1qni
From Proteopedia
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CRYSTAL STRUCTURE OF NITROUS OXIDE REDUCTASE FROM PSEUDOMONAS NAUTICA, AT 2.4A RESOLUTION
Overview
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.
About this Structure
1QNI is a Single protein structure of sequence from Marinobacter hydrocarbonoclasticus with , , and as ligands. Known structural/functional Sites: , , , , , , , , , , and . Full crystallographic information is available from OCA.
Reference
A novel type of catalytic copper cluster in nitrous oxide reductase., Brown K, Tegoni M, Prudencio M, Pereira AS, Besson S, Moura JJ, Moura I, Cambillau C, Nat Struct Biol. 2000 Mar;7(3):191-5. PMID:10700275
Page seeded by OCA on Thu Feb 21 14:41:40 2008
Categories: Marinobacter hydrocarbonoclasticus | Single protein | Brown, K. | Cambillau, C. | Tegoni, M. | CA | CL | CUA | CUZ | Crystal structure | Denitrification | Electron transfer | Mad
