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


ABSTRACT: 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.

SUBMITTER: Yano N 

PROVIDER: S-EPMC4461337 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature

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

Yano Naomine N   Muramoto Kazumasa K   Mochizuki Masao M   Shinzawa-Itoh Kyoko K   Yamashita Eiki E   Yoshikawa Shinya S   Tsukihara Tomitake T  

Acta crystallographica. Section F, Structural biology communications 20150522 Pt 6


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. ...[more]

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