The structure of ATP synthase changes in conformation as a result of
A. the rotation of the and
subunits.
B. the rotation of the subunit.
C. the rotation of the subunit.
D. the rotation of ATP.
Choose one letter please that makes the statement correct.
The structure of ATP synthase changes in conformation as a result of A. the rotation...
A representation of the structure of the mitochondrial ATP synthase is presented in Figure 2 of this document. Notably, the chloroplast version of the spinach ATP synthase is remarkably similar to the mitochondrial version of the ATP synthase, with one notable exception. In the Fo portion of the chloroplast ATP synthase there are 14 "c" subunits. Discuss this noteworthy structural difference in the ATP synthases relative to the values you calculated in parts D and E of this problem. F)...
1220 Which is not a result of one pass through the citric acid cycle? A. 2 molecules of Co, are produced. B. 3 molecules of NADH are produced from NAD C. 1 substrate-level phosphorylation occurs to produce GTP or ATP. D. 2 QH, are produced by the succinate dehydrogenase complex. E. The oxidation of L-malate regenerates oxaloacetate. 2012 Which enzyme catalyzes a substrate-level phosphorylation reaction? A. Isocitrate dehydrogenase B. Succinyl-CoA synthetase C. Fumarase D. Aconitase E. Citrate synthase 14.30 What...
The Fo stalk component of ATP synthase is named such because it is rendered useless by the antibiotic oligomycin. Which of the following would occur in the presence of oligomycin? A. The catalytic Loose site of the FoF1 ATP Synthase would be unable to bind ADP and Pi. B. The influx of protons and the rotation of the c subunits would slow and possibly сease. C. The y subunit would dissociate from the a and B subunits. D. All of...
The rotor portion of the ATP synthase is composed of 10-14 subunits called "c subunits." As protons bind the rotor, on the intermembrane space side of the rotor, the rotor turns one subunit worth of distance. If the rotor of ATP synthase is composed of 10 c subunits, how many protons would be necessary to produce 6 ATP molecules?
13. ATP synthase is made of multiple subunits. Briefly explain role of the following subunits (4 pts). (1) a and B subunit (2) ‘a’ and “c' subunit C10
The release of ATP by the beta subunit of the F1F0 ATP Synthase is most directly dependent on: A) The flow of protons from the intermembrane space to the matrix B) The rotation of the c-ring in the membrane C) The passage of electrons along the electron transport chain D) A conformational change in the beta subunit E) None of the above
26. Place the following statements for the production of ATP by ATP synthase in order: 1. The subunit binds ADP and Pi. II. The H+ binds to an acidic amino acid side chain and the cring rotates. III. The Tsubunit forces ADP and Pi together to form ATP. IV. The L subunit trap ADP and Pi in the active site. V. The gamma subunit linked to the c-ring rotates. VI. A H+ moves from the intermembrane space into a c...
Explain why isolated F1 subunits from the ATP synthase enzyme catalyze the hydrolysis of ATP. Use protein structure, conformational changes, and free energy in your response.
please explain the answer, thanks !!!
ATP synthase is located in or on the X membrane. There are Y subunits that bind ADP and inorganic phosphate and change Z during the synthesis of ATP. х Z A outer mitochondrial two quaternary structure inner mitochondrial three conformation outer mitochondrial three conformation Ꭰ ] . cell four primary sequence 9 Consider the following reaction, which is analogous to ones you have encountered. CH сно CHz C-C-COO WE CH-C-" + A + B...
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A mutation in human ATPase 6 (which corresponds to E. coll subunit a) from leucine to arginine at position 156 may allow the movement of protons across the membrane, but not the rotation of the ring of c subunits. How might this possible mechanism affect the function of ATP synthase? Choose two answers Proton binding to subunit c would not be impaired. There would be an uncoupling of proton translocation and ATP synthesis. ATP hydrolysis coupled to proton...