Functional implications of the structure of the 'Rieske' iron-sulfur protein of bovine heart mitochondrial cytochrome bc1 complex.
Recently, we have determined the structure of the catalytic domain of the 'Rieske' iron-sulfur protein of bovine heart mitochondrial bc1 complex at 1.5 A resolution (Iwata, S., Saynovits, M., Link, T.A. and Michel, H. (1996) Structure, 4, 567-579). This is the first structure of a bis-histidine coordinated [2Fe-2S] cluster. The spectroscopic, electrochemical, and functional implications of the structure will be discussed.
Link
T A
TA
Universitätsklinikum Frankfurt, Main, Germany. link@zbc.klinik.uni-frankfurt.de
Iwata
S
S
D000818:Animals; D002417:Cattle; D003580:Cytochromes / Q000737:chemistry; D045348:Cytochromes f; D014450:Electron Transport Complex III / Q000737:chemistry* / Q000502:physiology; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008929:Mitochondria, Heart / Q000201:enzymology*; D010084:Oxidation-Reduction
D003580:Cytochromes; D007506:Iron-Sulfur Proteins; D045348:Cytochromes f; D014450:Electron Transport Complex III