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Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa.

Authors
  • Fülöp, V
  • Ridout, C J
  • Greenwood, C
  • Hajdu, J
Type
Published Article
Journal
Structure
Publisher
Elsevier BV
Publication Date
Nov 15, 1995
Volume
3
Issue
11
Pages
1225–1233
Identifiers
PMID: 8591033
Source
Medline
License
Unknown

Abstract

The likely function of the calcium site is to maintain the structural integrity of the enzyme and/or to modulate electron transfer between the two haem domains. The low-potential haem has two histidine axial ligands (His55 and His71) and the high-potential haem is ligated by His201 and Met275. There are no polar residues at the peroxidatic site in the inactive oxidized enzyme. The structure suggests that, in the half-reduced functional form of the enzyme, the low-potential haem has to shed His71 in order to make the enzyme catalytically competent. This process is likely to trigger a reorganization of the active site, and may introduce a new residues into the haem pocket.

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