Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain.
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.
Sazanov
Leonid A
LA
Medical Research Council Dunn Human Nutrition Unit, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 2XY, UK. sazanov@ mrc-dunn.cam.ac.uk
D003461:Crystallography; D004579:Electron Transport; D042967:Electron Transport Complex I / Q000737:chemistry*; D011487:Protein Conformation; D016963:Thermus thermophilus / Q000201:enzymology
D042967:Electron Transport Complex I