Reaction mechanism and phospholipid structures of bovine heart cytochrome c oxidase.
Bovine heart cytochrome c oxidase is a large multi-component membrane protein containing several phospholipids. X-ray structures of this enzyme at high resolution, determined recently, show a trigonal planar structure of CuB site in the O2 reduction site, which could contribute critically to the four-electron reduction of O2 bound at haem a3, and a hydrogen bond network, through which the proton pump is driven by haem a. The possible roles of phospholipids in the enzyme functions are discussed.
Yoshikawa
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Department of Life Science, University of Hyogo, Kamigohri, Akoh Hyogo 678-1297, Japan. yoshi@sci.u-hyogo.ac.jp
D000818:Animals; D002417:Cattle; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000378:metabolism*; D006860:Hydrogen Bonding; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008929:Mitochondria, Heart / Q000201:enzymology*; D010101:Oxygen Consumption; D010743:Phospholipids / Q000737:chemistry* / Q000302:isolation & purification
D008565:Membrane Proteins; D010743:Phospholipids; D003576:Electron Transport Complex IV