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首页> 外文期刊>Amino acids >Crucial aminoacids in the F-O sector of the F1FO-ATP synthase address H+ across the inner mitochondrial membrane: molecular implications in mitochondrial dysfunctions
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Crucial aminoacids in the F-O sector of the F1FO-ATP synthase address H+ across the inner mitochondrial membrane: molecular implications in mitochondrial dysfunctions

机译：在内部线粒体膜的F1FO-ATP合酶地址H +的F-O-ATP合酶地址H +中的关键氨基酸：线粒体功能障碍的分子影响

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摘要

The eukaryotic F1FO-ATP synthase/hydrolase activity is coupled to H+ translocation through the inner mitochondrial membrane. According to a recent model, two asymmetric H+ half-channels in the a subunit translate a transmembrane vertical H+ flux into the rotor rotation required for ATP synthesis/hydrolysis. Along the H+ pathway, conserved aminoacid residues, mainly glutamate, address H+ both in the downhill and uphill transmembrane movements to synthesize or hydrolyze ATP, respectively. Point mutations responsible for these aminoacid changes affect H+ transfer through the membrane and, as a cascade, result in mitochondrial dysfunctions and related pathologies. The involvement of specific aminoacid residues in driving H+ along their transmembrane pathway within a subunit, sustained by the literature and calculated data, leads to depict a model consistent with some mitochondrial disorders.
机译：真核F1FO-ATP合酶/水解酶活性通过内部线粒体膜偶联至H +易位。 根据最近的模型，亚基中的两个不对称H +半通道将跨膜垂直H +通量转化为ATP合成/水解所需的转子旋转。 沿H +途径，保守的氨基酸残基，主要是谷氨酸，地址H +在下坡和上坡跨膜运动中分别合成或水解。 负责这些氨基酸的点突变会影响通过膜的H +转移，作为级联，导致线粒体功能障碍和相关病理。 特定氨基酸残基在亚基内沿其跨膜途径驱动H +的涉及，由文献和计算的数据持续，导致与一些线粒体疾病一致的模型。

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