A novel type of catalytic copper cluster in nitrous oxide reductase

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. , Nat Struct Biol, Mar, Volume 7, Number 3, p.191-5, (2000)


Nitrous oxide (N20) is a greenhouse gas, the third most significant contributor to global warming. As a key process for N20 elimination from the biosphere, N20 reductases catalyze the two-electron reduction of N20 to N2. 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 N20 reductase from Pseudomonas nautica by multiwavelength anomalous dispersion, to a resolution of 2.4 A. 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. N20 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.


1072-8368 (Print)1072-8368 (Linking)Journal ArticleResearch Support, Non-U.S. Gov't

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