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从梭菌固氮酶的钼铁蛋白中分离硫代钼酸盐化合物。

Isolation of thiomolybdate compounds from the molybdenum-iron protein of clostridial nitrogenase.

作者信息

Zumft W G

出版信息

Eur J Biochem. 1978 Nov 15;91(2):345-50. doi: 10.1111/j.1432-1033.1978.tb12686.x.

DOI:10.1111/j.1432-1033.1978.tb12686.x
PMID:729574
Abstract

Acid/base treatment of the molybdenum-iron protein of the nitrogenase from Clostridium pasteurianum 25 yields low-molecular-weight compounds of molybdenum, which can be separated from the protein by gel chromatography. Elementary analysis and spectral properties relate these compounds to thiomolybdate anions. It is proposed that in its native state nitrogenase contains a thio complex of molybdenum coupled to iron-sulfur clusters.

摘要

对巴氏梭菌25号菌株固氮酶的钼铁蛋白进行酸碱处理，会产生低分子量的钼化合物，这些化合物可通过凝胶色谱法与蛋白质分离。元素分析和光谱性质表明这些化合物与硫代钼酸根阴离子有关。有人提出，固氮酶在其天然状态下含有与铁硫簇相连的钼硫配合物。

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Isolation of thiomolybdate compounds from the molybdenum-iron protein of clostridial nitrogenase.从梭菌固氮酶的钼铁蛋白中分离硫代钼酸盐化合物。
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