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Chapter 8

by: Sophia Notetaker

Chapter 8 BIOC 0170

Sophia Notetaker
GPA 3.5
Foundation of Biology I
Barbara Barnhart

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Chapter 8
Foundation of Biology I
Barbara Barnhart
Class Notes
Chapter 8, Biology
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This 12 page Class Notes was uploaded by Sophia Notetaker on Monday February 8, 2016. The Class Notes belongs to BIOC 0170 at University of Pittsburgh taught by Barbara Barnhart in Spring 2016. Since its upload, it has received 19 views. For similar materials see Foundation of Biology I in Biology at University of Pittsburgh.


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Date Created: 02/08/16
Chapter 8 Metabolism Metabolism A sum of all chemical reactions inside the cells CATABOLISM ANABOLISM Break down to simplest molecules Build up of complex from simple Release Energy Required Energy l Energy Capacity to cause change capacity to do work 1 Kinetic a Energy associated with the relative movement of objects i Thermal energy Kinetic energy associated with the random movement of atoms or molecules 2 Potential a The energy that matter possesses as a result of its location or spatial arrangement structure i Chemical energy Potential energy available for release in chemical reactions Stored in molecular structure ll Thermodynamics The study of energy transformation differentiates between system What you are studying and surroundings 0 Rest of universe 0 Open system Energy and matter can be transferred between the system and the surroundings Closed system unable to exchange energy and matter with the surroundings lll Laws of Thermodynamics 1 First Law of Thermodynamics a Principles of conservation of energy b Energy can be transferred and transformed but it can not be created or destroyed 2 Second Law of Thermodynamics a Every energy transfers or transformation increases the entropy of the universe b entropy S measure of disorderrandomness c Sometimes see an increase in order which we see in decrease in entropy but it will be accompanied by a decrease in order elsewhere in the universe d Ex Knitting the blanket the energy to knit increase in disorder 3 Free Energy G a Amount of energy that can be put to work when temperature and pressure are uniform Ch 8 4 To Calculate Free Energy 1 enthalpy H total energy 2 entropy S disorder 3 temperature T quotabsolute temperaturequot Kelvin K oC273 AG AH TAS AG spontaneous change no energy input required AG nonspontaneous requires energy input from surroundings In a spontaneous change a The free energy of the system decreases AG lt 0 o The system becomes more stable The released free energy can be harnessed to do work a In Chemistry i AG H exergonic give energy away ii AG Endergonic absorbs energy b In Metabolism Ch 8 i Exergonic Reactions provide power for endergonic energy coup ng Reacztants d d iHI amount of einergillr released eeem Products Free energyr v Progress of the reaetfien I a Exergonic reaction energyr released Products Ame nt ef energy a required 33 AG 2 D i E Reactants i 9 u ll39 Pregress at the reactien b Endergenic reaction energy required Copyingth Pearson Education Inc publishing as Pearson Benjamin Cummings What about when AG 0 No net change Equilibrium Chen in equilibrium can not do any work Happens in closed system Open systems Delta G can never be equal to 0 Always affected by environment Ch 8 No equilibrium Metabolism is never at equilibrium Reason is that the products of a reaction does not accumulate by instead becomes a reactant in the next step What tvpes of work do cells do 1 Chemical work pushing endergonic reactions 2 Transport work Pumping substance across membranes against the direction of spontaneous movement 3 Mechanical Moving stuff around a Enerdv Couolino exergonic powers endergonic i Use of exergonic process to drive an endogenic process ii Exergonic powers endergonic b How does power get from one to the other i ATP The energy currency of the cell c Energy of ATP comes from breaking of phosphate group i Hydrolysis ii Look ath Figure 1 Adenine NH2 I ii i rl i i i Oquot 0 O Phosphate groups Phopholization when transferring Ch 8 ATPr gt ADP Pi E Pi inorganic phosphate Adenosine triphosphate ATP Inorganic phosphate Adenosine diphosphate ADP Copyiighl 2008 Pearson publishing as Pearson Benjamin Cu Figure 1 Energy of ATP comes from breaking of phosphate group Coupling Reactions Look at AG values of individual reactions EXO 1 ATPKLgt ADP P E AG 73 Kcalmol H2 Exergonic Endo 2 Glutamic Acid NH gt GlutNH2 AG 34 Kcallmol Total AG 39 Kcalmol Exogonic Ch 8 IgAGGM 34 kcallmol v AGGIU 3394 kc awmom L AGATF 97D3 kcallmol AGATP E Net AG 2 i3939 kcalmol c Freeenergy change for coupled reaction 24314 Pearson Education Inc Still how does the power get from exergonic to endergonic Transfer phosphate group onto some other molecule in the endergonic reaction Phosphorylation to attach the phosphate group broken off from ATP onto another molecule Energy from Energy for cellular catabolism exergonic i work endergonic energyereleasing ADP l i energyeconsuming processes processes shing as Pearson Benjamin Cummings Add h20 by hydrolysis What about speed AG does not tell us