Structure and function of the xanthine-oxidase family of molybdenum enzymes

被引:0
作者
Romao, MJ
Huber, R
机构
[1] Univ Nova Lisboa, Inst Tecnol Quim & Biol, P-2780 Oeiras, Portugal
[2] Inst Super Tecn, Dept Quim, P-1096 Lisbon, Portugal
[3] Max Planck Inst Biochem, D-82152 Martinsried, Germany
来源
METAL SITES IN PROTEINS AND MODELS: REDOX CENTRES | 1998年 / 90卷
关键词
hydroxylase; molybdoenzymes; molybdopterin; protein crystallography; xanthine oxidase;
D O I
暂无
中图分类号
O61 [无机化学];
学科分类号
070301 ; 081704 ;
摘要
This work gives an account of the recent achievements which have contributed towards the understanding of the structure and function of the xanthine oxidase family of enzymes-the molybdenum hydroxylases. It is based essentially on the crystallographic data of the aldehyde oxido-reductase from Desulfovibrio (D.) gigas, a member of that family, whose structure is described in detail. Comparisons are made, whenever appropriate, with spectroscopic, kinetic and model compound studies. Mechanistic implications of the crystal structure of the D. gigas enzyme are considered and extended to the xanthine oxidase family.
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页码:69 / 95
页数:27
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