Catching Copper in the Act

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Science  07 May 2004:
Vol. 304, Issue 5672, pp. 836-837
DOI: 10.1126/science.1098301

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Many important biological processes catalyzed by metalloproteins involve reactive metal-diatom intermediates that have been difficult to characterize. In their perspective, Aboelella et al. discuss new work ( Tocheva et al., Prigge et al.) in which binding modes for adducts of the simple diatomics NO and Oto single copper sites in the proteins nitrite reductase and peptidylglycine-hydroxylating monooxygenase, respectively, have been characterized by x-ray crystallography. These structures of novel reactive intermediates raise interesting questions about the mechanisms of catalysis by the metalloenzymes.