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Protein‐radical enzymes
Author(s) -
Pedersen Jens Z.,
Finazzi-Agrò Alessandro
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81412-s
Subject(s) - chemistry , biochemistry , enzyme
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 reduetase, 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.