1hj4 | pdb_00001hj4

Cytochrome cd1 Nitrite Reductase, x-ray reduced dioxygen complex

spinqualitylabelsall models 1hj4, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1hj4 is a 2 chain structure with sequence from Paracoccus pantotrophus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: DHE, GOL, HEC, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NIRS_PARPN Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Reduction of dioxygen to water is a key process in aerobic life, but atomic details of this reaction have been elusive because of difficulties in observing active oxygen intermediates by crystallography. Cytochrome cd(1) is a bifunctional enzyme, capable of catalyzing the one-electron reduction of nitrite to nitric oxide, and the four-electron reduction of dioxygen to water. The latter is a cytochrome oxidase reaction. Here we describe the structure of an active dioxygen species in the enzyme captured by cryo-trapping. The productive binding mode of dioxygen in the active site is very similar to that of nitrite and suggests that the catalytic mechanisms of oxygen reduction and nitrite reduction are closely related. This finding has implications to the understanding of the evolution of oxygen-reducing enzymes. Comparison of the dioxygen complex to complexes of cytochrome cd(1) with stable diatomic ligands shows that nitric oxide and cyanide bind in a similar bent conformation to the iron as dioxygen whereas carbon monoxide forms a linear complex. The significance of these differences is discussed. Structure of the bound dioxygen species in the cytochrome oxidase reaction of cytochrome cd1 nitrite reductase.,Sjogren T, Hajdu J J Biol Chem. 2001 Apr 20;276(16):13072-6. Epub 2001 Jan 26. PMID:11278884 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome c nitrite reductase

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