Haem_bd

Haem-binding domain

• SMART accession number: SM01235
• Description: This domain contains a potential haem-binding motif, CXXCH (PMID:17288564).
• Interpro abstract (IPR025992):

  This domain contains a potential haem-binding motif, CXXCH [ (PUBMED:17288564) ] and it is often found in association with and .

There are 2010 Haem_bd domains in 2010 proteins in SMART's nrdb database.

Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

• Yamada H, Takashima E, Konishi K
• Molecular characterization of the membrane-bound quinol peroxidase functionallyconnected to the respiratory chain.
• FEBS J. 2007; 274: 853-66

Here, we report for the first time quinol peroxidase (QPO), an enzyme that usesubiquinol-1 as an electron donor for the reduction of H(2)O(2) to water. Wepurified QPO to > 90% purity from the membrane fraction of Actinobacillusactinomycetemcomitans. QPO is a 53.6-kDa protein that contains three heme cmolecules. The qpo gene was predicted to encode a putative bacterial cytochrome cperoxidase with N-terminal extensions containing an additional potential hemec-binding motif. Although qpo has high sequence homology to bacterial cytochrome c peroxidases, QPO did not catalyze peroxidation in the presence of horse heartcytochrome c. In addition, the cytoplasmic membrane of A. actinomycetemcomitanshad apparent QPO-dependent peroxidase activity in the presence of NADH orsuccinate, which are substrates for the respiratory chain. Based on thesefindings, we present a new mechanism for the scavenging of reactive oxygenspecies in which quinol in the respiratory chain is consumed.

Links (links to other resources describing this domain)

• PFAM: Haem_bd
• INTERPRO: IPR025992