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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1996-4-3
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pubmed:abstractText |
Cytochrome c peroxidase from Pseudomonas aeruginosa (PsCCP) represents a new class of peroxidases which work without the need to create a semi-stable free radical for catalysis. The enzyme is located in the bacterial periplasm where its likely function is to provide protection against toxic peroxides. The soluble 323-residue single polypeptide chain contains two covalent c-type haems with very different properties: one of them is a low-potential (-330 mV) centre where hydrogen peroxide is reduced (the peroxidatic site); the other is a high-potential (+320 mV) centre which feeds electrons to the peroxidatic site from soluble electron-shuttle proteins such as cytochrome c and azurin.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1225-33
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8591033-Amino Acid Sequence,
pubmed-meshheading:8591033-Bacterial Proteins,
pubmed-meshheading:8591033-Binding Sites,
pubmed-meshheading:8591033-Calcium,
pubmed-meshheading:8591033-Catalysis,
pubmed-meshheading:8591033-Crystallography, X-Ray,
pubmed-meshheading:8591033-Cytochrome-c Peroxidase,
pubmed-meshheading:8591033-Electron Transport,
pubmed-meshheading:8591033-Free Radicals,
pubmed-meshheading:8591033-Heme,
pubmed-meshheading:8591033-Iron,
pubmed-meshheading:8591033-Models, Molecular,
pubmed-meshheading:8591033-Molecular Sequence Data,
pubmed-meshheading:8591033-Oxidation-Reduction,
pubmed-meshheading:8591033-Peroxidases,
pubmed-meshheading:8591033-Protein Conformation,
pubmed-meshheading:8591033-Pseudomonas aeruginosa,
pubmed-meshheading:8591033-Structure-Activity Relationship
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pubmed:year |
1995
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pubmed:articleTitle |
Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa.
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pubmed:affiliation |
Laboratory of Molecular Biophysics, University of Oxford, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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