Why was it necessary to use phosphoaminophosphohlc (ANP) in the ATP synthase enzyme active site rather than ATP to resolve the molecular structure of the ATP synthase active site by x-ray crystallography?
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- 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 KCan someone please show your work for tracking the radiolabel: draw structures indicating position of the radiolabeled carbon, giving names (not abbreviations) of metabolites and enzymes, The cell needs ribose 5-phosphate and NADPH. Note the structure, shown above – this is used as a starting point for the formation of ribose 5-phosphate while also generating NADPH. The red asterisk (*) denotes a radiolabeled carbon - where would the radiolabel end up? List all the names’ enzymes and intermediates involved in this conversion. Show all structures.If a reaction has a ΔG°′ value of at least −30.5 kJ · mol−1, suffi -cient to drive the synthesis of ATP (ΔG°′ = 30.5 kJ · mol−1), can it still drive the synthesis of ATP in vivo when its ΔG is only −10 kJ · mol−1? Explain.
- In the first step of the aldolase reaction, an active site Lys229 residue, with its side chain amino group in the deprotonated state, acts as a nucleophile and attacks the carbonyl C2 carbon of fructose 1,6-bisphosphate to form a Schiff base (boxed in the scheme). Since the pKa of the Lys side chain amino group in free solution is ~10.5, the pKa of Lys229 side chain must have been perturbed to a (higher lower) value for the enzyme to be active at neutral pH. the answer should include sufficient details, including the definition of pKa.When ATP and xylose are added to hexokinase, the enzyme produces a small amount of xylose-5-phosphate along with a large amount of ADP. How does this observation support the induced fit model?The mechanism involved in the reaction catalyzed by phosphoglyceromutase is known to involve a phosphorylatedenzyme intermediate. If 3-phosphoglycerate is radioactively labeledwith 32P, the product of the reaction, 2-phosphoglycerate, does nothave any radioactive label. Design a mechanism to explain these facts.
- Some anaerobic prokaryotes use nitrate (NO3- ) as the terminal electronacceptor for energy metabolism. Assuming 100% effi ciency, how much ATP could be synthesized by the oxidation of NADH by nitrate?The metabolism of alcohol pathway is showed in the figure characterized by biotransformation of: (Figure : Ethanol Metabolism Pathway - ADH : Alcohol dehydrogenases, ALDH: Aldehyde dehydrogenase ) (a) reaction phase I with two oxidations (b) reaction phase II with oxidation and sulfonation (c) reaction phase II with two hydrolysations (d) reaction phase II with two oxidations (e) reaction phase I with hydrolysis and oxidationA newly identified bacterium is unable to synthesize ubiquinone. A mobile electron carrier called CXC3 is used as a substitute. From the information provided in the table, calculate the delta G knot prime and the Keq value at 298 K for the redox reaction that occurs in this bacterium’s electron transport chain. Explain the impact that using CXC 3 instead of ubiquinol will have on ATP production in the cell. How might this cell adapt to this situation?
- Whatis the main idea behind the conformational coupling mechanism for ATP synthase? Describe the three conformational states.Select the following enzymes that utlize a mechanism involving covalent catalysis. Select ALL that apply: a) aldolase class 1 b) glyceraldehyde 3 phosphate dehydrogenase c) aldolase class 2 d) triose phosphate isomerase e) hexokinaseThe 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.