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首页> 外文期刊>Protoplasma: An International Journal of Cell Biology >Proton conduction through full-length gp91(phox) requires histidine 115
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Proton conduction through full-length gp91(phox) requires histidine 115

机译：通过全长gp91（phox）的质子传导需要组氨酸115

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摘要

The NADPH oxidase of neutrophils is a transmembrane electron transfer complex, containing a flavin adenine dinucleotide and two hemes, all of which are suggested to be contained within gp91(phox), one of four subunits of the enzyme. The transfer of electrons through the NADPH oxidase is associated with an efflux of protons. gp91(phox) has previously been demonstrated to function as the proton conduction pathway. The mutation of histidines 111, 115, and 119 to leucines and of histidine 115 to leucine within the N- terminal 230-amino-acid fragment of gp91(phox) has previously been demonstrated to result in the loss of proton conduction through this N-terminal fragment. In this paper we have investigated the role of these histidines in proton conduction by the full-length gp91(phox). Stable CHO cell lines were established which expressed full-length gp91(phox) in which histidines 111,115, and 119 had been mutated to leucines (CH091H111/115/119) and in which histidine 115 had been mutated to leucine (CHO91H115L). The expression of gp91(phox) and its cellular localisation in these cell lines were comparable between wild-type and the mutant gp91(phox). The mutation of histiclines 111 115. and 119 to leucines or just histidine 115 to leucine resulted in an almost total loss of both the arachidonate-activated influx and efflux of protons, in comparison with that observed for wild-type gp91(phox). Therefore. histidine 115 is required for proton conduction by both full-length gp91(phox) and the N-terminal 230-amino-acid fragment of gp91(phox). Histidine 115 has recently been proposed to act as a coordinating ligand for the outer heme iron of the NADPH oxidase. On the basis of observations for cytochrome c oxidase, we propose a model for this dual role of histidine 115. [References: 19]
机译：中性粒细胞的NADPH氧化酶是一种跨膜电子转移复合物，包含黄素腺嘌呤二核苷酸和两个血红素，所有这些血红素都建议包含在该酶四个亚基之一的gp91（phox）中。电子通过NADPH氧化酶的转移与质子的流出有关。 gp91（phox）先前已被证明可以充当质子传导途径。先前已证明，gp91（phox）N端230个氨基酸片段内的组氨酸111、115和119突变为亮氨酸，而组氨酸115突变为亮氨酸导致通过该N-的质子传导损失。末端片段。在本文中，我们研究了这些组氨酸在全长gp91（phox）质子传导中的作用。建立表达全长gp91（phox）的稳定CHO细胞系，其中组氨酸111,115和119已突变为亮氨酸（CH091H111 / 115/119），而组氨酸115已突变为亮氨酸（CHO91H115L）。在这些细胞系中，gp91（phox）的表达及其细胞定位在野生型和突变型gp91（phox）之间是可比的。与野生型gp91（phox）相比，组氨酸111 115和119突变为亮氨酸，或仅组氨酸115突变为亮氨酸，导致花生四烯酸激活的流入和质子流出几乎完全丧失。因此。组蛋白115是全长gp91（phox）和gp91（phox）N端230个氨基酸片段进行质子传导所必需的。最近已提出组氨酸115充当NADPH氧化酶的外血红素铁的配位配体。根据细胞色素C氧化酶的观察结果，我们提出了一种组氨酸115双重作用的模型。[参考文献：19]

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