Heteroscorpionate Ligands: Applications to Bioinorganic Chemistry

该奖项由无机、生物无机和有机金属化学项目颁发，支持圣地亚哥州立大学Carl J. Carrano教授对一类配体的研究，这些配体允许供体原子、电荷、空间体积、氢键和其他因素的系统变化，这些因素对金属催化的生物转化有重要影响。配体对有机膦等受体之间氧原子转移反应的影响以及钼酶的模型将被系统地研究。新的富硫模型配合物将更接近地模拟酶的活性位点。铁的五配位配合物将被制备为几种非血红素铁加氧酶的模型，以确定供体原子集、电荷、氢键和其他控制氧合与氧化的因素的影响。伪四面体铁配合物将被合成和研究作为肽去甲酰基酶的模型，并与Co(II), Ni（II）和Zn（II）的类似配合物进行比较，以确定为什么铁（II）而不是Zn（II）在这些独特的水解酶中被自然使用。将制备相对较小的金属离子配合物，模拟酶中金属活性位点的结构和功能。研究这些复合物将有助于阐明金属离子在许多重要酶中功能的基本性质。

This award by the Inorganic, Bioinorganic and Organometallic Chemistry program supports research by Professor Carl J. Carrano at San Diego State University to study a family of ligands that allows for the systematic variance of donor atom, charge, steric bulk, hydrogen-bonding and other factors that can have an important effect on metal-catalyzed biotransformations. Ligand effects on oxygen atom transfer reactions between acceptors such as organophosphines and models for molybdoenzymes will be systematically studied. New sulfur-rich model complexes to more closely mimic enzyme active sites will be prepared. Pentaacoordinate complexes of iron will be prepared as models for several non-heme iron oxygenase enzymes in order to determine the effects of the donor atom set, charge, and hydrogen bonding and other factors that control oxygenation versus oxidation. Pseudotetrahedral iron complexes will be synthesized and studied as models for peptide deformylases and compared with analogous complexes of Co(II), Ni(II) and Zn(II) in order to determine why Fe(II) rather than Zn(II) is employed by nature in these unique hydrolytic enzymes.Relatively small complexes of metal ions will be prepared that simulate the structure and function of metal active sites in enzymes. Studying these complexes will help to elucidate the fundamental nature of the function of the metal ions in a number of important enzymes.