Suppose you synthesize an ATP synthase that was devoid of the y (gamma) subunit. How would the catalytic sites of the B subunits of such an enzyme compare to one another? Why? What if only the c-terminus of the y subunit is missing?
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- Discuss the relationship between redox potentials E0’ and the organization of the components of the electron transport chain. Be specific, i.e., use data/actual values to back up your discussion. a) What are the values of E0’ for all the components of the ETS? b)How are the E0’ related to ∆G values? c) How do the values of E0’ vary among the participants in the ETS relative to their position in the ETS?ATP Synthase is known to catalyze the synthesis of ATP with a ΔG°’ close to zero, and a Keq' close to. 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?Based on your knowiedge of oxidative phosphorylation, answer the following questions: a) Suppose you synthesize an ATP synthase that was devoid of the y (gamma) subunit. How would the catalytic sites of the B subunits of such an enzyme compare to one another? Why? What if only the c-terminus of the y subunit is missing?
- Given the following information, calculate the catalytic efficiency of the enzyme. Step by step please [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμMTwo biochemistry students are about to usemitochondria isolated from rat liver for an experiment on oxidative phosphorylation. The directions for the experiment specifyaddition of purified cytochrome c from any source to the reactionmixture. Why is the added cytochrome c needed? Why does thesource not have to be the same as that of the mitochondria?Back in 1962, Gerhart and Pardee developed a model for the regulation of the activity of the ATCase enzyme by CTP and ATP, using the pathway given in Figure 1. Describe that model, using information presented here as well as what you have learned about allosteric enzymes. Be sure to include a sentence explaining the physiological significance of your model.
- When enzyme solutions are heated, there is a progessive loss of catalytic activty over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 degrees Celsius lost 50% of its activity in 12 minutes, but when incubated at 45 degrees Celsius in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 minutes. Suggest why thermal denaturation of hexokinase was retarded in the presence of one substrates.At what substrate concentration would an enzyme with a kcat of 25.0 s-1 and a KM of 3.5 mM operate at 25% of its maximal rate? How many reactions would the enzyme catalyze in 45 seconds when it is fully saturated with substate, assuming the enzyme has one active site?Identify each reaction catalyzed by (a) a nucdeotidase; (b) a phosphorylase; (c) a phosphoribosyltransferase. GMP A D E Guanine Guanosine F
- A substrate is converted to a product via the reaction sequence (1) E +S ES k2 (2) ES + S ES2 k4 (3) ES2 ES +P (4) ES , E +P (a). Using pseudo-steady state hypothesis for various forms of enzyme active sites, obtain relations between rates of individual steps in the mechanism. (b). Relating concentrations of vacant active sites to concentrations of occupied active sites, obtain expressions for the rate of consumption of S, (-Rs), and the rate of formation of P, Rp. (c). What are the maximum values of (-Rs) and Rp and under which conditions are these attained?When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 450C lost 50% of its activity in 12 minutes, but when incubated at 450C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 minutes. Suggest why thermal denaturation of hexokinase was retarded in the presence of one substratesDraw the catalytic mechanism of the reaction catalyzed by glyceraldehyde 3-phosphate dehydrogenase(GAPDH). In this reaction, which amino acid acts as a nucleophile? Which compound is oxidized andwhich is reduced? Which product is referred to as a “high-energy compound” and why?