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Life 102, Ch.8 notes

by: Bridget Kelly

Life 102, Ch.8 notes Life 102

Bridget Kelly
GPA 4.0

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Attributes of Living Systems
Jennifer Neuwald and Tanya Dewey
Class Notes
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This 5 page Class Notes was uploaded by Bridget Kelly on Friday September 30, 2016. The Class Notes belongs to Life 102 at Colorado State University taught by Jennifer Neuwald and Tanya Dewey in Fall 2016. Since its upload, it has received 6 views. For similar materials see Attributes of Living Systems in Animal Science at Colorado State University.

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Date Created: 09/30/16
Saturday, September 24, 2016 Cellular Metabolism Chapter 8 Metabolism - All chemical reactions in a cell - metabolism = change = - chemical reactions are reversible Direction of chemical reactions - energy or no energy? - Catabolic reaction - energy is released - Anabolic reaction - energy is used - Energy - capacity to do work - Kinetic energy - energy associated with a moving object • includes molecules and atoms • heat is the energy associated with moving atoms/molecules • light is the energy associated with moving photons - Potential Energy - energy associated with the location or structure of an object - Chemical energy - energy stored in the bonds of molecules • chemical potential energy transferred when bonds break • Cellular Respiration is the process which converts the chemical energy found in glucose into the chemical energy found in ATP - byproducts of cellular respiration are heat, carbon dioxide, and water - Cellular respiration is a catabolic pathway 1st Law of Thermodynamics - entropy (disorder) of the universe is always increasing - large molecule (low entropy) heat, small molecule #1, small molecule #2 (high entropy) - if entropy increases: reaction is spontaneous 1 Saturday, September 24, 2016 - if entropy decreases: reaction is non-spontaneous Spontaneous reactions so not mean fast reactions “Gibbs Free Energy” or FreeEnergy - usable energy G = H — T S - Free energy; Usable energy in chemical bonds before V.S usable energy in bonds after - Total energy - Temperature - Entropy - Free energy is less than 0 = spontaneous • Exergonic - spontaneous reactions; releasing energy - Free energy is greater than 0 = non-spontaneous reactions • Endergonic - non-spontaneous reactions; using energy - Endergonic reactions are fueled by Exergonic reactions - Energy Coupling - the use of an exergonic process to drive an endergonic one. Types of cellular work - chemical work - chemicals moving around - Transport work - carrier protein - Mechanical work - walk on cytoskeleton fueled by ATP - adenosine triphosphate • ATP structure 2 Saturday, September 24, 2016 Hydrolysis of ATP - Hydrolysis is the reaction that breaks the bonds that join the phosphate groups in a ATP molecule - energy released - exergonic G = -7.3 Kcal/mol (ATP to ADP) How does ATP work? - Glutamic acid + Ammonia Glutamine G = +3.4 Kcal/mol • spontaneous The ATP Cycle - energy is recycled - 10,000,000 molecules/cell/sec 3 Saturday, September 24, 2016 Rates of reactions - same direction, different rates - Transition state - initial hurdle • Activism energy • energy in the form heat will help get over the transition state - Amount of activation energy will decide how fast or slow a reaction will happen Enzymes - proteins that speed up (catalyzes), but are not consumed by, reactions Substrate-reactants -binds to enzyme then you have induced fit Active site can… 1.act as Template 2.Stress substrate bonds 3.provide Microenvironment 4.Bond to substrate briefly Enzymes do NOT… - add energy to a reaction Change the G - get changed in the net reaction • not actually part of the reaction Substrate [C] - affects rate of enzymatic activity Enzyme [C] - affects rate of enzymatic activity 4 Saturday, September 24, 2016 Temperature - affects rate of enzymatic activity - optimal temperature for typical human enzyme (37 degrees) - differ in species PH - affects rate of enzymatic activity - optimal pH for stomach (about 2) - optimal pH for intestinal enzyme (about 8) Regulation of enzymatic activity by: - cofactors - additional substances required for catalysis - coenzyme - an organic cofactor - enzyme inhibitors - molecules that hinder activity • Competitive - makes active site have the wrong fit - competing with substrate for active site Non-competitive - does bind in active site • - reversible or non-reversible Regulated enzymes = regulated metabolism Allosteric regulation - enzymes structure (and function) is affected by binding of molecules 1. Activators (increase) 2. Inhibitors (decrease) 3. Cooperactivity (all available to be open and active) 5


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