title: Chemical modifications of respiratory complex I for structural and functional studies.
abstract: Studies on chemical modifications of bacterial and mitochondrial complex I by synthetic chemical probes as well as endogenous chemicals have provided useful information on the structural and functional aspects of this enzyme. We herein reviewed recent studies that investigated chemical modifications of complex I by endogenous chemicals (e.g. Cys-S-nitrosation, Cys-S-glutathionylation, and Ser-O-phosphorylation) and synthetic reagents (e.g. Cys-SH modification by SH-reagents and the cross-linking of nearby subunits by bifunctional cross-linkers). We also reviewed recent photoaffinity labeling studies using complex I inhibitors, which can be recognized as "site-specific modification" by synthetic chemicals. In addition, we discussed the possibility of site-specific modification by various functional probes via ligand-directed tosylate (LDT) chemistry as a promising approach for unique biophysical studies on complex I.
authors.affiliation: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, 606-8502, Japan.
authors.forename: Masatoshi
authors.initials: M
authors.lastname: Murai
authors.forename: Hideto
authors.initials: H
authors.lastname: Miyoshi
mesh_terms: D000818:Animals; D003432:Cross-Linking Reagents / Q000737:chemistry*; D042967:Electron Transport Complex I / Q000737:chemistry*; D004791:Enzyme Inhibitors / Q000737:chemistry*; D006801:Humans
chemical_list: D003432:Cross-Linking Reagents; D004791:Enzyme Inhibitors; D042967:Electron Transport Complex I