AI Article Synopsis
- The crystal structure of cyanide-bound bovine heart cytochrome c oxidase was determined at a resolution of 2.0 Å.
- In this fully oxidized state, a cyanide ion replaces the peroxide that connects two metal sites in the enzyme.
- The binding of cyanide does not notably alter the overall protein shape, except in the areas around the metal sites.
Article 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.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4461337 | PMC |
| http://dx.doi.org/10.1107/S2053230X15007025 | DOI Listing |
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