Protein-radical enzymes.
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.
Department of Biology, Tor Vergata University of Rome, Italy.
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JZ
Pedersen
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Finazzi-Agrò
D004295:Dihydroxyphenylalanine / Q000031:analogs & derivatives / Q000737:chemistry; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism*; D005609:Free Radicals; D005998:Glycine / Q000737:chemistry; D015394:Molecular Structure; D045542:PQQ Cofactor; D015363:Quinolones / Q000737:chemistry; D014364:Tryptophan / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry
D004798:Enzymes; D005609:Free Radicals; D015363:Quinolones; C001388:6-hydroxydopa; D014443:Tyrosine; D004295:Dihydroxyphenylalanine; D045542:PQQ Cofactor; D014364:Tryptophan; D005998:Glycine