固氮酶铁钼辅因子插入的分子见解——钼铁蛋白α亚基中组氨酸274和组氨酸451的作用
Molecular insights into nitrogenase FeMoco insertion--the role of His 274 and His 451 of MoFe protein alpha subunit.
作者信息
Fay Aaron W, Hu Yilin, Schmid Benedikt, Ribbe Markus W
机构信息
Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.
出版信息
J Inorg Biochem. 2007 Nov;101(11-12):1630-41. doi: 10.1016/j.jinorgbio.2007.03.013. Epub 2007 Apr 19.
Abstract
The final step of FeMo cofactor (FeMoco) assembly involves the insertion of FeMoco into its binding site in the molybdenum-iron (MoFe) protein of nitrogenase. Here we examine the role of His alpha274 and His alpha451 of Azotobacter vinelandii MoFe protein in this process. Our results from combined metal, activity, EPR, stability and insertion analyses show that mutations of His alpha274 and/or His alpha451, two of the histidines that belong to a so-called His triad, to small uncharged Ala specifically reduce the accumulation of FeMoco in MoFe protein. This observation indicates that the enrichment of histidines at the His triad is important for FeMoco insertion and that the His triad potentially serves as an intermediate docking point for FeMoco through transitory ligand coordination and/or electrostatic interaction.
摘要
铁钼辅因子（FeMoco）组装的最后一步涉及将FeMoco插入固氮酶钼铁（MoFe）蛋白中的结合位点。在此，我们研究了棕色固氮菌MoFe蛋白的His α274和His α451在这一过程中的作用。我们结合金属、活性、电子顺磁共振、稳定性和插入分析得出的结果表明，His α274和/或His α451（属于所谓His三联体的两个组氨酸）突变为不带电荷的小丙氨酸会特异性降低FeMoco在MoFe蛋白中的积累。这一观察结果表明，His三联体处组氨酸的富集对于FeMoco插入很重要，并且His三联体可能通过瞬时配体配位和/或静电相互作用作为FeMoco的中间对接点。
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