NDLI: Chemical modifications of respiratory complex I for structural and functional studies

Content Provider	Springer Nature Link
Author	Murai, Masatoshi Miyoshi, Hideto
Copyright Year	2014
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.
Starting Page	313
Ending Page	321
Page Count	9
File Format	PDF
ISSN	0145479X
Journal	Journal of Bioenergetics and Biomembranes
Volume Number	46
Issue Number	4
e-ISSN	15736881
Language	English
Publisher	Springer US
Publisher Date	2014-07-04
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Cys-S-nitrosation Cys-S-glutathionylation SH-reagents bifunctional cross-linkers photoaffinity labeling ligand-directed tosylate (LDT) chemistry Bioorganic Chemistry Biochemistry Animal Anatomy / Morphology / Histology Animal Biochemistry Organic Chemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Physiology

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