Mechanistic Studies of Nickel Superoxide Dismutase

生命过程化学（CLP）计划中的这一奖项支持马萨诸塞州大学的Michael Maroney教授的工作，对镍依赖性超氧化物歧化酶（一种在细菌中发现的酶）催化的超氧化物歧化机制进行基础研究。 镍超氧化物歧化酶（NiSODs）代表了一种新的方法来消除超氧化物在生物系统中，从而有助于氧解毒机制的生物多样性。 其他镍金属酶在微生物氧化还原催化中起着关键作用，包括氢的利用（氢化酶），甲烷生产（甲基辅酶M还原酶）和CO/CO2化学（一氧化碳脱氢酶和乙酰辅酶A合酶），NiSOD的研究将有助于我们对生物镍位氧化还原催化作用的认识迄今为止，其特征在于不含其他辅因子，因此提供了所涉及的化学的清晰光谱视图。 这些研究，其中使用涉及分子生物学和光谱技术的多学科方法，将有助于我们的知识的氧化还原中心的催化，将有助于合成系统的氢生产/利用和CO2还原的设计。

This award in the Chemistry of Life Processes (CLP) program supports work by Professor Michael Maroney at the University of Massachusetts to carry out fundamental studies of the mechanism of superoxide disproportionation catalyzed by nickel-dependent superoxide dismutase, an enzyme found in bacteria. Nickel superoxide dismutases (NiSODs) represent a novel approach to the elimination of superoxide in biological systems, and thus contribute to the biodiversity of mechanisms for oxygen detoxification. Other nickel metalloenzymes play critical roles in microbial redox catalysis, including hydrogen utilization (hydrogenases), methane production (methylcoenzyme M reductase), and CO/CO2 chemistry (carbon monoxide dehydrogenase and acetylcoenzyme A synthase), and are thus important catalysts in energy science.The study of NiSOD will contribute to our understanding of redox catalysis by biological nickel sites via examination the only redox nickel enzyme characterized to date that contains no other cofactors, and thus offers a clear spectroscopic view of the chemistry involved. These studies, which use a multidisciplinary approach involving molecular biological and spectroscopic techniques, will contribute to our knowledge of the design of redox centers for catalysis that will contribute to synthetic systems for hydrogen production/utilization and CO2 reduction.