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After picking off from the trees some fruits and put them in a box, do they generate heat? , if yes how much in [j/s], if no, why not?
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- Assume that the complete combustion of one mole of glucose to carbon dioxide and water liberates 2870 kJ/mol (AGo' = -2870 kJ/mol). If one contraction cycle in muscle requires 67 kJ, and the energy from the combustion of glucose is converted with an efficiency of 35% to contraction, how many contraction cycles could theoretically be fueled by the complete combustion of one mole of glucose? Round your answer to the nearest whole number. суycles per mole glucoseOne step of the cycle that incorporates CO2 into glyceraldehyde in plants is the production of two 3-phosphoglycerates. ΔG = -3.5 kJ/mol for thisreaction. Is this process endergonic or exergonic?A research group discovers a new version of happyase, which they call happyase*, that catalyzes the chemical reaction: HAPPY-SAD The researchers begin to characterize the enzyme. The researchers determined the kcat of the enzyme to be 452 s-1. In a separate experiment with [E;) at 1.5 nM and [HAPPY) at 38 µM, the researchers find that Vo is equal to 320 nM s-1. What is the measured Km of happyase* for its substrate HAPPY? Make sure to include units in the answer.
- Two answers of correct, but which?A 75 kg person doing light work requires about 3000 kcal of food energy perday, 40% of which is actually used by the body’s cells. (The other 60% is lostas heat and in waste products.) Before being used by the cells, effectively allof this energy is stored in ATP, which is then cleaved into ADP and PO3−2 , with the release of 12.5 kcal per mole of ATP.(a) How many moles of ATP are turned over per day in this fashion? Whatmass of ATP does this correspond to? (The molecular weight of ATP is507 g/mol.)(b) The body actually contains approximately 5 g ATP. Estimate the averagerecycle time for an ATP molecule. You see that it is much more efficientto reuse ADP rather than to synthesize it de novo (from scratch).An enzyme is found that catalyzes the reaction X ⇌ Y. Researchers find that the Km for the substrate X is 4 μM, and the kcat is 20 min−1.(a) In an experiment, [X] = 6 mM, and V0 = 480 nM min−1. What was the [Et] used in the experiment?(b) In another experiment, [Et] = 0.5 μM, and the measured V0 = 5 μM min−1. What was the [X] used in the experiment?(c) The compound Z is found to be a very strong competitive inhibitor of the enzyme, with an α of 10. In an experiment with the same [Et] as in (a), but a different [X], an amount of Z is added that reduces V0 to 240 nM min−1. What is the [X] in this experiment?(d) Based on the kinetic parameters given above, has this enzyme evolved to achieve catalytic perfection? Explain your answer briefly, using the kinetic parameter(s) that define catalytic perfection.
- Can you help solve this problem?From data in Table 13-6, calculate the ΔG′° value for the following reactions:(a) Phosphocreatine + ADP → creatine + ATP(b) ATP + fructose → ADP + fructose 6-phosphateThis process requires 151 kJ for every 1.00 mol of Fe3O4 reduced. How much energy (in kilojoules) is required to produce 55 g of iron?