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Dive into the world of energy and metabolism, from catabolic to anabolic reactions, biochemical pathways, and the laws of thermodynamics. Understand enzymes, activation energy, and factors that influence enzymatic reactions. Discover the key role of redox reactions and the regulation of energy flow in biological systems.
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Metabolism • All the chemical reactions carried out by the cell
Metabolism • Catabolic reactions: • Break down large molecules into smaller substances • Exergonic: • Releases energy
Metabolism • Anabolic reactions: • Synthesis of large molecules from smaller substances • Endergonic: • Requires energy
Metabolism • Biochemical pathways: • Reactions in a cell • Occur in sequence • Product of one reaction • Becomes substrate in the next • Pathways are highly regulated and coordinated • Feedback inhibition: • End product of a reaction blocks the pathway from producing more.
Energy • Bioenergetics: • Analysis of how energy powers activities of living systems • Growth, order, reproduction, responsiveness & regulation
Energy • Energy: • The capacity to do work • Kinetic energy: • Energy of motion • Potential energy: • Energy of position or stored energy
Energy • Kinetic energy: • Potential energy:
Energy • Thermodynamics: • Study of energy “heat changes” • Most work done by living organisms • Transformation of PE to KE
Energy • Sun main source of energy • Energy from sun • Combine smaller molecules to make larger molecules • Energy is stored in the chemical bond
Energy • Redox(oxidation-reduction) reactions: • Transfer of an electron or electrons • Play a key role in the flow of energy in biological systems • An electron is passed from one atom to another energy is passed
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
First law • In living organisms: • Eating transfers energy from the bonds in food to organism • PE is transferred to KE
First Law • Heat: • Random motion of molecules • Heat can be lost in the system during conversions • Sun replaces energy lost as heat
Second law • Second law of thermodynamics: • Transformation of PE to heat (random motion of molecules). • Entropy (disorder) in the universe is increasing
Second law • Energy transformations tend to proceed spontaneously • Convert matter from a more ordered state to a less ordered or more stable state.
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
Second law • G=Gibbs free energy • G = H - TS (T=Kelvin temp) • G is positive • Products have more energy than reactants • Due to more energy in the bonds or less randomness • Endergonic reaction
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
Activation Energy • Energy needed to initiate a reaction • All reactions require activation energy. • Reactions with higher AE tend to move forward more slowly
Enzymes • Catalyst in living organisms • Large three-dimensional globular protein • Ribozymes: • RNA catalysts are specific & speed up reactions
Enzymes • Substrate: • Molecule that is going to undergo the reaction • Active sites: • Specific spots on the enzyme that substrates binds • Enzyme-substrate complex: • Enzymes are bound to substrates with a precise fit. • Induced fit: • When the substrate causes the enzyme to adjust to make a better fit • E+S ES E + P
Substrates enter active site; enzyme changes shape such that its active site enfolds the substrates (induced fit). 1 2 Substrates held in active site by weak interactions, such as hydrogen bonds and ionic bonds. Fig. 8-17 Substrates Enzyme-substrate complex Active site can lower EA and speed up a reaction. 3 6 Active site is available for two new substrate molecules. Enzyme 5 Products are released. 4 Substrates are converted to products. Products
Enzymes • Only small amounts are necessary • Can be recycled • Specific • Speeds up the reactions • Different types of cells have different enzymes • Determine the course of chemical reactions in the cell
Enzyme examples • Lipase, protease • Carbonic anhydrase • CO2 + H2O H2CO3 • Lactate dehydrogenase • Lactate to pyruvate • Pyruvate dehydrogenase • Enzyme that starts the Kreb cycle
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
Enzymes • Inhibitor: • Binds the enzyme • Prevents it from working • Occurs at the end of a pathway to stop the reactions • Two types of inhibitors • Competitive • Noncompetitive
Fig. 8-19 Substrate Active site Competitive inhibitor Enzyme Noncompetitive inhibitor (c) Noncompetitive inhibition (b) Competitive inhibition (a) Normal binding
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
Enzymes • Cofactor: • Assists enzyme function such as Zn, Mg, Cu • Coenzymes: • Cofactors that are not proteins but are organic molecules • Help transfer electrons & energy associated with the electrons • Vitamins are coenzymes • NAD+ important coenzyme
ATP • ATP powers the energy requiring processes in the cell • 1. Chemical work (making polymers) • 2. Transporting substances • 3. Mechanical work • Muscle movement, cilia
ATP • Structure of ATP • Ribose sugar • Adenine • 3 phosphate attached in a row
ATP • ATP • ADP • Losses a inorganic phosphate • Hydrolysis • 7.3kcal/mole of energy is released.