1QKS

CYTOCHROME CD1 NITRITE REDUCTASE, OXIDISED FORM

Summary for 1QKS

• Entry DOI: 10.2210/pdb1qks/pdb
• Related: 1AOF 1AOM 1AOQ
• Descriptor: CYTOCHROME CD1 NITRITE REDUCTASE, HEME C, HEME D, ... (6 entities in total)
• Functional Keywords: enzyme, nitrite reductase, oxidoreductase, denitrification, electron transport, periplasmic
• Biological source: PARACOCCUS PANTOTROPHUS
• Total number of polymer chains: 2
• Total formula weight: 129094.43

Authors

Fulop, V. (deposition date: 1999-08-05, release date: 1999-08-18, Last modification date: 2024-11-06)

Primary citation

Fulop, V.,Moir, J.W.,Ferguson, S.J.,Hajdu, J.
The anatomy of a bifunctional enzyme: structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1.
Cell(Cambridge,Mass.), 81:369-377, 1995

PubMed Abstract: 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.

PubMed: 7736589
DOI: 10.1016/0092-8674(95)90390-9

Experimental method

X-RAY DIFFRACTION (1.28 Å)