IPR003143
Cytochrome cd1-nitrite reductase, C-terminal domain superfamily
InterPro entry
Short name | Cyt_cd1_C_sf |
Overlapping entries |
Description
Cytochrome cd1 (cyt cd1) nitrite reductase is a dimeric enzyme of the bacterial periplasm that plays a key role in denitrification, the respiratory reduction of nitrite to nitric oxide in the nitrogen cycle. Each subunit of the cyt cd1 dimer contains one cytochrome c and one d1 haem group
[1]. The active site contains a specialised d1 haem, where the nitrite substrate is bound and reduced. This d1 haem is bound in an 8-bladed β-propeller
[2]. This superfamily represents the C-terminal region of the d1 domain.
References
1.Structure and kinetic properties of Paracoccus pantotrophus cytochrome cd1 nitrite reductase with the d1 heme active site ligand tyrosine 25 replaced by serine. Gordon EH, Sjogren T, Lofqvist M, Richter CD, Allen JW, Higham CW, Hajdu J, Fulop V, Ferguson SJ. J. Biol. Chem. 278, 11773-81, (2003). View articlePMID: 12556530
2.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 81, 369-77, (1995). View articlePMID: 7736589
Cross References
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:2.140.10.20
Representative structure
6tv2: Heme d1 biosynthesis associated Protein NirF