首页> 外文期刊>Journal of the American Chemical Society >Mossbauer and EPR Evidence for an All-Ferrous Fe_4S_4 Cluster with S = 4 in the Fe Protein of Nitrogenase
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Mossbauer and EPR Evidence for an All-Ferrous Fe_4S_4 Cluster with S = 4 in the Fe Protein of Nitrogenase

机译:固氮酶铁蛋白中S = 4的全铁Fe_4S_4簇的Mossbauer和EPR证据

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摘要

The data reported here confirm the earlier conclusion of Watt and Reddy that the Fe protein can be reduced to an all-ferrous state. This state can also be produced using the hydroquinone form of the physiological electron donor flavodoxin. Since flavodoxin is known to serve as a one-electron donor under these conditions, this observation suggests a reason for why the Fe protein is a dimer with a single Fe_4S_4 cluster: thus, two molecules of flavodoxin may have to bind for the delivery of two electrons.
机译:此处报道的数据证实了Watt和Reddy的早期结论,即铁蛋白可以还原为全铁状态。也可以使用生理电子给体黄酮毒素的氢醌形式产生这种状态。由于已知黄素毒素在这些条件下可作为单电子供体,因此该观察结果说明了Fe蛋白是具有单个Fe_4S_4簇的二聚体的原因:因此,两个黄素毒素分子可能必须结合才能递送两个电子。

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