Symphoria: the success of modeling the active site function of oxo-molybdoenzymes

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• 作者：Chaudhury ; Pradeep K. ; Nagarajan ; Kowliki ; Dubey ; Prashant ; Sarkar ; Sabyasachi
• 关键词：Symphoria ; Saturation kinetics ; Random order pathway mechanism ; Competitive inhibition
• 刊名：Journal of Inorganic Biochemistry
• 出版年：2004
• 期刊代码：53_01620134
• 类别：ch
• 出版时间：November, 2004
• 卷：98
• 期：11
• 页码：1667-1677
• 文件大小：410 K

摘要

The success of modeling the active site function of oxomolybdoenzymes have been claimed generally on the basis of reactivity of the synthetic analogues towards PPh₃ or DMSO (dimethyl sulfoxide). Here it has been shown that the success of modeling the active site function of these enzymes may not be determined by the ability of a model to undergo oxotransfer with PPh₃ or DMSO (except for the modeling of DMSO reductase) and one should adhere to the criteria accepted by the bioinorganic community. A critical evaluation of two of those criteria which requires a synthetic analogue (a) should react with the enzyme substrate (b) should follow the same rate law as does the enzyme, has been presented in this paper. We have shown that the fulfillment of criterion (b) and the inhibition phenomena to that effect both are dictated by symphoria (from sympherin in Greek: the bringing together of reactants into the proper spatial relationship) on the basis of kinetic studies of the reactivity of enzyme substrate the HSO₃^芒芒芒 and its analogues (anions of oxyacids of phosphorous) towards a functional model sulfite oxidase [Bu₄N]₂[Mo^VIO₂(mnt)₂] (mnt^2芒芒芒