Tracking protons from respiratory chain complexes to ATP synthase c-subunit: The critical role of serine and threonine residues

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• 作者：Isabella Panfoli^a ; Marco Ponassi^b ; Silvia Ravera^a ; Daniela Calzia^a ; Maider Beitia^c ; ^d ; ^e ; Alessandro Morelli^a ; Camillo Rosano^b ; ^{camillo.rosano@gmail.com}
• 关键词：ATP synthase ; Mitochondria ; Bioenergetics ; Proton wires ; Molecular modelling
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2017
• 出版时间：22 January 2017
• 年：2017
• 卷：482
• 期：4
• 页码：922-927
• 全文大小：2089 K
• 卷排序：482

文摘

F1Fo-ATP synthase is a multisubunit enzyme responsible for the synthesis of ATP. Among its multiple subunits (8 in E. coli, 17 in yeast S. cerevisiae, 16 in vertebrates), two subunits a and c are known to play a central role controlling the H+ flow through the inner mitochondrial membrane which allows the subsequent synthesis of ATP, but the pathway followed by H+ within the two proteins is still a matter of debate. In fact, even though the structure of ATP synthase is now well defined, the molecular mechanisms determining the function of both F1 and FO domains are still largely unknown. In this study, we propose a pathway for proton migration along the ATP synthase by hydrogen-bonded chain mechanism, with a key role of serine and threonine residues, by X-ray diffraction data on the subunit a of E. coli Fo.