Citation:

A novel type of catalytic copper cluster in nitrous oxide reductase, Brown, K., Tegoni M., Prudencio M., Pereira A. S., Besson S., Moura J. J., Moura I., and Cambillau C. , Nature Structural Biology, Apr, Volume {7}, Number {3}, 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA, p.{191-195}, (2000) copy at https://sites.fct.unl.pt/molecular-biophysics/publications/novel-type-catalytic-copper-cluster-nitrous-oxide-reductase

Abstract:

Nitrous oxide (N(2)O) is a greenhouse gas, the third most significant contributor to global warming. As a key process for N(2)O elimination from the biosphere, N(2)O reductases catalyze the two-electron reduction of N(2)O to N(2). These 2 x 65 kDa copper enzymes are thought to contain a CuA electron entry site, similar to that of cytochrome c oxidase, and a CuZ catalytic center. The copper anomalous signal was used to solve the crystal structure of N(2)O reductase from Pseudomonas nautica by multiwavelength anomalous dispersion, to a resolution of 2.4 Angstrom. The structure reveals that the CuZ center belongs to a new type of metal cluster, in which four copper ions are liganded by seven histidine residues. N(2)O binds to this center via a single copper ion. The remaining copper ions might act as an electron reservoir, assuring a fast electron transfer and avoiding the formation of dead-end products.

Notes:

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