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

生命过程化学(CLP)项目的这一合作研究奖支持芝加哥洛约拉大学化学和生物化学系的Richard C.Holz教授与威斯康星医学院(CHE-1058396)的Brian Bennett教授合作，对铁和钴型氰基水合酶(NHase，EC 4.2.1.84)的催化机制进行基础研究。在常压、温度和生理pH条件下，NHase以化学、区域和/或对映体选择性的方式催化腈的水合反应生成相应的商业价值的酰胺类化合物。由于这些原因，氨酶作为制备有机化学中的生物催化剂引起了人们的极大兴趣，而含有氨酶的细菌已经在大规模生产丙烯酰胺和烟酰胺中找到了一些工业应用。由于人们对氨酶的功能知之甚少，更好地了解氨酶的结构和反应机理将使人们能够获得底物范围更广、活性更高、稳定性更好的氰基水解物。这些生物材料还将为丁腈水合所需的苛刻工业条件提供一种“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.