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协同催化——[NiFe]氢化酶与 NiRu 模型催化剂的协同作用。

Concerto catalysis--harmonising [NiFe]hydrogenase and NiRu model catalysts.

机构信息

Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, 744 Moto-oka, Nishi-ku, Fukuoka 819-0395, Japan.

出版信息

Dalton Trans. 2010 Mar 28;39(12):2993-4. doi: 10.1039/b926061g. Epub 2010 Jan 12.

Abstract

This communication reports the successful merging of the chemical properties of a natural [NiFe]hydrogenase (Desulfovibrio vulgaris Miyazaki F) and our previously reported [NiRu] hydrogenase-mimic. The catalytic activity of both the natural enzyme and the mimic is almost identical, with the exception of working pH ranges, and this allows us to use them simultaneously in the same reaction flask. In such a manner, isotope exchange between D(2) and H(2)O could be conducted over an extended pH range (about 2-10) in one pot under mild conditions at ambient temperature and pressure.

摘要

本通讯报道了一种天然[NiFe]氢化酶(脱硫弧菌 Miyazaki F)和我们之前报道的[NiRu]氢化酶模拟物的化学性质的成功融合。除了工作 pH 范围外,天然酶和模拟酶的催化活性几乎完全相同,这使得我们可以在同一个反应瓶中同时使用它们。通过这种方式,可以在温和的条件下在环境温度和压力下在一个锅中在较宽的 pH 范围内(约 2-10)进行 D(2)和 H(2)O 之间的同位素交换。

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