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Energy and Metabolism Chapter 8
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Energy
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Metabolism All the chemical reactions carried out by the cell
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Metabolism Catabolic reactions: Break down large molecules into smaller substances Exergonic: Releases energy
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Metabolism Anabolic reactions: Synthesis of large molecules from smaller substances Endergonic: Requires energy
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Metabolism Biochemical pathways: Reactions in a cell Occur in sequence Product of one reaction Becomes substrate in the next Pathways are highly regulated & coordinated Feedback inhibition: End product of a reaction blocks the pathway from producing more.
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Energy
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Bioenergetics: Analysis of how energy powers activities of living systems Growth, order, reproduction, responsiveness & regulation
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Energy Energy: The capacity to do work Kinetic energy: Energy of motion Potential energy: Energy of position or stored energy
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Energy Kinetic energy: Potential energy:
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Energy Thermodynamics: Study of energy “heat changes” Most work done by living organisms Transformation of PE to KE
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Energy Sun main source of energy Combines smaller molecules Make larger molecules Energy is stored in the chemical bond
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Energy Redox(oxidation-reduction) reactions: Transfer of an electron or electrons Important in the flow of energy in biological systems An electron is passed from one atom to another energy is passed
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Law of thermodynamics Laws of thermodynamics govern all energy changes in the universe. First law of thermodynamics: Energy cannot be created or destroyed Change from one form to another. (potential to kinetic) Total amount of energy stays the same
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First law In living organisms: Eating transfers energy from the bonds in food to organism PE is transferred to KE
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First Law Heat: Random motion of molecules Heat can be lost in the system during conversions Sun replaces energy lost as heat
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Second law Second law of thermodynamics: Transformation of PE to heat (random motion of molecules). Entropy (disorder) in the universe is increasing
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Second law Energy transformations tend to proceed spontaneously Convert matter from a more ordered state to a less ordered More stable state.
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Second law Entropy(s): Disorder in a system Enthalpy (H): Heat content Free energy(G): Amount of energy available to do work in any system. Amount of energy available to break and then make other chemical bonds
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Second law G=Gibbs free energy G = H - T S (T=Kelvin temp) G is positive Products have more energy than reactants More energy in the bonds or less randomness Endergonic reaction
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Second law G is negative Products have less energy than reactants H is lower (bond energy) or S is greater- more randomness Exergonic: Reaction that releases energy
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Exergonic reaction
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Exergonic reactions
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Activation Energy Energy needed to initiate a reaction All reactions require activation energy. Reactions with higher AE tend to move forward more slowly
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Enzymes Catalyst in living organisms Large three-dimensional globular protein Ribozymes: RNA catalysts are specific & speed up reactions
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Enzymes Substrate: Molecule that is going to undergo the reaction Active sites: Specific spots on the enzyme that substrates binds Enzyme-substrate complex: Enzymes bind to substrates with a precise fit. Induced fit: Substrate causes the enzyme to adjust to make a better fit E+S ES E + P
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Fig. 8-17 Substrates Enzyme Products are released. Products Substrates are converted to products. Active site can lower E A and speed up a reaction. Substrates held in active site by weak interactions, such as hydrogen bonds and ionic bonds. Substrates enter active site; enzyme changes shape such that its active site enfolds the substrates (induced fit). Active site is available for two new substrate molecules. Enzyme-substrate complex 5 3 2 1 6 4
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Enzymes Only small amounts are necessary Can be recycled Specific Speeds up the reactions Different types of cells have different enzymes Determines course of chemical reactions in the cell
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Enzyme examples Lipase, protease Carbonic anhydrase –CO 2 + H 2 O H 2 CO 3 Lactate dehydrogenase –Lactate to pyruvate Pyruvate dehydrogenase –Enzyme that starts the Kreb cycle
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Enzymes Factors that affect the rate of enzyme 1. Concentration of enzyme & substrate 2. Factors that affect 3-D shape of the enzyme Temperature, pH, salt concentration and regulatory molecules
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Enzymes Inhibitor: Binds the enzyme Prevents it from working Occurs at end of a pathway to stop reactions Two types of inhibitors Competitive Noncompetitive
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Fig. 8-19 (a) Normal binding (c) Noncompetitive inhibition (b) Competitive inhibition Noncompetitive inhibitor Active site Competitive inhibitor Substrate Enzyme
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Enzymes Allosteric site: On/off switch for the enzyme Usually at different location than the active site Allosteric inhibitor: Binds at the allosteric site Stops the enzyme activity Activators: Binds & increases the activity
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Enzymes Cofactor: Assists enzyme function such as Zn, Mg, Cu Coenzymes: Organic molecules that are not proteins Help transfer electrons & energy associated with the electrons Vitamins are coenzymes NAD + important coenzyme
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Energy
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ATP ATP powers the energy requiring processes in the cell 1. Chemical work (making polymers) 2. Transporting substances 3. Mechanical work Muscle movement, cilia
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ATP Structure of ATP Ribose sugar Adenine 3 phosphate attached in a row
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ATP
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ADP Losses a inorganic phosphate Hydrolysis 7.3kcal/mole of energy is released.
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