Chapter Eight An Introduction to Metabolism You Must Know: Key role of ATP in energy coupling Enzymes work by lowering

ng the energy of activation Catalytic cycle of a enzyme that results in the production of a final product Factors that influence efficiency of enzymes An Organisms Metabolism Transforms Matter & Energy, Subject to the Laws of Thermodynamics Metabolism: The totality of an organisms chemical reactions. Bioenergetics: The study of how energy flows thru the organism. Metabolic Pathways: A series of chemical reactions that either builds a complex molecule (Anabolic) or breaks a complex molecule into simpler compounds (Catabolic). Catabolic Pathways: Breakdown Pathways Ex) Digestive enzymes break down food & release energy during respiration. Anabolic Pathways: Biosynthetic pathways consume energy to build complicated molecules. Ex) Amino Acids linked together to form muscle tissue. Forms of Energy -Energy is the capacity to do work or cause change. Life depends on the ability of cells to transform energy from one form to another. 1) Kinetic Energy: Energy associated with the relative motion of objects Heat/Thermal Energy: The kinetic energy associated with the random movement of atoms or molecules. 2) Potential Energy: An object at rest may possess stored energy as a result of its position or structure. 3) Chemical Energy: A form of potential energy is stored in molecules. The amount of chemical energy a molecule possesses depends on its chemical bonds. Ex) Catabolic pathways that occur during respiration to break down glucose. Laws of Energy Transformation -Organisms are energy transformers. -Organisms are open systems; they absorb & release energy with their surroundings.

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Thermodynamics: The study of energy transformations that occur in matter. First Law of Thermodynamics (Principle of Conservation of Energy) Energy of the universe is constant Energy can be transferred & transformed, but it cant be created or destroyed. Second Law of Thermodynamics Energy transfer or transformation increases the entropy of the universe. Entropy: A measure of disorder or randomness. The more randomly arranged a collection of matter is, the greater its entropy. Spontaneous: Used for a process that can occur without an input of energy. As organisms increase their order, the decrease the order of their surroundings. Free Energy: A part of a systems energy that is able to perform work when temperature & pressure of the system is uniform. G=H-TS G= Gibbs Free Energy H= Change in total energy (Enthalpy) S= Change in systems entropy T= Absolute temperature in Kelvin When we know G, we can predict whether the process will be spontaneous or not. *Processes with a negative G are usually spontaneous. Unstable systems (G) tend to change to become more stable (G) MAXIMUM STABILITY=EQUILIBRIUM Free Energy & Metabolism Exergonic Reaction (Energy Outwards): One in which energy is released. These reactions occur spontaneously & release free energy into the system. Ex) Cellular Respiration Endergonic Reaction (Energy Inward): Reaction that requires energy to proceed. These reactions absorb free energy from the system. Ex) Photosynthesis ATP -The hydrolysis of ATP releases free energy. -The phosphate group is transferred to a reactant & is phosphorylated. Cells do 3 main kinds of work that is driven by Chemical Potential Energy. 1) Chemical Work: Endergonic reactions like the synthesis of polymers from monomers. 2) Transport Work: Pumping materials across membranes. 3) Mechanical Work: Beating cilia, contraction of muscle cells, chromosome movement during cell reproduction.

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Energy Coupling Helps cells manage their energy resources. The use of an exergonic process to drive an endergonic one. ATP is responsible for energy required in energy coupling. ATP is made of: 1. Nitrogenous Base Adenine 2. Ribose 3. Chain of 3 Phosphate Groups

Work in a cell is done by the release of a phosphate group from ATP. The exergonic release of the phosphate group is used to do the endergonic work of the cell. When ATP transfers 1 phosphate (Hydrolysis), it becomes ADP. Reactant changes shape

Enzymes -Biological catalysts -Macromolecules -Change the rate of a reaction without being altered in the process -Most enzymes are considered proteins (RNA enzymes=Ribozymes) How do enzymes speed up reactions? Enzymes catalyze reactions by lowering the activation energy (EA), enabling the reactant molecules to absorb enough energy to reach the transition state even at moderate temperatures. What is Activation Energy? (AKA Free Energy of Activation) The energy required to start a reaction (break bonds) Often in the form of heat that reactants absorb from surroundings

Chapter Eight Sometimes the activation energy is so high that the reaction wont take place at allEnzymes lower the EA

Enzyme-Substrate Complex Substrate- Reactant that an enzyme work on Enzyme + Substrate(s) Enzyme-Substrate Complex (Induced Fit) Enzyme + Product(s) Reactions are catalyzed by specific enzymes The specificity of an enzyme results from its shape

Active Site: Region of the enzyme that actually binds to the substrate. When the substrate enters the active site & causes a change in the shape of the enzymes. Induced Fit: Brings chemical groups of the active site into positions that enhance their ability to catalyze the chemical reaction. What can affect the activity of an Enzyme? -pH & Temperature can change the shape & function of enzymes. (Draw a graph showing how pH and Temperature affect enzymes)

Many enzymes need non-protein helpers called cofactors to function properly. Ex) Metal ions like Zinc, Iron, Copper

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Coenzymes: Organic cofactors Ex) Vitamins Enzyme Inhibitors 1. Competitive Inhibitors: Reverse Inhibitors. Some resemble the substrate & block the active site of the enzyme. They compete with the substrate for the enzymes active site. *This can be overcome by increasing the amount of substrate. 2. Noncompetitive Inhibitors: Do not compete for the active site, instead they bind to a different part of the enzyme & change its shape Ex) Hydroxylamine from lab, Toxins, poisons, pesticides, antibiotics, naturally occurring molecules to regulate enzyme activity 3. Selective Inhibition: How cells regulate their metabolic pathways. Essential to the control of cellular metabolism. These molecules behave as reversible noncompetitive inhibitors. They change the enzymes shape & the functioning of its active site by binding somewhere else (non-covalent interactions). Allosteric Regulation: Any case in which a proteins function at one site is affected by the binding of a regulatory molecule at a separate site. This can inhibit or stimulate the enzymes activity. (Work in both Catabolic & Anabolic reactions) Ex) ATP can act as an allosteric regulator Products of ATP hydrolysis (ADP+P) ATP binds to several catabolic enzymes allosterically inhibiting their activity (Allosteric Inhibitor) ADP functions as an activator of the same enzymes (Allosteric Activator) *When ATP production is less than ATP consumption, ADP activates the enzymes that speed up catabolism, making more ATP. *When ATP production is more than ATP consumption, ATP binds to the enzymes responsible for catabolism & inhibits there. Feedback Inhibition -A metabolic pathway is switched off by the inhibitory binding of its end product to an enzyme that acts early in the pathway. -Type of Allosteric Inhibition -Increases the efficiency of the pathway by it off when the end product accumulates in the cell. *Isoleucine allosterically inhibits the production of itself. Allosteric Enzymes -Oscillate between 2 different shapes, one catalytically active & the other inactive.