1qks

From Proteopedia

Revision as of 10:27, 5 November 2007

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. Structure known Active Sites: C1A, C1B, D1A and D1B. 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

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