Redox Chemistry of 2His-1 Carboxylate Metalloenzymes

描述（由申请人提供）：一种常见的金属结合基序，即2- his -l-羧酸酯（2H-1D/E）表面三元，正在金属酶中出现，催化双氧活化。这些酶催化一系列“重要的代谢转化”。这些依赖于2H-1D/E的金属中心的还原-氧化（氧化还原）电位被认为在这种双氧活化中起重要作用，而这一提议的目标是更好地理解这种作用。具体来说，本研究旨在通过2H-1D/E金属结合基序表征金属酶的静止M2+和氧化M3+状态之间的氧化还原电位。这项研究将为比较该酶家族中的金属中心提供一个基准，从而开始收集描述2H-1D/E金属结合基序的物理性质。为此，我们建议对化学氧化的2H-1D/E依赖金属中心进行光谱和化学表征。利用一系列与二氧相关的物质探测这些中心，我们将探索这些活性中心的化学性质，明确地寻找与它们的反应机制中提出的中间体相似的中间体。

DESCRIPTION (provided by applicant): A common metal binding motif, namely the 2-His-l-carboxylate (2H-1D/E) facial triad, is emerging in metalloenzymes that catalyze dioxygen activation. These enzymes catalyze a diverse range of "metabolically important transformations. The reduction-oxidation (redox) potentials of these 2H-1D/E dependent metal centers are proposed to play an important role in this dioxygen activation, and it is the goal of this proposal to better understand this role. Specifically, this study aims to characterize the redox potential between the resting M2+ and the oxidized M3+ states of metalloenzymes with the 2H-1D/E metal binding motif. This study will provide a benchmark to compare metal centers within this family of enzymes, thus beginning a collection of physical properties describing the 2H-1D/E metal binding motif. To do this, we propose to characterize the chemically oxidized 2H-1D/E dependent metal centers both spectroscopically and chemically. Probing these centers with a series of dioxygen related species, we will explore the chemistry of these active centers, explicitly searching for intermediates similar to those proposed in their reaction mechanisms.