Bioenergetics and Enzymology — DU B.Sc. (Hons.) Zoology Previous Year Question Papers

Draw neat, well labelled diagrams and structures, wherever required. 1. (a) Define the following (i) Electrostatic bond (iii) Binding energy (iv) Redox potential (v) Equilibrium constant (b) Differentiate between the following (i) Reversible and Irreversible Inhibition (ii) Coenzyme and holoenzyme (iii) Positive Cooperativity and negative cooperativity (iv) Inhibitors and Uncouplers (v) NAD and FAD (c) Write the contribution of the following scientists (i) E. Racker (iv) Frederick Kuhne (d) Give reasoning (6) (i) Km is a measure of enzyme affinity. (ii) Dinitrophenol acts as an uncoupler of oxidative phosphorylation. (iii) Vmax is unchanged by the presence of a competitive inhibitor. (e) Give an example of each (i) An enzyme regulated by reversible covalent modification (iii) first enzyme to be crystallized 2. (a) Explain the mechanism through which ATP transfers its energy. 3. 4. 5. 6. (8) (b) Discuss hydrophilic and hydrophobic electron carriers. (7) (a) Describe the pathway of transfer of electrons from Complex I to Complex IV in the ETC of mitochondria. (8) (b) Draw a neat, well-labelled diagram of ATP synthase. Add a note on rotational catalysis exhibited by this enzyme. (7) (a) Derive the Michaelis-Menten equation and show under what conditions (b) Discuss the factors that influence the activity of enzymes. (7) (a) Describe any three different types of enzyme regulation, giving one example of each. (9) (b) Explain the mechanism of positive and negative cooperativity. (6) Write a short note on the following (any three). (3×5=15) (i) Shuttle system (ii) Multi-enzyme complexes (iii) Classification of enzymes (iv) Competitive inhibition