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Difference between revisions of "Walker 2013 Biochem Soc Trans"

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{{Publication
{{Publication
|title=Walker JE (2013) The ATP synthase: the understood, the uncertain and the unknown. Biochem Soc Trans 41: 1-16. ย 
|title=Walker JE (2013) The ATP synthase: the understood, the uncertain and the unknown. Biochem Soc Trans 41: 1-16.
|info=[http://www.ncbi.nlm.nih.gov/pubmed/23356252 PMID: 23356252]
|info=[http://www.ncbi.nlm.nih.gov/pubmed/23356252 PMID: 23356252]
|authors=Walker JE
|authors=Walker JE
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{{Labeling
{{Labeling
|preparations=Chloroplasts
|enzymes=Complex V; ATP Synthase
|enzymes=Complex V; ATP Synthase
|topics=ATP; ADP; AMP; PCr
|topics=ATP; ADP; AMP; PCr
}}
}}

Revision as of 17:10, 7 August 2013

Publications in the MiPMap
Walker JE (2013) The ATP synthase: the understood, the uncertain and the unknown. Biochem Soc Trans 41: 1-16.

ยป PMID: 23356252

Walker JE (2013) Biochem Soc Trans

Abstract: The ATP synthases are multiprotein complexes found in the energy-transducing membranes of bacteria, chloroplasts and mitochondria. They employ a transmembrane protonmotive force, ฮ”p, as a source of energy to drive a mechanical rotary mechanism that leads to the chemical synthesis of ATP from ADP and Pi. Their overall architecture, organization and mechanistic principles are mostly well established, but other features are less well understood. For example, ATP synthases from bacteria, mitochondria and chloroplasts differ in the mechanisms of regulation of their activity, and the molecular bases of these different mechanisms and their physiological roles are only just beginning to emerge. Another crucial feature lacking a molecular description is how rotation driven by ฮ”p is generated, and how rotation transmits energy into the catalytic sites of the enzyme to produce the stepping action during rotation. One surprising and incompletely explained deduction based on the symmetries of c-rings in the rotor of the enzyme is that the amount of energy required by the ATP synthase to make an ATP molecule does not have a universal value. ATP synthases from multicellular organisms require the least energy, whereas the energy required to make an ATP molecule in unicellular organisms and chloroplasts is higher, and a range of values has been calculated. Finally, evidence is growing for other roles of ATP synthases in the inner membranes of mitochondria. Here the enzymes form supermolecular complexes, possibly with specific lipids, and these complexes probably contribute to, or even determine, the formation of the cristae. โ€ข Keywords: ATPsynthase


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Preparation: Chloroplasts  Enzyme: Complex V; ATP Synthase"Complex V; ATP Synthase" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property.  Regulation: ATP; ADP; AMP; PCr"ATP; ADP; AMP; PCr" is not in the list (Aerobic glycolysis, ADP, ATP, ATP production, AMP, Calcium, Coupling efficiency;uncoupling, Cyt c, Flux control, Inhibitor, ...) of allowed values for the "Respiration and regulation" property.