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Eric C. Niederhoffer, Ph.D. Associate Professor of Biochemistry and Molecular Biology Southern Illinois University School of Medicine 600 Agriculture Drive, Carbondale, IL 62901-6503 Rm 112 Lindegren, 618-453-6467 eniederhoffer@siumed.edu Copyright 2000- , E.C. Niederhoffer. All Rights Reserved. All trademarks and copyrights are the property of their respective owners.

Cytochrome c oxidase in the oxidized (2occ) and reduced state (1ocr) from Bos taurus (bovine)

• What structural elements are present in the protein?
• What is the subunit composition?
• Locate the low-potential, high-potential, Cu_A, Cu_B, Hem a, and Hem a₃ sites.
• What is the coordination geometry about each metal ion?
• What is the distance between metal ions and ligands?
• Where is the most probable binding region for cytochrome c?
• What is significant about Tyr244 and His240?
• What changes have occurred upon oxidation-reduction?

Yoshikawa, S., K. Shinzawa-Itoh, R. Nakashima, R. Yaono, E. Yamashita, N. Inoue, M. Yao, M. J. Fei, C. P. Libeu, T. Mizushima, H. Yamaguchi, T. Tomizaki, and T. Tsukihara. 1998. Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase. Science 280:1723-1729.

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