Comparison of redox and ligand binding behaviour of yeast and bovine cytochrome c oxidases using FTIR spectroscopy.

Comparison of redox and ligand binding behaviour of yeast and bovine cytochrome c oxidases using FTIR spectroscopy.
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DOI:
10.1016/j.bbabio.2018.05.018
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发表时间:
2018-09
期刊:
Biochimica et biophysica acta. Bioenergetics
影响因子:
--
通讯作者:
Rich PR
Rich PR
中科院分区:
其他
文献类型:
--
作者:
Maréchal A;Hartley AM;Warelow TP;Meunier B;Rich PR

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将酵母细胞色素C氧化酶WT及其突变体的氧化还原和CO光解FTIR光谱与牛和脱氮假单胞菌CCOS的氧化还原和CO光解FTIR光谱进行了比较,以建立共同的功能特征。所有显示的变化都可以归因于它们的E242(牛编号)等效物和弱H键水分子。在牛CCO的1736 cm−1上报告的另外一个氧化还原敏感带,以前被指定为D51,在酵母CCO中缺失,并且不能通过在酵母蛋白的对等位置引入D残基来恢复。酵母菌CcO的氧化还原光谱在酰胺I区的变化也要小得多,这可能与D51附近区域和亚基I/II界面的结构差异有关。给出了WT和突变酵母CcO在氧化还原诱导下的FTIR差谱。功能相关的特征与其他A1型血红素铜氧化酶进行了比较。在氧化还原方面,都显示了牛残留物E242的微扰,将牛D51引入酵母中不会产生额外的IR氧化还原带。FR-CO形式的光解均表现为E242和水分子的微扰
Redox and CO photolysis FTIR spectra of yeast cytochrome c oxidase WT and mutants are compared to those from bovine and P. denitrificans CcOs in order to establish common functional features. All display changes that can be assigned to their E242 (bovine numbering) equivalent and to weakly H-bonded water molecules. The additional redox-sensitive band reported at 1736 cm−1 in bovine CcO and previously assigned to D51 is absent from yeast CcO and couldn't be restored by introduction of a D residue at the equivalent position of the yeast protein. Redox spectra of yeast CcO also show much smaller changes in the amide I region, which may relate to structural differences in the region around D51 and the subunit I/II interface. Redox-induced FTIR difference spectra of WT and mutant yeast CcO are presented. Functionally-relevant features are compared with other A1-type haem copper oxidases. On oxidoreduction, all show perturbations of bovine residue E242 Introduction of bovine D51 in yeast doesn't result in an additional IR redox band. On photolysis of the FR-CO form all show perturbations of E242 and water molecules
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