A thiolate-bridged, fully delocalized mixed-valence dicopper (I, II) complex that models the CuA biological electron-transfer site

RP Houser, VG Young, WB Tolman

Index: Houser, Robert P.; Young Jr., Victor G.; Tolman, William B. Journal of the American Chemical Society, 1996 , vol. 118, # 8 p. 2101 - 2102

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Citation Number: 152

Abstract

Nitrous oxide reductase (N2OR) and cytochrome c oxidase (CcO) catalyze the reductions of N2O to N2 during microbial denitrification and of O2 to H2O during cellular respiration, respectively. 1, 2 These disparate metalloenzymes have in common an unusual copper site, CuA, that functions analogously to the ubiquitous type 1 monocopper centers3 to transfer electrons during enzyme turnover. Controversy surrounding the structure of CuA appears ...