Site-Specific Mutation of Nitrogenase Proteins

对固氮组分酶进行了分离和结晶。三维结构很快就会为人所知。该奖项的目的是为了提高对铁蛋白成分的生化和生物物理研究的特异性诱变方法。实验旨在阐明：a) 5个保守的半胱氨酸和精氨酸-100的作用；b)参与氮酶组分之间复合物形成的氨基酸残基，黄氧还蛋白结合和ATP结合。取代的影响将通过生物化学、生物物理和晶体学方法进行研究。这一结果将增强我们对氮酶的结构和功能的理解，氮酶是一种将分子氮转化为氨并使其被地球上所有形式的生命所利用的酶。

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.