The Novel Iron-Sulfur Clusters of Hydrogenase

新型氢化酶铁硫簇

• 批准号: 9105150
• 负责人: Michael Adams
• 金额: $ 27.75万
• 依托单位: University of Georgia Research Foundation Inc
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 1991
• 资助国家: 美国
• 起止时间: 1991-11-01 至 1995-04-30
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9105150&HistoricalAwards=false
• 关键词: Novel; Iron; Sulfur; Clusters; Hydrogenase

This project seeks to expand upon our knowledge of the structure, function and chemical reactivity of biological iron- sulfur (FeS) clusters, the most ubiquitous electron carriers in nature. Dr. Adams is investigating the structure and properties of a new type of FeS center, termed the H cluster, found at the catalytic site of hydrogenase. This enzyme has the unique ability to catalyze H2 oxidation and H2 production, reactions of fundamental chemical and biological significance. In two hydrogenases from the anaerobic bacterium, Clostridium pasteurianum, he has shown that the novel H cluster is comprised of four to six Fe atoms and has two nitrogenous ligands, one of which is displaced when the cluster covalently binds CO, a potent inhibitor. Further potentiometric, spectroscopic and crystallographic analyses of these enzymes are proposed. He will also investigate the biochemical and spectroscopic properties of an extremely thermophilic version of the H cluster in a tungsten-dependent FeS-Hydrogenase that has been purified from Thermotoga maritima, a unique eubacterium that grows at 90C. He has show that spectroscopic properties similar to those of the hydrogenase H cluster are exhibited by the novel FeS cluster of an exceptionally thermostable Ferredoxin from Pyrococcus furiosus, an archaebacterium that grows optimally at 100C. Further modification of this FeS center will be explored as a potential model for the H2-activating H cluster of the hydrogenases.

该项目旨在扩展我们对生物铁硫（FES）簇的结构，功能和化学反应性的了解，这是本质上最普遍的电子载体。 亚当斯博士正在研究一种新型FES中心的结构和特性，称为H簇，该中心在氢化酶的催化位点发现。 该酶具有催化H2氧化和H2产生的独特能力，基本化学和生物学意义的反应。 在厌氧菌细菌的两种氢化酶（梭菌氏梭菌）中，他表明，新型H簇由四到六个Fe原子组成，并具有两个硝基配体，其中一种是当簇共价结合co（一种有效的抑制剂）时，其中一个被移位。 提出了这些酶的进一步的电位，光谱和晶体学分析。 他还将研究H Thermotoga Maritima纯化的钨依赖性FES-Hydregenase中H簇的生物化学和光谱特性，该类别已从Thermotoga Maritima纯化，这是一种独特的卵细菌，它在90c下生长。 他表明，与氢化酶H簇相似的光谱特性是由来自富洛氏菌的异常热稳态铁氧还蛋白的新型FES簇展示的，这是一种在100C时最佳生长的古细菌。 该FES中心的进一步修改将作为H2激活H氢酶H簇的潜在模型探讨。