固氮酶铁钼辅因子的金属和硫组成
Metal and sulfur composition of iron-molybdenum cofactor of nitrogenase.
作者信息
Nelson M J, Levy M A, Orme-Johnson W H
出版信息
Proc Natl Acad Sci U S A. 1983 Jan;80(1):147-50. doi: 10.1073/pnas.80.1.147.
Abstract
The sulfur content of N-methylformamide solutions of cofactor from Clostridium pasteurianum nitrogenase has been determined to be 11.9 (+/- 0.9) mol per mol of molybdenum. This number was determined radiochemically, using iron-molybdenum cofactor isolated from molybdenum-iron protein from bacteria grown on 35SO4. A total of 3.2 (+/- 0.2) mol of sulfur per mol of molybdenum was found to be present in cysteine and methionine, probably arising from contaminating proteins not intrinsic to the cofactor. Combined with accumulated evidence that is discussed, these results lead to an updated stoichiometry of MoFe6S8 or 9, not MoFe6S4 as previously thought, for this cluster.
摘要
已测定来自巴氏梭菌固氮酶的辅因子在N-甲基甲酰胺溶液中的硫含量为每摩尔钼11.9（±0.9）摩尔。这个数值是通过放射化学方法测定的，使用的是从在35SO4上生长的细菌的钼铁蛋白中分离出的铁钼辅因子。发现每摩尔钼中共有3.2（±0.2）摩尔的硫存在于半胱氨酸和蛋氨酸中，这可能源于并非该辅因子固有的污染性蛋白质。结合所讨论的累积证据，这些结果得出该簇合物的化学计量比更新为MoFe6S8或9，而非之前认为的MoFe6S4。
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