词
Mitochondrial complex I; A/D transition; ND3; subunit; 39 kDa subunit; NDUFA9; SPDP; Crosslinking; NADH-UBIQUINONE OXIDOREDUCTASE; ACTIVE-INACTIVE TRANSITION; SUBUNIT; IDENTIFICATION; PROTEINS; BINDING; DOMAIN; OXYGEN; STATE; KDA;
D O I
10.1016/j.febslet.2013.02.039
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
Complex I is the only component of the eukaryotic respiratory chain of which no high-resolution structure is yet available. A notable feature of mitochondrial complex I is the so-called active/deactive conformational transition of the idle enzyme from the active (A) to the de-active, (D) form. Using an amine-and sulfhydryl-reactive crosslinker of 6.8 angstrom length (SPDP) we found that in the D-form of complex I the ND3 subunit crosslinked to the 39 kDa (NDUFA9) subunit. These proteins could not be crosslinked in the A-form. Most likely, both subunits are closely located in the critical junction region connecting the peripheral hydrophilic domain to the membrane arm of the enzyme where the entrance path for substrate ubiquinone is and where energy transduction takes place. Structured summary of protein interactions: ND3 and NDUFA9 physically interact by cross-linking study (View interaction) (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码:867 / 872
页数:6
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