Abstract
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 a3-CuB site). Electron density for the NO molecule was observed close to CuB. The refined structure indicates that NO is bound to CuB in a side-on manner. © 2010 International Union of Crystallography All rights reserved.
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CITATION STYLE
Ohta, K., Muramoto, K., Shinzawa-Itoh, K., Yamashita, E., Yoshikawa, S., & Tsukihara, T. (2010). X-ray structure of the NO-bound CuB in bovine cytochrome c oxidase. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(3), 251–253. https://doi.org/10.1107/S1744309109055109
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