Hawkes T R, McLean P A, Smith B E
Biochem J. 1984 Jan 1;217(1):317-21. doi: 10.1042/bj2170317.
When the iron-molybdenum cofactor (FeMoco) was extracted from the MoFe protein of nitrogenase from a nifV mutant of Klebsiella pneumoniae and combined with the FeMoco-deficient MoFe protein from a nifB mutant, the resultant MoFe protein exhibited the NifV phenotype, i.e. in combination with wild-type Fe protein it exhibited poor N2-fixation activity and its H2-evolution activity was inhibited by CO. These data provide strong evidence that FeMoco contains the active site of nitrogenase. The metal contents and e.p.r. properties of FeMoco from wild-type and nifV mutants of K. pneumoniae are very similar.
当从肺炎克雷伯氏菌nifV突变体的固氮酶钼铁蛋白中提取铁钼辅因子（FeMoco），并与来自nifB突变体的缺乏FeMoco的钼铁蛋白结合时，所得的钼铁蛋白表现出NifV表型，即与野生型铁蛋白结合时，其固氮活性较差，并且其放氢活性受到CO的抑制。这些数据提供了强有力的证据，证明FeMoco含有固氮酶的活性位点。肺炎克雷伯氏菌野生型和nifV突变体的FeMoco的金属含量和电子顺磁共振特性非常相似。
