Site-Specific Mutation of Nitrogenase Proteins

固氮酶蛋白的位点特异性突变

• 批准号: 8808943
• 负责人: James Howard
• 金额: $ 28.82万
• 依托单位: University of Minnesota-Twin Cities
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 1988
• 资助国家: 美国
• 起止时间: 1988-09-01 至 1992-08-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=8808943&HistoricalAwards=false
• 关键词: Site; Specific; Mutation; Nitrogenase; Proteins

Nitrogen fixation component enzymes have been isolated and crystallized. The 3-dimensional structures will soon be known. The objective of this award is to the methods of side specific mutagenesis to augment biochemical and biophysical studies of the Fe-protein component. The experiments are designed to elucidate: a) the role of the five conserved cysteines, and arginine-100 and b) the amino acid residues involved in complex formation between components of nitrogenase, flavodoxin binding and ATP binding. The effects of substitutions will be studied by biochemical, biophysical and crystallographic methods. The results will enhance our understanding of the structure and function of nitrogenase, an enzyme which converts molecular nitrogen into ammonia and makes it utilizable by all the forms of life on earth.

固氮组分酶已被分离和结晶。这种三维结构很快就会为人所知。该奖项的目标是加强对铁蛋白成分的生化和生物物理研究的侧特异性突变方法。这些实验旨在阐明：a)五个保守的半胱氨酸和精氨酸-100的作用；b)参与固氮酶、黄还蛋白结合和ATP结合的组份之间形成复合体的氨基酸残基。取代的影响将通过生化、生物物理和结晶学方法进行研究。这些结果将加深我们对固氮酶的结构和功能的理解，固氮酶是一种将分子氮转化为氨并使其可被地球上所有生命利用的酶。