Cyclic photophosphorylation uses two photons to generate one ATP. If the AG of ATP hydrolysis is -50 kj/mol. What is the percent efficiency of cyclic photophosphorylation? F =96.5 kj/mol*V. Use AG=-nFAV → Show Transcribed Text to solve.
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- In cyclic photophosphorylation, it is estimated that two electrons must be passed through the cycle to pump enough protons to generate one ATP. Assuming that the AG for hydrolysis of ATP under conditions existing in the chloroplast is about –50 kJ/mol, what is the corresponding percent ef- ficiency of cyclic photophosphorylation, using light of 700 nm?Calculate (in kJ/mol) the energy that is required by the Rhodopseudomonas viridis photophosphorylation system to synthesize 3 ATP? (Assume that the R. viridis F1F-ATP synthase c-subunit rotor contains 12 c-subunits and that the R. viridis cytochrome b/c complex translocates 2 H/e". Also assume that the wavelength of lig! is 680 nm.) Number of photons required to synthesize 3 ATP = photons Energy = kJ/molStaphylococcal nuclease has a ΔΔG‡ of -84.1 kJ mol-1 at 25.0 °C. If the uncatalyzed rate is 0.630x10-13 µmol s-1, calculate the enzyme-catalyzed rate in µmol s-1. (Use R = 8.3145 J mol-1 K-1)
- The Relative Efficiency of ATP Synthesis in Noncyclic versus Cyclic Photophosphorylation If noncyclic photosynthetic electron transport leads to the translocation of 7 H+/2e- and cyclic photosynthetic electron transport leads to the translocation of 2 H+/e-, what is the relative photosynthetic efficiency of ATP synthesis (expressed as the number of photons absorbed per ATP synthesized) for noncyclic versus cyclic photophosphorylation? (Assume that the CF1CF0-ATP synthase yields 3 ATP/14 H+.)The muscle enzyme lactate dehydrogenase catalyzes the reaction NADH and NAD+ are the reduced and oxidized forms, respectively, of the coenzyme NAD. Solutions of NADH, but not NAD+, absorb light at 340 nm. This property is used to determine the concentration of NADH in solution by measuring spectrophotometrically the amount of light absorbed at 340 nm by the solution. Explain how these properties of NADH can be used to design a quantitative assay for lactate dehydrogenase.Neutral sphingomyelinase 2 converts sphingomyelin into ceramide and phosphorcholine. What kind of enzyme is it? Assume Vmax is 35 µM min-1. When you provide 3.0 x 10-5 M of sphingomyelin, you observe an initial velocity of 6.0 µM min-1. Calculate the KM.
- How many moles of ATP could theoretically be synthesized under standard conditions using the energy of the photons in red light (λ = 700 nm).The standard reduction potential for ubiquione (A or coenzyme Q) is .045 V, and the standard reduciton potential (E) for FAD is -0.219 V. Using these values, show that the oxidation for FADH2 by ubiquinone theoretically liberates enough energy to drive the synthesis of ATP. Faraday constant =96.48KJ/Vol delta G' standard for ATP Synthesis is +30.5 KJ/mol R=8.314 J/mol K=1.987 cal/mol KYou are isolating mitochondria from insect cells and incubating in a test tube with 0.005 M FADH2, 0.05 M ADP and 0.05 M Pi. Assuming, these 3 can enter mitochondria at no cost,no glucose/products of glucose metabolism remain in the isolated mitochondria, and oxygen is present. Part 1) If all expected reactions go to completion, how much ATP is expected formed? (0 M)(0.02 M) (0.03 M) (0.05 M) (0.1 M) (0.005 M) (0.01 M) (0.015 M) Part 2) The ratio of FADH2/FAD at completion of all expected reactions would be? (2) (>>2) (0) (1) Part 3) After completion of all expected reactions, ratio of H ion concentration inside vs. outside the mitochondrial inner membrane should be? (<1) (~1) (>1)(0) Please provide brief explanation
- Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) 0.20 per minute 0.50 per minute 1.0 per minute 2.0 per minute 5.0 per minuteATP Synthase is known to catalyze the synthesis of ATP with a ΔG°’ close to zero, and a Keq' close to 1. Why is the value of ΔG°’ different from the known value which is 30.5 kJ/mol (the energy for the reverse of ATP hydrolysis)? If the Keq' value is close to one, how is it ensured that the reaction is driven to the product side and more ATP is obtained?ATP can be hydrolyzed into ADP + inorganic phosphate (P.) with a AG of -30500 J/mol. If, galactose-1-phosphate can be hydrolyzed into galactose + P, with a AG of -15.3 kJ/mol what is the Gibbs free energy change for the reaction of galactose + ATP = galactose-1-phospate + ADP? O a. -45.8 kJ/mol O b. 15.2 kJ/mol Oc. -30484.7 J/mol O d. -15.2 kJ/mol Oe. -1520 J/mol