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Figure 6.1 The complexity of metabolism
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Figure 6.2 Transformations between kinetic and potential energy
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Figure 6.2x1 Kinetic and potential energy: dam
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Figure 6.2x2 Kinetic and potential energy: cheetah at rest and running
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Figure 6.3 Two laws of thermodynamics
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Figure 6.4 Order as a characteristic of life
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Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change
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Figure 6.6 Energy changes in exergonic and endergonic reactions
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Figure 6.7 Disequilibrium and work in closed and open systems
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Figure 6.8 The structure and hydrolysis of ATP
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Figure 6.8x ATP
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Figure 6.9 Energy coupling by phosphate transfer
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Figure The ATP cycle
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Endergonic reactions, such as photosynthesis, proceed
glucose (C6H12O6) + 6 O2 Endergonic reactions, such as photosynthesis, proceed only with a net input of energy. Cells can store energy in the products of such reactions. Exergonic reactions, such as aerobic respiration, end with a net output of energy. Such reactions help cells access energy stored in chemical bonds of reactants. energy in energy out 6 CO2 + 6 H2O Fig. 5.3, p. 74
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Figure 6.11 Example of an enzyme-catalyzed reaction: Hydrolysis of sucrose
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Figure 6.12 Energy profile of an exergonic reaction
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Figure 6.13 Enzymes lower the barrier of activation energy
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product: glucose-6-phosphate activation energy activation energy
without enzyme activation energy with enzyme Energy starting substances: glucose and phosphate Time Fig. 5.6, p. 76
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Figure 6.14 The induced fit between an enzyme and its substrate
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Enzyme Action: Hexokinase
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Figure 6.15 The catalytic cycle of an enzyme
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Figure 6.16 Environmental factors affecting enzyme activity
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glycogen phosphorylase trypsin pepsin Enzyme activity 1 2 3 4 5 6 7 8
9 10 11 pH Fig. 5.11, p. 79
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Figure 6.17 Inhibition of enzyme activity
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X X allosteric activator allosteric inhibitor
allosteric binding site vacant enzyme active site allosteric binding site vacant; active site can bind substrate X substrate cannot bind X active site altered, can’t bind substrate active site altered, substrate can bind Fig. 5.8, p. 78
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Figure 6.18 Allosteric regulation of enzyme activity
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Figure 6.19 Feedback inhibition
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Excess molecules of end product bind to molecules
enzyme 2 enzyme 3 enzyme 4 enzyme 5 Excess molecules of end product bind to molecules of an enzyme that catalyzes this pathway’s first step. The greater the excess, the more enzyme molecules are inhibited, and the less product is synthesized. enzyme 1 end product substrate Fig. 5.9, p. 78
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Figure Cooperativity
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Figure 6.21 Organelles and structural order in metabolism
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