BIOL 111 1st Edition Exam 2 Study Guide Metabolism o Energy the capacity to do work or cause Change Types of energy Kinetic energy due to motion o Ex light heat sound Potential energy stored due to position or structure o Ex chemical atomic Measuring energy o Calorie cal amt heat required to raise 1 g of water 1 C Kcal 1000 cal Calorie in food Thermodynamics o Studying energy flow in natural systems 1st Law Energy and matter can be transferred but cannot be created or destroyed 2nd Law In every energy transfer some energy becomes unusable heat which increases entropy or disorder of the universe Spontaneous Reactions o Require no input of energy o Increases entropy Gibbs Free Energy o Measures the energy in a system ex living cell o Value of G will predict spontaneity of a reaction o G H T S G change in free energy E avail for work H change in enthalpy potential E T temperature measured in degrees Kelvin S change in entropy G spontaneous o Exergonic net release of free energy o Products are more stable but w less free energy G NOT spontaneous o Endergonic absorbs stores free energy o Products are less stable but w more free energy Metabolism o Chemical reactions in a cell required to maintain life o Types of metabolism Anabolic building molecules requires energy Catabolic breaking down molecules produces energy Enzymes catalytic proteins not consumed in reaction o Active site Have precise physical shape for specific reactants substrates Site of catalysis provides microenvironment Changes shape to form induced fit Applies force to break bonds form new bonds Measuring enzyme activity o How did you measure the rate of reaction in lab o Spectrophotometer Measures either transmitted or absorbed light How molecules absorb light o Enzymes alter molecules thus alter light absorbing properties Rates of Reaction Vary o Enzyme concentration o Substrate concentration o Temperature o pH Rates of Reaction Vary o Cofactors nonprotein molecules aid enzyme catalysis Inorganic metal ions Organic coenzymes from vitamins o Inhibitors o Allosteric Regulation Inhibitors o Chemicals that inactivate enzyme activity o Competitive bind active site o Non competitive bind other site but alters active site Allosteric Regulation o Examples Hemoglobin 4 polypeptides each bind O2 or CO2 cooperative binding of O2 or CO2 o Reversible binding loses affinity o Binding of molecule to protein at one site that affects protein function at another site Examples ADP catabolic enzyme activator ATP catabolic enzyme inhibitor Review quiz o What do you need to remove pairs of e o What are the net products of glycolysis o Name 3 enzymes and 4 substrates you need to know from glycolysis Enzymes hydrogenase isomenase pysomerase Substrates glucose pyruvate G3P DHAP Review Preview o Energy Matter o Redox rxns o Laws of Thermodynamics o Kinetic vs Potential energy o Follow carbons o Follow electrons o Carbon cycle o Electron transport chain chemiosmosis o ATP synthase Review o 1 Which parts of the chloroplast are we concentrating on Why o 2 Which wavelengths are absorbed by the pigments in the chloroplast o 3 What is the primary purpose of the light reactions o 4 What is the source of the electrons for the light reactions o 5 Describe electron flow during the light reactions o 6 Where is the high H concentration in a chloroplast o 7 What is the purpose of cyclic electron flow
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