Schwarz Günter, Mendel Ralf R, Ribbe Markus W
Institute of Biochemistry, Department of Chemistry & Centre for Molecular Medicine, University of Cologne, 47 Zuelpicher Street, 50674 Cologne, Germany.
Nature. 2009 Aug 13;460(7257):839-47. doi: 10.1038/nature08302.
The trace element molybdenum is essential for nearly all organisms and forms the catalytic centre of a large variety of enzymes such as nitrogenase, nitrate reductases, sulphite oxidase and xanthine oxidoreductases. Nature has developed two scaffolds holding molybdenum in place, the iron-molybdenum cofactor and pterin-based molybdenum cofactors. Despite the different structures and functions of molybdenum-dependent enzymes, there are important similarities, which we highlight here. The biosynthetic pathways leading to both types of cofactor have common mechanistic aspects relating to scaffold formation, metal activation and cofactor insertion into apoenzymes, and have served as an evolutionary 'toolbox' to mediate additional cellular functions in eukaryotic metabolism.
微量元素钼对几乎所有生物体来说都是必不可少的，并且它构成了多种酶的催化中心，如固氮酶、硝酸还原酶、亚硫酸盐氧化酶和黄嘌呤氧化还原酶。自然界已经形成了两种将钼固定在位的支架结构，即铁钼辅因子和基于蝶呤的钼辅因子。尽管依赖钼的酶具有不同的结构和功能，但仍存在重要的相似之处，我们在此予以强调。导致这两种辅因子的生物合成途径在支架形成、金属活化以及辅因子插入脱辅基酶等方面具有共同的机制，并且已成为一种进化的“工具箱”，用于在真核生物代谢中调节其他细胞功能。
