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学科主题: 生命有机化学
题名: Catalytic mechanism of quinoprotein methanol cehydrogenase: A theoretical and X-ray crystallographic investigation
其他题名: 醌蛋白-甲醇脱氢酶的催化机理:理论的和X射线晶体学的研究
作者: ZHENG YAYUN ; Xia ZX(夏宗芗) ; CHEN ZHIWEI ; F. SCOTT MATHEWS ; THOMAS C. BRUICE
通讯作者: ZHENG YAYUN
刊名: Proc. Natl. Acad. Sci. U. S. A.
发表日期: 2001-01-01T00:00:00Z
卷: 98, 期:2, 页:432-434
收录类别: SCI
部门归属: 中国科学院上海有机化学研究所生命有机化学实验室; Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine; Department of Chemistry, University of California, Santa Barbara, CA
英文摘要: The catalytic mechanism of the reductive half reaction of the quinoprotein methanol dehydrogenase (MDH) is believed to proceed either through a hemiketal intemediate or by direct ttransfer of a hydride ion from the substrate methyl group to the cofactor, pyrroloquinoline quinone (PQQ). A crystal structure of the enzyme-substrate complex of a similar quinoprotein, glucose dehydrogenase, has recently been reported that strongly favors the hydride transfer mechanism in that enzyme. A the oretical analysis and an improved refinement of the 1.9-A resolution crystal structure of MDH from methylophilus methylotrophus W3A1 in the presence of methanol, reported earlier, indicates that the observed tetrahedral configuration of the C-5atom of PQQ in that study represents the C-5-reduced form of the cofactor and lends supprt for a hydride transfer mechanism for MDH.
语种: 英语
相关网址: 查看原文
内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/23670
Appears in Collections:生命有机化学国家重点实验室_期刊论文

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Recommended Citation:
ZHENG YAYUN,Xia ZX,CHEN ZHIWEI,et al. Catalytic mechanism of quinoprotein methanol cehydrogenase: A theoretical and X-ray crystallographic investigation[J]. Proc. Natl. Acad. Sci. U. S. A.,2001,98(2):432-434.
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