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ZieglerLecture10-Bioenergetics-ppt1

ZieglerLecture10-Bioenergetics-ppt1 - Lecture 10...

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Lecture 10: Lecture 10: Bioenergetics Bioenergetics Campbell & Farrell, pp. 27-32, and chapter 15 Campbell & Farrell, pp. 27-32, and chapter 15 BIOCHEMISTRY 100 Winter 2009 M. Ziegler
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Learning Objectives Learning Objectives 1. Terminology (explain/define; understand use of terms): mass action ratio, free energy change, standard free energy change, equilibrium constant, free energy coupling, metabolism, catabolism, anabolism, oxidizing agent/oxidant, reducing agent/reductant 2. Explain the difference between the standard free energy change ( Δ G o ' ) for a process/reaction and the actual or physiological free energy change ( Δ G' ) for the process.); 3. What 2 conditions (consistent with physiological conditions) make "biochemical standard conditions" different from standard conditions normally referred to in chemistry? (Assuming these conditions means the free energy change or K eq is referred to with a “prime” symbol, Δ ' .) 4. Calculate any one of the following parameters from the other two: Δ G', Δ G o ' and the actual mass action ratio (given the absolute temperature and the value of R, the gas constant). 5. Calculate Δ G o ' from K eq ' or vice versa , given the absolute temperature and the value of R, the gas constant. 6. Relate the sign of Δ G' to the direction in which a reaction will go to get to equilibrium. 7. Explain the concept of free energy coupling and additivity of free energy changes .
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Learning Objectives, continued 8. Explain the relationship of the term “high energy bond” to the (negative) free energy of hydrolysis of that bond. 9. Given 2 phosphorylated compounds and their free energies of hydrolysis (for removal of the phosphate), write a coupled reaction in which the phosphate group is transferred from one compound to the other, and H 2 O and P i cancel out of the overall coupled reaction. Draw a conclusion about in which direction it would be favorable to transfer the phosphate (from compound 1 to compound 2, or from compound 2 to compound 1). 10. Give an example of a coenzyme that carries activated acyl groups in metabolism, explain how the acyl group becomes attached to the coenzyme (reaction, and type of linkage of acyl group to coenzyme). 11. Draw ATP and ADP, and recognize NAD + /NADH, NADP + /NADPH, FAD/FADH 2 , and Coenzyme A. 12. Draw the “business end” of CoA with an acyl group on it (acyl-CoA, but not the whole coenzyme). 13. Be able to point to the position(s) in NAD + and FAD that are the “business ends” of those coenzymes, where electrons (and proton(s)) are added to give the reduced forms. You don ʼ t have to draw the oxidized or reduced forms.
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Bioenergetics: Bioenergetics: Thermodynamics and Life Thermodynamics and Life Does the existence of life on earth violate physical laws? Free energy, G, for a substance defined in terms of its enthalpy (H), entropy (S), and temperature (T) at constant pressure G = H – TS We are interested in changes ( Δ ) in free energy for cellular processes, G final – G initial : Δ G = Δ H – T Δ S Enthalpy (H): making bonds: Δ H < 0, favorable (exothermic) breaking bonds: Δ
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