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1qks
From Proteopedia
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CYTOCHROME CD1 NITRITE REDUCTASE, OXIDISED FORM
Overview
Cytochrome cd1-nitrite reductase is a bifunctional enzyme that catalyzes, the one-electron reduction of nitrite to nitric oxide and the, four-electron reduction of oxygen to water. The 1.55 A crystal structure, of the dimeric enzyme from Thiosphaera pantotropha is reported here. The, protein was sequenced from the X-ray structure. Each subunit contains a, covalent c heme with two axial His ligands (His-17, His-69) and a unique, noncovalent d1 heme ligated by Tyr-25 and His-200. The d1 heme is the, mononuclear iron center where both oxygen and nitrite reduction take, place. The two types of heme are located in separate domains whose, arrangement suggests a mechanism requiring domain movement during, catalysis.
About this Structure
1QKS is a Single protein structure of sequence from Paracoccus denitrificans with SO4, HEC, DHE and GOL as ligands. Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
Reference
The anatomy of a bifunctional enzyme: structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1., Fulop V, Moir JW, Ferguson SJ, Hajdu J, Cell. 1995 May 5;81(3):369-77. PMID:7736589
Page seeded by OCA on Tue Dec 18 17:55:16 2007
Categories: Paracoccus denitrificans | Single protein | Fulop, V. | DHE | GOL | HEC | SO4 | Denitrification | Electron transport | Enzyme | Nitrite reductase | Oxidoreductase | Periplasmic
