Abstract:
:The molecular mechanism by which the membrane-embedded FO sector of the mitochondrial ATP synthase translocates protons, thus dissipating the transmembrane protonmotive force and leading to ATP synthesis, involves the neutralization of the carboxylate residues of the c-ring. Carboxylates are thought to constitute the binding sites for ion translocation. In order to cast light on this mechanism, we exploited N,N'-dicyclohexylcarbodiimide, which covalently binds to FO c-ring carboxylates, and ionophores which selectively modulate the transmembrane electric (Δφ) and chemical (ΔpH) gradients such as valinomycin, nigericin and dinitrophenol. ATP hydrolysis was evaluated in mitochondrial preparations and/or inside-out submitochondrial particles from mussel and mammalian tissues under different experimental conditions. The experiments pointed out striking similarities between mussel and mammalian mitochondrial ATP synthase. Our results support the hypothesis that the ATP synthase of Mytilus galloprovincialis induces intersubunit torque generation and translocates H(+) by coordinating the hydronium ion (H3O(+)) in the ion binding site of FO. Our results are consistent with the hypothesis that in mussel mitochondria the main component of the electrochemical gradient driving proton flux and ATP synthesis is Δφ. Therefore, mussel FO probably contains a small c-ring, which implies a low bioenergetic cost of making ATP as in mammals. These features which make mussel mitochondria as efficient in ATP production as mammalian ones may be especially advantageous in facultative aerobic species which intermittently exploit mitochondrial respiration to generate ATP.
journal_name
J Bioenerg Biomembrjournal_title
Journal of bioenergetics and biomembranesauthors
Nesci S,Ventrella V,Trombetti F,Pirini M,Pagliarani Adoi
10.1007/s10863-013-9504-1subject
Has Abstractpub_date
2013-06-01 00:00:00pages
289-300issue
3eissn
0145-479Xissn
1573-6881journal_volume
45pub_type
杂志文章abstract::Specific molecular interactions that determine many of the functions of a biomembrane have a high probability of occurring at the surface of that membrane. However, unlike their hydrophobic core, the polar-apolar interface of biomembranes has been somewhat neglected experimentally. Reasons for this are that the chemic...
journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
pub_type: 杂志文章,评审
doi:10.1007/BF00762689
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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