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 ... [(full description)]
About this Structure
1QNI is a [Single protein] structure of sequence from [Marinobacter hydrocarbonoclasticus] with CA, CL, CUA and CUZ as [ligands]. 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 Mon Oct 29 22:12:10 2007
Categories: Marinobacter hydrocarbonoclasticus | Single protein | Brown, K. | Cambillau, C. | Tegoni, M. | CA | CL | CUA | CUZ | Crystal structure | Denitrification | Electron transfer | Mad