Structure And Function Of Atp Synthase Pdf

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A concise overview of the chloroplast ATP synthase is presented, with an emphasis on its functions, regulation, composition, and structure from fluorescence energy transfer mapping.

Skip to main content Skip to table of contents. This service is more advanced with JavaScript available. Encyclopedia of Biophysics Edition. Editors: Gordon C.

ATP Synthases from Archaea: Structure and Function

As for every enzyme, the laws of thermodynamics command it; however, it is privileged to have a dedicated molecular regulator that controls its rotation. Recent evidence has also demonstrated that IF 1 may control the alignment of the enzyme along the mitochondrial inner membrane, thus increasing the interest for the molecule. We conceived this review to outline the fundamental knowledge of the F 1 F o -ATPsynthase and link it to the molecular mechanisms by which IF 1 regulates its way of function, with the ultimate goal to highlight this as an important and possibly unique means to control this indispensable enzyme in both physiological and pathological settings. It is present in bacteria and intracellular organelles such as chloroplasts and mitochondria. The molecular structure, catalytic mechanism, and regulation of the mitochondrial F 1 F o -ATPsynthase were described by the seminal work of the Nobel Laureates Mitchell, Boyer and Walker, that revealed its complexity and the functional steps that drive the synthesis of ATP. IF 1 is primarily responsible for inhibiting the hydrolysis of ATP by the ATP synthase [ 6 ], an event that occurs when the electrochemical proton gradient across the mitochondrial inner membrane is lost e.

Mitochondrial ATP synthase: architecture, function and pathology

Bacterial ATP synthases have been studied extensively because they are the simplest form of the enzyme and because of the relative ease of genetic manipulation of these complexes. We expressed the Bacillus PS3 ATP synthase in Eschericia coli , purified it, and imaged it by cryo-EM, allowing us to build atomic models of the complex in three rotational states. The architecture of the membrane region shows how the simple bacterial ATP synthase is able to perform the same core functions as the equivalent, but more complicated, mitochondrial complex. The structures reveal the path of transmembrane proton translocation and provide a model for understanding decades of biochemical analysis interrogating the roles of specific residues in the enzyme. These enzymes are found in bacteria and chloroplasts as monomers, and in mitochondria as rows of dimers that bend the inner membrane to facilitate formation of the mitochondrial cristae Davies et al. Proton translocation across the membrane-embedded F O region of the complex occurs via two offset half-channels Vik and Antonio, ; Junge et al. The passage of protons causes rotation of a rotor subcomplex, inducing conformational change in the catalytic F 1 region to produce ATP Walker, while a peripheral stalk subcomplex holds the F 1 region stationary relative to the spinning rotor during catalysis.

Mitochondrial ATP synthase: architecture, function and pathology

J Gen Physiol 1 December ; 6 : — The nature of this turbine-like energy conversion mechanism has been elusive for decades, owing to the lack of definitive structural information on subunit a or its c -ring interface. In a recent breakthrough, several structures of this complex were resolved by cryo—electron microscopy cryo-EM , but the modest resolution of the data has led to divergent interpretations. Moreover, the unexpected architecture of the complex has cast doubts on a wealth of earlier biochemical analyses conducted to probe this structure. Here, we use quantitative molecular-modeling methods to derive a structure of the a — c complex that is not only objectively consistent with the cryo-EM data, but also with correlated mutation analyses of both subunits and with prior cross-linking and cysteine accessibility measurements.

Human mitochondrial mt ATP synthase, or complex V consists of two functional domains: F 1 , situated in the mitochondrial matrix, and F o , located in the inner mitochondrial membrane. This review covers the architecture, function and assembly of complex V. The role of complex V di-and oligomerization and its relation with mitochondrial morphology is discussed. Finally, pathology related to complex V deficiency and current therapeutic strategies are highlighted.

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  3. Leonides A. 17.05.2021 at 12:19

    A multi subunit structure that works like a pump functions along the proton gradient across the membranes which not only results in ATP synthesis and breakdown, but also facilitates electron transport. The Mitochondrial Electron transport chain and ATP synthase.

  4. Georges G. 18.05.2021 at 10:32

    A multi subunit structure that works like a pump functions along the proton gradient across the membranes which not only results in ATP synthesis and.