Protein‐radical enzymes

FEBS Letters

Pedersen, Jens Z.¹  Finazzi-Agrò, Alessandro² 

[1] Department of Biology, ‘Tor Vergata’ University of Rome, Via O. Raimondo, 00173 Rome, Italy;Department of Experimental Medicine, ‘Tor Vergata’ University of Rome, Via O. Raimondo, 00173 Rome, Italy

关键词: Protein-radical enzyme;    Pyrroloquinoline quinone;    Trioxyphenylalanine;    Tryptophan tryptophyl quinone;    Free radical;    ESR;    PQQ;    pyrroloquinoline quinone;    TOPA;    trioxyphen-ylalanine (2;    4;    5-trihydroxyphenylalanine);    TTQ;    tryptophan tryptophyl quinone;   

DOI  :  10.1016/0014-5793(93)81412-S

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown