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Chapter 8 Introduction to Metabolism
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Think Tank Question… Using the concepts of energy, entropy, and metabolism answer the following: Does the concept of evolution violate the 2nd law of thermodynamics? Explain. It would appear the answer is yes since organisms get more complex…but…SEE ANSWERS ON SLIDE
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Metabolism Metabolism is the sum of all of the chemical reactions in a biological organism A metabolic pathway is a series of defined steps resulting in a certain product, each step catalyzed by an enzyme Catabolic pathway – release energy by breaking down complex molecules into simpler compounds; energetically “downhill”; example – cellular respiration Anabolic pathway – consume energy to build complicated molecules from simple ones; energetically “uphill”; example - photosynthesis The energy released from a catabolic pathway is stored and used to complete an anabolic pathway
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Energy Energy – the capacity to cause change or do work
Kinetic energy – energy of motion Potential energy – stored energy, the energy in an object currently not moving
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Thermodynamics Thermodynamics – the study of energy transformations that occur in a collection of matter 1st law – energy can be transferred and transformed, but cannot be created or destroyed 2nd law – every energy transfer or transformation increases the entropy of the universe Entropy is a measure of randomness or disorder in the universe Disorder = randomness caused by the thermal motion of particles; the energy is so dispersed it is unusable.
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Back to the tank… Does evolution violate the 2nd law??? NOPE.
The construction of complex molecules (metabolism) generates disorder. Life requires as constant input of energy to maintain order.
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The Laws of Thermodynamics
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Free Energy Free energy – the energy available to do work
ΔG = ΔH - T ΔS ; the Gibbs-Helmholtz equation ΔG = the change in free energy, the maximum amount of usable energy that can be harvested ΔH = enthalpy or total energy in biological systems T = temperature in Kelvin ΔS = change in entropy Significance Indicates the maximum energy available to do work Indicates whether a reaction will occur spontaneously or not At equilibrium ΔG = 0
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Reaction types Exergonic Endergonic
Chemical products have less free energy than the reactants Energetically downhill Spontaneous Loses free energy ΔG is negative - ΔG is the max amount of work the reaction can perform Endergonic Products have more free energy than reactants Energetically uphill Non-spontaneous Requires energy ΔG is positive + ΔG is the minimum amount of work required to drive the reaction
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Applying Concepts… REACTION REACTANTS PRODUCTS ΔG Hydrolysis of sucrose Sucrose + H2O Glucose + Fructose 7.0 Triglyceride attachment Glycerol + fatty acid Monoglyceride 3.5 Photosynthesis 6CO2 + 6H2O Glucose + 6O2 686 The table shows some reactions and the absolute values of their associated free energy changes (ΔG). For each reaction, would you expect ΔG to be positive or negative? Which reactions will be spontaneous? Explain your answers. Hydrolysis of sucrose = negative free energy and therefore spontaneous (Hint: from complicated to less complicated molecules – catabolic reaction); more disorder with the glucose and the fructose. The glycosidic bond between the two monosaccharides in sucrose creates more order. Triglyceride attachment = positive and therefore NOT spontaneous Photosynthesis = positive and therefore NOT spontaneous (requires energy)
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Cellular Work ATP powers cellular work by coupling exergonic and endergonic reactions Cell conducts 3 main types of work: mechanical, transport, and chemical ATP – Adenosine triphosphate
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ATP Hydrolysis Breaking of the bonds between phosphate groups
ATP + H2O ADP + Pi ΔG = -7.3 kcal/mol or kJ/mol (under standard conditions
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Energy Coupling Example
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How ATP Performs Work
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Regeneration of ATP Organisms at work are constantly using ATP, but ATP can be regenerated with the addition of a phosphate to ADP Requires energy; ΔG = +7.3 kcal/mol or kJ/mol
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Enzymes Enzyme – biological catalysts or catalytic protein (a chemical agent that speeds up a reaction without being consumed by the reaction) All reactions require an initial investment of energy for starting a reaction called the activation energy (EA) Enzymes reduce this activation energy
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How Enzymes Work
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Induced Fit Model Substrate – enzyme reactant
Active site – pocket or groove on enzyme that binds to substrate Enzyme substrate complex – enzyme flexes and molds to the shape of the substrate Analogy = baseball and a catchers mitt
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Induced Fit Model
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Enzyme Specificity Enzymes function in a very specific range of environmental conditions including temperature and pH Some enzymes require ions or other molecule partners: Cofactors – inorganic nonprotein helpers, ex: zinc, iron, copper Coenzymes – organic cofactors, ex: vitamins
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Enzyme Inhibitors Competitive inhibitors – block active site, direct competition with substrate Noncompetitive inhibitors – bind away from the active site, not in direct competition with substrate
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Allosteric Regulation
Allosteric regulation can be described as any case in which a protein’s function at one site is affected by the binding of a regulatory molecule to a separate site Activation, inhibition, and cooperativity
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Feedback Inhibition In feedback inhibition a metabolic pathway is switched off by the binding of its end product to an enzyme that acts early in the pathway
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Applying Concepts… The Scenario:
In the boy’s locker room a bacteria is found growing on some old socks made of a synthetic polymer. You make a protein extract from the bacteria and isolate the probable enzyme that can cleave the monomers from the polymer. You also synthesize a dipeptide glycine-glycine to test as a possible inhibitor of the enzyme.
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RATE OF POLYMER CLEAVAGE
Applying Concepts… EXPERIMENT CONDITION RATE OF POLYMER CLEAVAGE 1 No enzyme 0.505 2 Enzyme 825.0 3 Enzyme pre-boiled at 100 C 0.520 4 Enzyme + RNA 799.0 5 Enzyme + dipeptide 0.495 Explain the results of each experiment. How do you think the dipeptide works? How would you test your hypothesis?
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