atp synthase mechanism
Other three subunits catalyze the ATP synthesis. Degradation of CCNK mediated by HQ461 compromised CDK12 function, leading to reduced phosphorylation of a CDK12 substrate, downregulation of DNA damage response genes, and cell death. We have not tested the ability of the “The proposed channels are consistent with a series of experiments probing water accessibility of residues in the 4) Based on the structure with the fixed position of bAs far as we understand, “kinetic limping” is seen in kinesin motors, where the timing of consecutive steps is unequal. Protons flow against their concentration gradient into a half-channel in subunit a Choose] FALSE TRUE Protons neutralize a lysine residue in the center of a C-subunit, allowing it to enter the membrane. 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 (Compared to their mitochondrial counterparts, bacterial ATP synthases have a simpler subunit composition. In many species this is a Glu-His pair.7) It would be interesting to know if the authors observed any features of the enzyme that are characteristic of thermophilic proteins, perhaps illustrating an adaption relative to other organisms.8) Typo: in the Discussion section "a water molecule" or "water molecules".1) It would useful if the authors compiled a table indicating which residues of each subunit appear in the model.We agree that this information is important and have added it in Table 1C.2) The following references on the elastic function of the rotor should be cited:We have cited these two important papers along with the other manuscripts that we cited earlier.The authors may, at their discretion, consider commenting on two items:3) The mechanism of FO as a whole is mono-specific for the proton, due to the almost full round of the bound proton on an acid residue of the c-ring. ATP synthase is a complex structure consisting of two domains FAccording to the current model of ATP synthesis (known as the alternating catalytic model), the proton-motive force across the inner mitochondrial membrane, generated by the electron transport chain, drives the passage of protons through the membrane via the FThe mechanism that drives ATP synthesis seems to depend upon a binding charge conception in which catalytic sites on the β-subunits have different affinities for nucleotides and are designated loose (L), tight (T), and open (O). HG was supported by an Ontario Graduate Scholarship and a University of Toronto Excellence Award.
www.mrc-mbu.cam.ac.uk/projects/2680/structure-and-function-atp-synthases We expressed the Adenosine triphosphate (ATP) synthases are multi-subunit protein complexes that use an electrochemical proton motive force across a membrane to make the cell’s supply of ATP from adenosine diphosphate (ADP) and inorganic phosphate (Pi). Mutagenesis of the alpha subunit of the F1Fo-ATPase from Escherichia coli. The authors focused on the half-channels to the conserved Glu residues of the All 3 referees agreed that the data are convincing, the manuscript makes major contributions towards understanding the function of bacterial ATP synthases and that the article is very well written.1) It would useful if the authors compiled a table indicating which residues of each subunit appear in the model.2) The following references on the elastic function of the rotor should be cited:The authors may, at their discretion, consider commenting on two items:3) The mechanism of FO as a whole is mono-specific for the proton, due to the almost full round of the bound proton on an acid residue of the c-ring. After reading this article you will learn about the structure and mechanism of ATP synthase, with the help of suitable diagrams. The authors found water access. Mechanism of the F 1 ATP-ase . The resolution of the structures reached 3.0-3.1 Å, allowing a close look at several important features of the enzyme.a) Species specific structural differences are related to different inhibition of ATP hydrolysis by the ε-subunit. This effect on ETC complexes appears to be independent of protein lipoylation, the best characterized function of mtFAS, as mutants lacking lipoylation have an intact ETC. (links to download the citations from this article in formats compatible with various reference manager tools) (links to open the citations from this article in various online reference manager services)
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