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-1-羧酸酯（2 H-1D/E）面三联体，出现在催化双氧活化的金属酶中。这些酶催化多种多样的“代谢重要转化”。这些2 H-1D/E依赖的金属中心的还原-氧化（氧化还原）电位被提出在这种分子氧活化中起重要作用，并且本提案的目标是更好地理解这种作用。具体而言，本研究的目的是表征与2 H-1D/E金属结合基序的金属酶的静息M2+和氧化M3+状态之间的氧化还原电位。这项研究将提供一个基准，比较金属中心在这个家庭的酶，从而开始收集的物理性质描述的2 H-1D/E金属结合基序。要做到这一点，我们建议表征的化学氧化2 H-1D/E依赖的金属中心光谱和化学。探测这些中心与一系列的分子氧相关的物种，我们将探索这些活性中心的化学，明确寻找类似的中间体，在他们的反应机制提出。

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.