Structural highlights
9qdt is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
|
| Method: | X-ray diffraction, Resolution 2.572Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
CCP_ECOLI Cytochrome peroxidase that enables anaerobic respiration with H(2)O(2) as a terminal electron acceptor (PubMed:28696311). It receives electrons from the quinol pool (PubMed:28696311, PubMed:29550214). Menaquinol is probably the electron donor in vivo (PubMed:28696311, PubMed:29550214). It can use menadiol (a menaquinol analog), hydroquinone, duroquinol and the artificial electron donor ABTS(2-) in vitro, but only menadiol and hydroquinone can efficiently transfer electrons to Ccp, maintaining the catalytic activity of the enzyme (PubMed:29550214). It enables E.coli to grow on a nonfermentable carbon source when H(2)O(2) is supplied (PubMed:28696311). Plays a role in the peroxide stress response under anaerobic conditions (PubMed:17464064). However, it does not degrade H(2)O(2) quickly enough to lower the periplasmic H(2)O(2) level below that of the surrounding medium and protect the cell from its toxic effects (PubMed:28696311).[1] [2] [3]
References
- ↑ Partridge JD, Poole RK, Green J. The Escherichia coli yhjA gene, encoding a predicted cytochrome c peroxidase, is regulated by FNR and OxyR. Microbiology (Reading). 2007 May;153(Pt 5):1499-1509. PMID:17464064 doi:10.1099/mic.0.2006/004838-0
- ↑ Khademian M, Imlay JA. Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor. Proc Natl Acad Sci U S A. 2017 Aug 15;114(33):E6922-E6931. PMID:28696311 doi:10.1073/pnas.1701587114
- ↑ Nóbrega CS, Devreese B, Pauleta SR. YhjA Biochim Biophys Acta Bioenerg. 2018 Jun;1859(6):411-422. PMID:29550214 doi:10.1016/j.bbabio.2018.03.008
