Heteroscorpionate Ligands: Applications to Bioinorganic Chemistry

这项由无机、生物无机和金属有机化学项目颁发的奖项支持圣地亚哥州立大学的卡尔·J·卡拉诺教授的研究，他研究了一系列配体，这些配体允许施主原子、电荷、空间体积、氢键和其他因素的系统变化，这些因素可能对金属催化的生物转化产生重要影响。将系统地研究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。将制备新的富硫模型络合物，以更接近地模拟酶的活性部位。将制备五配位铁络合物作为几种非血红素铁加氧酶的模型，以确定给体原子组、电荷和氢键以及控制氧化与氧化的其他因素的影响。我们将合成假四面体铁络合物，并将其作为肽脱甲酰基酶的模型，并与Co(II)、Ni(II)和Zn(II)的类似络合物进行比较，以确定为什么在这些独特的水解酶中自然界使用的是Fe(II)而不是Zn(II)。研究这些络合物将有助于阐明金属离子在一些重要酶中作用的基本性质。

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.