X-ray structure of the NO-bound Cu(B) in bovine cytochrome c oxidase.
The X-ray crystallographic structure of nitric oxide-treated bovine heart cytochrome c oxidase (CcO) in the fully reduced state has been determined at 50 K under light illumination. In this structure, nitric oxide (NO) is bound to the CcO oxygen-reduction site, which consists of haem and a Cu atom (the haem a(3)-Cu(B) site). Electron density for the NO molecule was observed close to Cu(B). The refined structure indicates that NO is bound to Cu(B) in a side-on manner.
Ohta
Kazuhiro
K
Institute for Protein Research, Osaka University, OLABB, 6-2-6 Furuedai, Suita, Osaka 565-0874, Japan.
Muramoto
Kazumasa
K
Shinzawa-Itoh
Kyoko
K
Yamashita
Eiki
E
Yoshikawa
Shinya
S
Tsukihara
Tomitake
T
D000818:Animals; D002417:Cattle; D003300:Copper / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D009569:Nitric Oxide / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary
D009569:Nitric Oxide; D003300:Copper; D003576:Electron Transport Complex IV