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

生命过程化学（CLP）计划中的这一合作研究奖支持Richard C.芝加哥洛约拉大学化学和生物化学系的Holz与威斯康星州医学院的Brian班尼特教授合作（CHE-1058396），对铁和钴型腈水合酶（NHase，EC4.2.1.84）的催化机制进行基础研究。 腈水合酶在环境压力、温度和生理pH下以化学选择性、区域选择性和/或对映选择性方式催化腈水合成其相应的商业上有价值的酰胺。作为制备有机化学中的生物催化剂，腈水合酶已经引起了人们的极大兴趣，并且含有腈水合酶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。随着人们对腈水解酶功能的了解越来越深入，对腈水解酶的结构和反应机理的更好理解将使人们能够获得具有更宽底物范围、更高活性和更高稳定性的腈水解材料。 这些生物材料还将为腈水合所需的苛刻工业条件提供“绿色”替代品。

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.