期刊论文详细信息
FEBS Letters | |
Protein‐radical enzymes | |
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
【 预 览 】
Files | Size | Format | View |
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RO201912020298015ZK.pdf | 632KB | download |