X-ray structure of cyanide-bound bovine heart cytochrome c oxidase in the fully oxidized state at 2.0Å resolution

X-ray structure of cyanide-bound bovine heart cytochrome c oxidase in the fully oxidized state at 2.0Å resolution

The X-ray structure of cyanide-bound bovine heart cytochrome c oxidase in the fully oxidized state was determined at 2.0Å resolution. The structure reveals that the peroxide that bridges the two metals in the fully oxidized state is replaced by a cyanide ion bound in a nearly symmetric end-on fashio...

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Veröffentlicht in:Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2015-06, Vol.71 (6), p.726
Hauptverfasser: Yano, Naomine, Muramoto, Kazumasa, Mochizuki, Masao, Shinzawa-Itoh, Kyoko, Yamashita, Eiki, Yoshikawa, Shinya, Tsukihara, Tomitake
Format: Artikel
Sprache:eng
Schlagworte:
Cyanides
Cytochrome
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Zusammenfassung:The X-ray structure of cyanide-bound bovine heart cytochrome c oxidase in the fully oxidized state was determined at 2.0Å resolution. The structure reveals that the peroxide that bridges the two metals in the fully oxidized state is replaced by a cyanide ion bound in a nearly symmetric end-on fashion without significantly changing the protein conformation outside the two metal sites.
ISSN:2053-230X
DOI:10.1107/S2053230X15007025