1. Cell Physiology: Metabolism Biology 211 Anatomy & Physiology 1 Dr. Tony Serino

2. Metabolism Refers to all of the reactions that occur in the cell Refers to all of the reactions that occur in the cell Each reactions requires a specific enzyme Each reactions requires a specific enzyme Energy may be released or consumed in the reactions Energy may be released or consumed in the reactions

3. Energy Flow in Reactions

4. Metabolic Reactions (R  P) Most reactions are reversible Most reactions are reversible All reactions try to proceed to a dynamic equilibrium. Therefore, one way to favor a reaction is to manipulate the amount of reactants or products present. All reactions try to proceed to a dynamic equilibrium. Therefore, one way to favor a reaction is to manipulate the amount of reactants or products present. A + B  C + D

5. Metabolic Pathways A series of reactions in the body. A series of reactions in the body. Most are linked with other sets, so that the products of one reaction become the reactants of the next. Most are linked with other sets, so that the products of one reaction become the reactants of the next. Two Kinds: Two Kinds: Degradative (Catabolism) Degradative (Catabolism) Biosynthetic (Anabolism) Biosynthetic (Anabolism)

6. Pathway Map of Cell Metabolism Note: Kreb Cycle

7. Enzymes Catalyze reactions Reactants = substrates (S) S bind to active site on E S bound non-covalently 3D structure give E specificity # of bonds formed gives affinity May use co-factors (co-enzymes) May bind other chemicals that act as modulators (change 3D shape of active site) Active Site Substrate The enzyme’s 3D shape allows it to bind to a specific substrate.

9. Energy flow in a reaction Every reactions must overcome an energy barrier to begin. Energy of Activation (E A )

10. Energy Flow with Enzyme Present Enzymes increase reaction rates by lowering the E A Enzymes increase reaction rates by lowering the E A

11. Enzymes Lower E A Bring reactants into close proximity Bring reactants into close proximity Produce bond strain in substrates Produce bond strain in substrates Both of these characteristics allows the enzyme to lower the reaction’s E A

12. Control of Enzyme Function  Proteins remain functional in a narrow range of pH and temp.  Radical changes in these values can cause proteins to denature; that is, change its 3D shape

13. Enzyme Control Enzyme activity can be modified by changes in both enzyme and substrate concentrations Enzyme activity can be modified by changes in both enzyme and substrate concentrations Excess substrate eventually hits a maximum or saturation point Excess substrate eventually hits a maximum or saturation point

14. Enzyme Control Other substances may bind to the enzyme and modify its behavior; either as an activator or inhibitor Other substances may bind to the enzyme and modify its behavior; either as an activator or inhibitor If the substance competes with the substrate for the active site; it is a competitive inhibitor If the substance competes with the substrate for the active site; it is a competitive inhibitor If it binds elsewhere and changes the enzymes shape at its active site then it is a noncompetitive inhibitor/activator If it binds elsewhere and changes the enzymes shape at its active site then it is a noncompetitive inhibitor/activator

15. Enzyme Modulation: non-competitive inhibition and activation Binding of a molecule to a site other than the active site may result in an enzyme conformational change that either turns the enzyme “on or off” Binding of a molecule to a site other than the active site may result in an enzyme conformational change that either turns the enzyme “on or off” If the modulator is bound by non-covalent forces; it is allosteric modulation (the most common type); if bound covalently, it is covalent modulation (which is more difficult to change) If the modulator is bound by non-covalent forces; it is allosteric modulation (the most common type); if bound covalently, it is covalent modulation (which is more difficult to change)

16. ATP cycle

17. Utilization of ATP

18. ATP Synthesis Two ways to produce ATP Two ways to produce ATP Substrate Phosphorylation Substrate Phosphorylation Oxidative Phosphorylation Oxidative Phosphorylation

19. Substrate Phosphorylation An ATPase binds a substrate that can be stripped of a high energy phosphate to synthesize ATP An ATPase binds a substrate that can be stripped of a high energy phosphate to synthesize ATP

20. Oxidative Phosphorylation High energy electrons are scavenged from the breakdown of food molecules and used to power an electron transport chain which allows the cell to synthesize ATP High energy electrons are scavenged from the breakdown of food molecules and used to power an electron transport chain which allows the cell to synthesize ATP Uses a series of Redox reactions to power pumps Uses a series of Redox reactions to power pumps Note: the PO 4 - is an ion of the environment and contains no extra energy Note: the PO 4 - is an ion of the environment and contains no extra energy

21. Co-enzymes: NADH & FADH 2 The co-enzymes pick up high energy electrons and transport them to where they are needed, such as, the electron transport chain. Oxidized Reduced NAD+  NADH FAD+  FADH 2

23. Glycolysis

24. Kreb Cycle

25. Electron Transport Chain

26. Glycolysis: Overview 2 PGAL

31. Transition Reaction: Acetyl-CoA For one molecule of glu, 2 pyruvates will be processed.

32. Kreb Cycle

33. For one molecule of glucose, 2 acetyl-CoAs will be processed, so the Kreb cycle will make 2 complete turns For one molecule of glucose, 2 acetyl-CoAs will be processed, so the Kreb cycle will make 2 complete turns All of the carbon atoms of the sugar have now been converted to CO 2 All of the carbon atoms of the sugar have now been converted to CO 2 After the co-enzymes are processed, the total amount of ATP produced per turn of the wheel will be 12 ATP After the co-enzymes are processed, the total amount of ATP produced per turn of the wheel will be 12 ATP Transition reaction

34. Electron Transport Chain (Respiratory Chain) NADH unloads its electrons at the start of the chain; yielding the maximum energy release per electron pair NADH unloads its electrons at the start of the chain; yielding the maximum energy release per electron pair FADH 2 unloads further down the line, thereby diminishing its energy return FADH 2 unloads further down the line, thereby diminishing its energy return Oxygen is the final electron acceptor, it combines with hydrogen to form water Oxygen is the final electron acceptor, it combines with hydrogen to form water

35. Chemiosmosis Generates a high H+ concentration in the intermembrane space

36. ATP synthase complex H+ are pushed through the channel due to their electro- chemical gradient H+ are pushed through the channel due to their electro- chemical gradient This spins the rotor molecules which produces the energy needed to convert ADP to ATP This spins the rotor molecules which produces the energy needed to convert ADP to ATP

37. Cellular Respiration Overview

38. Aerobic vs. Anaerobic Respiration

39. Anaerobic Respiration (fermentation)

40. Food Processing

41. Protein Metabolism Proteins  Amino Acids Proteins  Amino Acids Amino Acids Amino Acids Deamination –removes NH forming a keto-acid Deamination –removes NH forming a keto-acid Transamination –transfers NH to other keto-acid Transamination –transfers NH to other keto-acid Keto-acids can be fed into Kreb Cycle Keto-acids can be fed into Kreb Cycle Amino group may form ammonia which can be converted to urea and excreted by kidney Amino group may form ammonia which can be converted to urea and excreted by kidney

45. Fat Metabolism Triglyceride  3 fatty acids + glycerol ( a sugar)

46. Fat Metabolism  Fatty acids broken down 2 C’s at one time = Beta-oxidation of fat 8 C fatty acid would yield 62 ATP molecules (17x-6) = # of ATP produced x = # of C pairs in the FA