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Highly Selective Ligand Binding by Methylophilus methylotrophus Cytochrome c′′

机译:甲基嗜甲基菌细胞色素c''的高选择性配体结合

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摘要

Cytochrome c′′ (cyt c′′) from Methylophilus methylotrophus is unusual insofar as the heme has two axial histidine ligands in the oxidized form but one is detached when the protein is reduced. Despite cyt c′′ having an axial site available for binding small ligands, we show here that only NO binds readily to the ferrous cyt c′′. Binding of CO, as well as CN–, on the other hand requires considerable structural reorganization, or reduction of the disulfide bridge close to the heme. Standard free energies for the binding of NO and CO reveal high selectivity of the ferrous cyt c′′ for NO, indicating its putative physiological role. In this work, we characterize in detail the kinetics of NO binding and the structural features of the Fe2+–NO adduct by stopped-flow and resonance Raman spectroscopy, respectively.
机译:甲基嗜甲基菌的细胞色素c''(cyt c'')是不寻常的,因为血红素有两个轴向的组氨酸配体呈氧化形式,但是当蛋白质被还原时一个被分离。尽管cyt c''具有可用于结合小的配体的轴向位点,但在此我们显示只有NO容易与亚铁cyt c''结合。另一方面,CO和CN–的结合需要相当大的结构重组,或还原血红素附近的二硫键。用于结合NO和CO的标准自由能表明,cyt亚铁胞质c''对NO的选择性高,表明其推测的生理作用。在这项工作中,我们分别通过停止流和共振拉曼光谱详细描述了NO结合的动力学和Fe2 + -NO加合物的结构特征。

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  • 来源
    《Biochemisty》 |2011年第25期|p.5624-5632|共9页
  • 作者单位

    Instituto de Tecnologia Qumica e Biolgica, Universidade Nova de Lisboa, Av. da Repblica, 2780-157 Oeiras, PortugalDepartamento de Qumica, Faculdade de Cincias e Tecnologia, FCT, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal;

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