Premium
X‐ray structure of cyanide‐bound bovine heart cytochrome c oxidase in the fully oxidized state at 2.0 Å resolution
Author(s) -
Yano Naomine,
Muramoto Kazumasa,
Mochizuki Masao,
ShinzawaItoh Kyoko,
Yamashita Eiki,
Yoshikawa Shinya,
Tsukihara Tomitake
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15007025
Subject(s) - cyanide , cytochrome c oxidase , chemistry , peroxide , cytochrome c , oxidation state , metal , crystallography , electron transport complex iv , oxidoreductase , oxidase test , stereochemistry , photochemistry , inorganic chemistry , enzyme , biochemistry , organic chemistry , mitochondrion
The X‐ray structure of cyanide‐bound bovine heart cytochrome c oxidase in the fully oxidized state was determined at 2.0 Å 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.