EXAFS STUDIES OF NON-HEME IRON ENZYME INTERMEDIATES AND MODEL COMPOUNDS

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目及 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 非血红素酶中的双铁中心激活双氧以进行许多不同的重要代谢转化。在这些酶与O2的反应中，已经观察到各种中间体，这对于理解反应机理至关重要。XAS在建立其中一些中间体的核心结构方面发挥了关键作用。我们建议使用EXAFS研究几种非血红素二铁酶的短寿命中间体，并将它们的结构与已经报道的三种中间体进行比较。具体地说，我们将研究E.大肠杆菌，中间Q的甲烷单加氧酶（MMO）在底物的存在下，和亚稳态（但尚未结晶）模型复合物有关的氧活化化学这些nonheme二铁酶。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The diiron centers in non-heme enzymes activate dioxygen to carry out many different important metabolic transformations. In the reactions of these enzymes with O2 various intermediates have been observed which are critical for understanding the reaction mechanisms. XAS has played a key role in establishing the core structures of some of these intermediates. We propose to use EXAFS to study the short-lived intermediates of several non-heme diiron enzymes and compare their structures with those of the three intermediates already reported. Specifically, we will study the peroxo intermediate of the ferritin from E. coli, intermediate Q of methane monooxygenase (MMO) in the presence of substrate, and metastable (but as yet not crystallized) model complexes related to the oxygen activation chemistry of these nonheme diiron enzymes.