Di-haem cytochrome c peroxidase

Di-haem cytochrome c peroxidase
crystal structure of the di-haem cytochrome c peroxidase from pseudomonas aeruginosa
Identifiers
Symbol	CCP_MauG
Pfam	PF03150
Pfam clan	CL0318
InterPro	IPR004852
SCOP	1eb7
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

In molecular biology, the di-haem cytochrome c peroxidase family is a group of distinct cytochrome c peroxidases (CCPs) that contain two haem groups. Similar to other cytochrome c peroxidases, they reduce hydrogen peroxide to water using c-type haem as an oxidizable substrate. However, since they possess two, instead of one, haem prosthetic groups, this family of bacterial CCPs reduce hydrogen peroxide without the need to generate semi-stable free radicals. The two haem groups have significantly different redox potentials. The high potential (+320 mV) haem feeds electrons from electron shuttle proteins to the low potential (-330 mV) haem, where peroxide is reduced (indeed, the low potential site is known as the peroxidatic site).^[1] The CCP protein itself is structured into two domains, each containing one c-type haem group, with a calcium-binding site at the domain interface. This family also includes MauG proteins, whose similarity to di-haem CCP was previously recognised.^[2]

References

1. ^ Fulop V, Ridout CJ, Greenwood C, Hajdu J (November 1995). "Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa". Structure 3 (11): 1225–33. PMID 8591033. 
2. ^ Gak ER, Tsygankov YD, Chistoserdov AY (June 1997). "Organization of methylamine utilization genes (mau) in 'Methylobacillus flagellatum ' KT and analysis of mau mutants". Microbiology (Reading, Engl.) 143 ( Pt 6): 1827–35. PMID 9202457. 

This article includes text from the public domain Pfam and InterPro IPR004852