The structure of the metal centers in cytochrome c oxidase

Sunney I. Chan, Craig T. Martin, Hsin Wang, Gary W. Brudvig, Tom H. Stevens, The Coordination Chemistry of Metalloenzymes, 313-328, 1983

Progress toward elucidation of the structure of the metal centers in cytochrome c oxidase will be reviewed. Our studies are based on low-temperature electron paramagnetic resonance (EPR) spectroscopy. We have used nitric oxide (NO) extensively to probe the O2 reduction site of the enzyme. In addition, we have isolated auxotrophs of Saccharomyces cerevisiae in order to incorporate isotopically substituted amino acids into the yeast protein. This latter approach, in conjunction with low-temperature EPR and electron nuclear double resonance (ENDOR) spectroscopy, has allowed unambiguous Information on the structure of two of the four metal centers.