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An Introduction to Metabolism
Ch. 8 AP Biology Ms. Haut
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Metabolic Pathways Catabolic Pathways
Release energy by breaking down complex molecules into simpler ones Cellular respiration provides energy for cellular work C6H12O6 + 6O2 6CO2 + 6H2O + energy Energy released drives anabolic reactions
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Metabolic Pathways Anabolic Pathways
Consume energy by building molecules Photosynthesis uses energy 6CO2 + 6H2O energy C6H12O6 + 6O2
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Organisms Transform Energy
Solar Energy (EK) Plants (glucose) Stored in chemical bonds (EP) Animals Break down Sugars; Some used (EK), some stored in chemical bonds (EP)
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Energy Kinetic energy is energy associated with motion
Heat (thermal energy) is kinetic energy associated with random movement of atoms or molecules Potential energy is energy that matter possesses because of its location or structure Chemical energy is potential energy available for release in a chemical reaction Energy can be converted from one form to another
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Laws of Thermodynamics
First Law—Energy can be transferred, but never created or destroyed Second Law—Every energy transfer results in increased entropy (randomness in the universe) Some of the energy is converted to heat Reactions occur spontaneously Chemical energy Heat CO2 First law of thermodynamics Second law of thermodynamics H2O
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Free Energy Organisms live at the expense of free energy (portion of a system’s energy available for work) acquired from the surroundings Free energy is needed for spontaneous changes to occur
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Gibbs-Helmholtz Equation
G = H - TS Can be used to determine if a reaction is spontaneous Spontaneous reactions occur in systems moving from instability to stability Free energy Total energy enthalpy Temp (K) entropy High energy Low energy
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Gibbs-Helmholtz Equation
G = H - T S Measure of heat in the reaction In chemical reactions, reactions absorb energy to break bonds Energy is then released when bonds form between rearranged atoms of the product
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Key Importance of G Indicates amount of energy available for work
Indicates whether a reaction will occur spontaneously (low G) G decreases as reaction approaches equilibrium G increases as reaction moves away equilibrium G = 0 when a reaction is in equilibrium
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Chemical Reactions Exergonic Endergonic Chemical products have lower G than reactants Products store more G than reactants Reaction releases energy Reaction requires energy input (absorbs) G = negative value G = positive value Spontaneous Non spontaneous In cellular metabolism, exergonic reactions drive endergonic reactions
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Rate of Reactions G indicates spontaneity not speed of reaction
Spontaneous reactions will occur if it releases free energy (- G ), but may occur too slowly to be effective in living cells Can leave sucrose in sterile water for yrs. with hydrolysis occuring; add sucrase and reaction will hydrolyze in seconds Biochemical reactions require enzymes to speed up and control reaction rates
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ATP couples exergonic reactions to endergonic reactions
A cell does three main kinds of work: Mechanical Transport Chemical To do work, cells manage energy resources by energy coupling, the use of an exergonic process to drive an endergonic one
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ATP Powers Cellular Work
Unstable Bonds—can release energy when broken Energy transferred to another molecule (phos-phorylated intermediate) with the phosphate Less stable More stable
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Reactants: Glutamic acid
LE 8-11 P i P Motor protein Protein moved Mechanical work: ATP phosphorylates motor proteins Membrane protein ADP ATP + P i P P i Solute Solute transported Transport work: ATP phosphorylates transport proteins P NH2 + NH3 Glu + P i Glu Reactants: Glutamic acid and ammonia Product (glutamine) made Chemical work: ATP phosphorylates key reactants
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The Regeneration of ATP
ATP is a renewable resource that is regenerated by addition of a phosphate group to ADP The energy to phosphorylate ADP comes from catabolic reactions in the cell The chemical potential energy temporarily stored in ATP drives most cellular work
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Enzymes Catalyst—chemical agent that speeds up a chemical reaction without being consumed by the reaction Hydrolysis of sucrose by the enzyme sucrase is an example of an enzyme-catalyzed reaction
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The Activation Energy Barrier
Every chemical reaction between molecules involves bond breaking and bond forming The initial energy needed to start a chemical reaction is called the free energy of activation, or activation energy (EA) Activation energy is often supplied in the form of heat from the surroundings
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Enzymes Catalytic proteins that speed up metabolic reactions by lowering energy barriers Reactants must absorb energy to reach transition state (unstable) Rxn occurs and energy is released as new bonds form to make products G for overall rxn is difference b/w G of products and G of reactants
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Substrate Specificity of Enzymes
Substrate—reactant that an enzyme acts Substrate binds to the active site on the enzyme Induced fit of a substrate brings chemical groups of the active site into positions that enhance their ability to catalyze the reaction
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Induced Fit Model of Enzymatic Reactions
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How do Enzymes Work? Active site holds 2 or more reactants in the proper position to react Induced fit may distort chemical bonds so less thermal energy is needed to break them Active site may provide micro-environment that aids a reaction (localized pH) Side chains of amino acids in active site may participate in reaction
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Enzyme Activity A cell’s physical and chemical environment affects enzyme activity Each enzyme has optimal environmental conditions that favor the most active enzyme conformation
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Effects of Temperature
Optimal temp. allows greatest number of molecular collisions without denaturing the enzyme Reaction rate when temperature Kinetic energy increases and collisions increases Beyond optimal temperature, reaction rate slows Too low, collisions b/w substrate and active site don’t occur fast enough Too high, agitation disrupts weak bonds of the tertiary structure of enzyme (enzyme unfolds)
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Effects of pH Optimal pH range for most enzymes is pH 6 – 8
Beyond optimal pH, reaction rate slows Too low (acidic) H+ ions interact with amino acid side-chains and disrupt weak bonds of the tertiary structure of enzyme Too high (basic) OH- ions interact with amino acid side-chains and disrupt weak bonds of the tertiary structure of enzyme
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Cofactors Small non-protein molecules that are required for proper enzyme catalysis Inorganic—Zn, Fe, Cu Coenzymes—vitamins
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Effects of Substrate Concentration
The higher the [substrate], the faster the rate (up to a limit) If [substrate] high enough, enzyme is saturated with substrate Reaction rate depends on how fast the active site can convert substrate to product When reaction is saturated with substrate, you can speed up reaction rate by adding more enzyme
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Effects of Enzyme Inhibitors
Competitive inhibitors—chemicals that resemble an enzyme’s normal substrate and compete with it for the active site Blocks active site from substrate If reversible, can be overcome by increasing substrate concentration
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Competitive Inhibitor
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Effects of Enzyme Inhibitors
Noncompetitive inhibitors—chemicals that bind to another part (allosteric site)of an enzyme Causes enzyme to change shape and prevents substrate from fitting in active site Essential mechanism in cell’s regulating metabolic reactions Allosteric site
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Negative Feedback
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Metabolic Control often Depends on Allosteric Regulation
Allosteric enzymes have 2 conformations, catalytically active and inactive Binding of an activator to the allosteric site stabilizes active conformation Binding of an inhibitor (noncompetitive) to the allosteric site stabilizes inactive conformation
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Control of Metabolism In feedback inhibition, the end product of a metabolic pathway shuts down the pathway Feedback inhibition prevents a cell from wasting chemical resources by synthesizing more product than is needed
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Specific Localization of Enzymes Within the Cell
Structures within the cell help bring order to metabolic pathways Some enzymes act as structural components of membranes Some enzymes reside in specific organelles, such as enzymes for cellular respiration being located in mitochondria
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