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Science 7 May 2004:
Vol. 304. no. 5672, pp. 836 - 837
DOI: 10.1126/science.1098301
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Perspectives

BIOPHYSICS:
Catching Copper in the Act

Nermeen W. Aboelella, Anne M. Reynolds, William B. Tolman

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 O2 to single copper sites in the proteins nitrite reductase and peptidylglycine alpha-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.

The authors are in the Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, Minneapolis, MN 55455, USA. E-mail: tolman{at}chem.umn.edu

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Science. ISSN 0036-8075 (print), 1095-9203 (online)