Mechanistic Studies of Nickel Superoxide Dismutase

镍超氧化物歧化酶的机理研究

• 批准号: 1111462
• 负责人: Michael Maroney
• 金额: $ 37.8万
• 依托单位: University of Massachusetts Amherst
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-08-01 至 2015-07-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=1111462&HistoricalAwards=false
• 关键词: Mechanistic; Studies; Nickel; Superoxide; Dismutase

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.

生命过程化学（CLP）项目的这一奖项支持了马萨诸塞州大学的Michael Maroney教授对镍依赖的超氧化物歧化酶（一种在细菌中发现的酶）催化的超氧化物歧化机制的基础研究。镍超氧化物歧化酶（NiSODs）代表了一种消除生物系统中超氧化物的新途径，从而促进了氧解毒机制的多样性。其他镍金属酶在微生物氧化还原催化中发挥重要作用，包括氢利用（氢化酶）、甲烷产生（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合成酶），因此是能源科学中的重要催化剂。NiSOD的研究将有助于我们通过检测迄今为止唯一表征的不含其他辅助因子的氧化还原镍酶来理解生物镍位点的氧化还原催化作用，从而为所涉及的化学提供清晰的光谱视图。这些研究采用了涉及分子生物学和光谱技术的多学科方法，将有助于我们设计用于催化氧化还原中心的知识，这将有助于氢生产/利用和二氧化碳减排的合成系统。