Pterin chemistry and its relationship to the molybdenum cofactor

被引：108

作者：

Basu, Partha ^{[1
]}

Burgmayer, Sharon J. N. ^{[2
]}

机构：

[1] Duquesne Univ, Dept Chem & Biochem, Pittsburgh, PA 15282 USA

[2] Bryn Mawr Coll, Dept Chem, Bryn Mawr, PA 19010 USA

来源：

COORDINATION CHEMISTRY REVIEWS | 2011年 / 255卷 / 9-10期

基金：

美国国家卫生研究院;

关键词：

Pterin; Molybdenum; Chemical synthesis; Redox reaction; Biosynthesis; GTP CYCLOHYDROLASE-I; ELECTRON-TRANSFER; CRYSTAL-STRUCTURE; DIHYDROPTERIDINE REDUCTASE; PHENYLALANINE-HYDROXYLASE; REGIOSPECIFIC SYNTHESIS; NITRATE REDUCTASE; XANTHINE-OXIDASE; DMSO REDUCTASE; PTERIDINES;

D O I：

10.1016/j.ccr.2011.02.010

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

The molybdenum cofactor is composed of a molybdenum coordinated by one or two rather complicated ligands known as either molybdopterin or pyranopterin. Pterin is one of a large family of bicyclic N-heterocycles called pteridines. Such molecules are widely found in Nature, having various forms to perform a variety of biological functions. This article describes the basic nomenclature of pterin, their biological roles, structure, chemical synthesis and redox reactivity. In addition, the biosynthesis of pterins and current models of the molybdenum cofactor are discussed. (C) 2011 Elsevier B.V. All rights reserved.

引用

页码：1016 / 1038

页数：23

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