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Exploring Biological Energy Processes: Thermodynamics, Enzymes, Cellular Respiration, and Photosynthesis - Document preview page 1

Exploring Biological Energy Processes: Thermodynamics, Enzymes, Cellular Respiration, and Photosynthesis - Page 1

Document preview content for Exploring Biological Energy Processes: Thermodynamics, Enzymes, Cellular Respiration, and Photosynthesis

Exploring Biological Energy Processes: Thermodynamics, Enzymes, Cellular Respiration, and Photosynthesis

A review sheet on biological energy processes, including thermodynamics, enzymes, cellular respiration, and photosynthesis.

Christopher Lee
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Exploring Biological Energy Processes: Thermodynamics, Enzymes, Cellular Respiration, and Photosynthesis - Page 1 preview imageExploring Biological Energy Processes: Thermodynamics, Enzymes,Cellular Respiration, and PhotosynthesisChapter 8Thermodynamics, enzymes, and ATP1. Definitions of First and Second Laws of Thermodynamics:First Law of Thermodynamics: Energycannot be created or destroyed, onlytransformed from one form to another. Total energy in the universe remainsconstant.Second Law of Thermodynamics: The entropy (disorder) of an isolatedsystem tends to increase over time. In simpler terms, systems naturallyprogress toward disorder or randomness.2. Why Cells and Organisms are Considered Open Systems:Cells and organisms are open systems because they exchangeenergyandmatterwith their surroundings. They take in nutrients and expel waste, andrequire energy from the environment (like sunlight or food) to maintain theirstructure and function.3. Definition of Energy and Its Units:Energy: The capacity to do work or produce change. It exists in variousforms such as chemical, kinetic, and potential energy.Units of Energy: In biological systems, energy is often measured inkilocalories (kcal)orkilojoules (kJ). TheJoule (J)is the standard SI unit.4. Definitions of Entropy (S), Free Energy (G), and Free Energy Change (ΔG):Entropy (S): A measure of disorder or randomness in a system.Free Energy (G): The energy available to do work in a system at constanttemperature and pressure.
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Exploring Biological Energy Processes: Thermodynamics, Enzymes, Cellular Respiration, and Photosynthesis - Page 2 preview image
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Exploring Biological Energy Processes: Thermodynamics, Enzymes, Cellular Respiration, and Photosynthesis - Page 3 preview imageFree Energy Change (ΔG): The change in free energy during a process. Anegative ΔG indicates a spontaneous reaction, while a positive ΔG indicates anon-spontaneous reaction.5. Relationships Between ΔH, ΔG, and ΔS:ΔH (Change in Enthalpy): The heat content or total energy of a system.ΔG = ΔH-TΔS: This equation links the change in enthalpy, entropy, andtemperature to determine the spontaneity of a reaction.oΔG < 0: Exergonic reaction (spontaneous).oΔG > 0: Endergonic reaction (non-spontaneous).6. Endergonic vs. Exergonic Reactions and Spontaneous Reactions:Endergonic Reactions:Reactions that require energy input (ΔG > 0), non-spontaneous.Exergonic Reactions: Reactions that release energy (ΔG < 0), spontaneous.Spontaneous Reactions: Reactions that occur naturally without externalenergy input, typically with a negative ΔG.7. Equilibrium Constant (Keq) and Reaction at Equilibrium:Keq: The ratio of the concentrations of products to reactants at equilibrium.A reaction isat equilibriumwhen the rates of the forward and reversereactions are equal, and the concentrations of reactants and products remainconstant.8. Equation Relating ΔG, Keq, and Substrate/Product Concentrations:ΔG = ΔG° + RT ln([products]/[reactants])
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Exploring Biological Energy Processes: Thermodynamics, Enzymes, Cellular Respiration, and Photosynthesis - Page 4 preview imageoΔG° is the standard free energy change, R is the gas constant, T istemperature, and the brackets represent concentrations of productsand reactants.9. Why ATP is Considered a Universal Energy Carrier:ATP is considered a universal energy carrier because it stores energy in itsphosphate bonds. When ATP is hydrolyzed to ADP and inorganic phosphate(Pi), energy is released, which can then be used to drive biochemicalprocesses like muscle contraction, protein synthesis, and active transport.10. Why Actual ΔG for ATP Hydrolysis is-10 to-12 kcal/mol (Not-7.3kcal/mol):The actual ΔG for ATP hydrolysis is more negative than the standard value (-7.3 kcal/mol) due to the actual intracellular concentrations of ATP, ADP, andPi, which makes the hydrolysis reaction more exergonic in living cells.11. ATP Used to Drive Endergonic Reactions (Example):Example:Protein Synthesis-The formation of peptide bonds during proteinsynthesis is an endergonic process (requires energy). ATP hydrolysisprovides the necessary energy to drive this reaction, ensuring the synthesisof proteins.12. Why Cells Maintain Product-to-Substrate Ratio Much Less Than Keq:Cells maintain a product-to-substrate concentration ratio much lower thanKeq to ensure that reactions proceed in the direction that supports cellfunctions (homeostasis). This helps cells to regulate metabolic pathwaysefficiently.13. Energy of Activation, Active Center of an Enzyme:
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Exploring Biological Energy Processes: Thermodynamics, Enzymes, Cellular Respiration, and Photosynthesis - Page 5 preview imageEnergy of Activation: The energy required to start a reaction. Enzymeslower this energy barrier, making reactions occur faster.Active Site: The part of an enzyme where the substrate binds. The specificamino acids in the active site participate in catalysis by stabilizing thetransition state.14. pH, Temperature Optima, Enzyme Specificity, and Induced Fit:pH and Temperature Optima: Enzymes function best at specific pH andtemperature conditions.Enzyme Specificity: Enzymes are highly specific for their substrates.Induced Fit: When an enzyme binds to its substrate, it undergoes aconformational change that helps catalyze the reaction.15. Effect of Substrate on Enzyme Activity, Km, and Vmax:Km: The substrate concentration at which the enzyme operates at half itsmaximum rate (Vmax).Vmax: The maximum rate of an enzyme-catalyzed reaction when the enzymeis saturated with substrate.16.Competitive and Noncompetitive Inhibition:Competitive Inhibition: Inhibitor competes with the substrate for the activesite. Itincreases Kmbutdoes not affect Vmax.Noncompetitive Inhibition: Inhibitor binds to a different site (allostericsite), changing the enzyme's shape. Itdecreases Vmaxbutdoes not affectKm.17. Feedback Inhibition and Allosteric Regulation:
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