Binding sites of lipophilic quinone and quinone analogue inhibitors in the cytochrome b6f complex of oxygenic photosynthesis.
The main structural features of the cytochrome b6f complex, solved to 3.0-3.1 A (1 A = 10(-10) m) in the cyanobacterium Mastigocladus laminosus and the green alga Chlamydomonas reinhardtii are discussed. The discussion is focused on the binding sites of plastoquinone and quinone analogue inhibitors discerned in the structure. These sites mark the pathway(s) of quinone translocation across the complex.
Cramer
W A
WA
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-2154, USA. waclab@purdue.edu
Zhang
H
H
Yan
J
J
Kurisu
G
G
D001665:Binding Sites; D045346:Cytochrome b6f Complex / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D019281:Dimerization; D010101:Oxygen Consumption; D010788:Photosynthesis; D011809:Quinones / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000494:pharmacology
D011809:Quinones; D045346:Cytochrome b6f Complex