about speed AG 5Kcamo vs AG 500 Kcalmol Doesn39t mean the reaction goes faster Just means it more likely to occur Ch 8 Activation Energy EA Amount of energy that reactant must absorb before a reaction will start Need energy to make and break bonds in order to get from reactant to product Transition between reactant to products is unable 0 High free energy G Transition state Free energy it Products Progress of the reaction 1I gt13 ll 33535011 Edutatcn Inc EA Is the occurring transition state AG lt 0 is negative Products Is this spontaneous or nonspontaneous Spontaneous reaction always look at AG reaction exergonic Enzymes proteins that act as catalysts which speed up a chemical reaction without being consumed by it Comes out the same way it went in Can catalyze many reactions Enzyme lower activation energy BUT does not change AG Ch 8 Course of reaction E A without without enzyme enzyme EA ch enzyme T is lower E Beactants w 5 Course of AG is u affected E reaction by enzt e u with enzyme Prducts A Progress of the reaction Q 2011 Pearson Educaliom Inc Terms Substrate R Reactant that the enzyme binds with Active Site the site on the enzyme where the substrate binds 0 Active site has a very similar by not identical shape to the substrate When the substrate binds the enzyme has to change shape a little bit to get the perfect t Called Induced t Has a more complimentary shape for the transition state Substrate Active site 2 Enzymesubstrate corn ptex Enzyme 531 bl How do enzymes lower activation energy AKA Lowers Activation Energy Substrate bound through weak interactions When weak interaction form between enzyme and substrate have spontaneous reaction releasing energy This released energy helps lower activation energy 0 10th to the 8th A lot of speed Ch 8 Rate of reaction gt O 0 Substrates enter active 5mquot GSubstrates are held in active site by weak interactions Substrates Enzymesubstrate complex 0 Active site can lower EA and speed up a reaction Active site is available for two new substrate molecules Enzyme 6 Products are 9 Substrates are released converted to products K 43 Weakening interaction can be effected by the environment 201I Pearson Education Inc 1 Optimal Temperature a Temperature that allows the greatest number of molecular collision thus the fasted reaction rate without denaturing the enzyme b Optimal pH i pH that enzyme has highest level activity ii Temperature around 37C Stomach enzyme pH of 2 Optimal temperature for typical human enzyme 37 C Optimal temperature for enzyme of thermophilic heattolerant bacteria 77 C I l 20 4D I v I 60 80 Temperature C 1 00 1 20 a Optimal temperature for two enzymes Optimal pH for pepsin Optimal pH for trypsin T stomach intestinal I enzyme I enzyme 0 39 I E I I IE I I 2 I I a O l I In I El 39 39 E l vl I I I l I IV I 0 1 2 3 4 5 6 7 8 9 10 pH b Optimal pH tor two enzymes 9 Ch 8 2 Cofactor a Nonprotein ions or inorganic molecules needed for some enzyme functions b Ex Metal Ion 3 Coenzyme a An organic molecule that binds to an enzyme to help it do it job b Ex Vitamins 4 Note Both can bind permanently or loosely need to help catalyze reactions 5 Enzyme Inhibitors a Reduced enzyme function decreasesstops enzyme activity by binding to enzyme i Competitive 1 Structurally similar to the substrate 2 Can bind to active site therefore blocking the substrate 3 Ex Musical chair Substrate wont let another person get the chair ii NonCompetitive 1 Binds to another place on enzyme 2 Disrupts the enzymes shape and function 3 Ex Aspirin and Ibuprofen are enzyme inhibitors 3 Normal binding 3 Competitive inhibition c Noncompetitive inhibition astlbmrate V i Active l l 53919 I ompetitive inhibitor quot Enzyme Noncompetitive inhibitor 2211 Pearson Educaivm Inc 6 Regulation Deals with increasing and decreasing enzyme activity helps to control metabolism a Allosteric protein function at one site is affected by binding of regulatory protein at another site i More than one active site ii Inhibiting or enhancing activity iii Can be cooperative binding 10 Ch 8 b Cooperativity i A substance molecule binds to one active site in a multiunit enzyme and trigger a shape change in all subunits and increases catalytic activity of the other active sites ii Ampli es the response of the enzymes to substrates 3 Allosteric activators and inhibitors b Cooperativity another type of allosteric activation Allosteric enzyme Active site fOU subunits one four Substrate Regulatory w one AGtIV tOT of four Active term Stabilized inactive form Stabilized n active form active form Oscillation Non func onal quot active site inhibitor Inactive form Stabmzed inactive form 2014 Pearson Education Inc 7 Feedback Inhibition a Products of reaction will turn off enzyme b Common for metabolic control 11 Ch 8 V Threonine in active site Enzyme 1 threonine Isoleucme deaminase used up by cell Feedback Active te edlate V quot1mm site no 1 Enzymez m pv v longer available pathway g is halted l quot A Intermediate C Isoleucme binds to quot site no u l 3 End product isoleucine 2014 Pearson Education Inc 8 Where are enzymes in the cell Not a random mix Somme are arranged in a multienzyme complex Some are xed in membrane Some are inside organelles apem 12 Ch 8


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