Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain.

TitleRespiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain.
Publication TypeJournal Article
Year of Publication2007
AuthorsSazanov, LA
JournalBiochemistry
Volume46
Issue9
Pagination2275-88
Date Published2007 Mar 06
ISSN0006-2960
KeywordsCrystallography, Electron Transport, Electron Transport Complex I, Protein Conformation, Thermus thermophilus
Abstract

Complex I of respiratory chains plays a central role in cellular energy production. Mutations in its subunits lead to many human neurodegenerative diseases. Recently, a first atomic structure of the hydrophilic domain of complex I from Thermus thermophilus was determined. This domain represents a catalytic core of the enzyme. It consists of eight different subunits, contains all the redox centers, and comprises more than half of the entire complex. In this review, novel mechanistic implications of the structure are discussed, and the effects of many known mutations of complex I subunits are interpreted in a structural context.

DOI10.1021/bi602508x
Alternate JournalBiochemistry
Citation Key10.1021/bi602508x
PubMed ID17274631
Grant ListMC_U105674180 / / Medical Research Council / United Kingdom