|Title||Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain.|
|Publication Type||Journal Article|
|Year of Publication||2007|
|Date Published||2007 Mar 06|
|Keywords||Crystallography, Electron Transport, Electron Transport Complex I, Protein Conformation, Thermus thermophilus|
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.
|Grant List||MC_U105674180 / / Medical Research Council / United Kingdom|