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首页> 外文期刊>Biochemistry >Spectral-Kinetic Analysis of Recombination Reaction of Heme Centers of bd-Type Quinol Oxidase from Escherichia coli with Carbon Monoxide
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Spectral-Kinetic Analysis of Recombination Reaction of Heme Centers of bd-Type Quinol Oxidase from Escherichia coli with Carbon Monoxide

机译：大肠杆菌大肠杆菌血红素氧化酶血红素中心重组反应的光谱动力学分析

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摘要

Recombination of the isolated, fully reduced bd-type quinol oxidase from Escherichia coli with carbon monoxide was studied by pulsed absorption spectrophotometry with microsecond time resolution. Analysis of the kinetic phases of recombination was carried out using the global analysis of multiwavelength kinetic data ("Global fitting"). It was found that the unresolved photodissociation of CO is followed by a stepwise (with four phases) recombination with characteristic times (tau) of about 20 mu s, 250 mu s, 1.1 ms, and 24 ms. The 20-mu s phase most likely reflects bimolecular recombination of CO with heme d. Two subsequent kinetic transitions, with tau similar to 250 mu s and 1.1 ms, were resolved for the first time. It is assumed that the 250-mu s phase is heterogeneous and includes two different processes: recombination of CO with similar to 7% of heme b(595) and transition of heme d from a pentacoordinate to a transient hexacoordinate state in this enzyme population. The 24-ms transition probably reflects a return of heme d to the pentacoordinate state in the same protein fraction. The 1.1-ms phase can be explained by recombination of CO with similar to 15% of heme b(558). Possible models of interaction of CO with different heme centers are discussed.
机译：通过脉冲吸收分光光度法研究了来自大肠杆菌的分离的，完全降低的BD型喹啉氧化酶的分离的全脂氧化物氧化酶，通过微秒时间分辨率研究了一氧化碳。使用多波长动力学数据（“全球拟合”）的全局分析进行重组动力学相的分析。结果发现，CO的未解决的光解离之后是逐步（具有四个阶段）重组，其特征时间（TAU）约为20μm，250μm，1.1ms和24ms。 20-mu S期最有可能反映与血红素d的共分子重组。两种随后的动力转换，Tau的动力学过渡是类似于250 mu s和1.1 ms的，首次得到解决。假设250-mu S相是异质的并且包括两个不同的方法：CO的重组与血红素B（595）的7％，并从五个酶群中从五个六邻四血管转变为血红素D转变。 24-ms过渡可能反映了血红素D的返回到相同的蛋白质级分中的五角形状态。 1.1-MS相可以通过与血红素B（558）的相似的CO重组来解释。讨论了不同血红中中心的CO相互作用的可能模型。

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