Collaborative Research: Mechanistic Studies on Fe-type Nitrile Hydration Catalysts

这项生命过程化学（CLP）项目的合作研究奖支持芝加哥洛约拉大学化学与生物化学系的Richard C. Holz教授与威斯康星医学院的Brian Bennett教授（CHE-1058396）合作，对铁和钴型腈水合酶（NHase, EC 4.2.1.84）的催化机制进行基础研究。在环境压力、温度和生理ph下，NHase以化学、区域和/或对映选择性的方式催化腈水化成相应的具有商业价值的酰胺。由于这些原因，NHase作为制备有机化学中的生物催化剂引起了极大的兴趣，并且含有NHase的细菌已经在丙烯酰胺和烟酰胺的大规模生产中发现了一些工业应用。由于对nase酶的功能知之甚少，更好地了解nase酶的结构和反应机制将使我们能够获得更广泛的底物范围、更高的活性和更大的稳定性的腈水解材料。这些生物材料还将为腈水化所需的恶劣工业条件提供“绿色”替代方案。

This collaborative research award in the Chemistry of Life Processes (CLP) program supports work by Prof. Richard C. Holz of the Department of Chemistry and Biochemistry at Loyola University Chicago to carry out fundamental studies on the catalytic mechanism of iron- and cobalt-type nitrile hydratases (NHase, EC 4.2.1.84), in collaboration with Prof. Brian Bennett at the Medical College of Wisconsin (CHE-1058396). NHase's catalyze the hydration of nitriles to their corresponding commercially valuable amides in a chemo-, regio-, and/or enantio-selective manner at ambient pressures, temperatures, and physiological pH. For these reasons, NHases have attracted substantial interest as biocatalysts in preparative organic chemistry and NHase containing bacteria have found some industrial applications in the large scale production of acrylamide and nicotinamide.Since little is understood about how NHase enzymes function, a better understanding of the structure and reaction mechanism of NHase enzymes will enable access to nitrile-hydrolyzing materials with broader substrate ranges, higher activities, and greater stabilities. These biomaterials will also provide a "green" alternative to the harsh industrial conditions required for nitrile hydration.