Document Detail

Protein-radical enzymes.
MedLine Citation:
PMID:  8390374     Owner:  NLM     Status:  MEDLINE    
Protein-radical enzymes use a free radical located on an intrinsic amino acid residue as a cofactor. The amino acid involved can be a tyrosine (ribonucleotide reductase, photosystem II, prostaglandin H synthase), a modified tyrosine (amine oxidase, galactose oxidase), a tryptophan (cytochrome c peroxidase), a modified tryptophan (methylamine dehydrogenase) or a glycine (ribonucleotide reductase, pyruvate formate lyase). The mechanistic role of these radicals appears to be that of a one-electron gate, allowing the separation of single reducing equivalents in time and space.
J Z Pedersen; A Finazzi-Agrò
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  FEBS letters     Volume:  325     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1993 Jun 
Date Detail:
Created Date:  1993-07-22     Completed Date:  1993-07-22     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  53-8     Citation Subset:  IM    
Department of Biology, Tor Vergata University of Rome, Italy.
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MeSH Terms
Dihydroxyphenylalanine / analogs & derivatives,  chemistry
Enzymes / chemistry,  metabolism*
Free Radicals
Glycine / chemistry
Molecular Structure
PQQ Cofactor
Quinolones / chemistry
Tryptophan / chemistry
Tyrosine / chemistry
Reg. No./Substance:
0/Enzymes; 0/Free Radicals; 0/Quinolones; 21373-30-8/6-hydroxydopa; 55520-40-6/Tyrosine; 56-40-6/Glycine; 63-84-3/Dihydroxyphenylalanine; 72909-34-3/PQQ Cofactor; 73-22-3/Tryptophan

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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