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Chapter 8: Overview: The Energy of Life

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    Overview: The Energy of Life

    y The living cell is a miniature factory where thousands of reactions occur and convertsenergy in many ways

    An organisms metabolism transforms matter and energy, subject to the laws of

    thermodynamics

    y Metabolism- all of an organisms chemical reactionsOrganization of the Chemistry of Life into Metabolic Pathways

    y Metabolic pathway- begins w/ a specific molecule which is then altered in a series ofdefined steps, resulting in a product.

    y Catabolic pathways- break down pathway,release energyy Anabolic pathways- consume energy to build complicated molecules from simpler ones

    Forms of Energy

    y Energy- the capacity to cause changey Kinetic energy- energy associated w/ the relative motion of objectsy Heat or thermal energy is kinetic energy associated w/ the random movement of atoms

    or molecules

    y Potential energy- is energy that matter possesses b/c of its location or structurey Chemical energy- the potential energy available for release in a chemical reactiony Energy can be converted from one form to another:

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    The Laws of Energy Transformation

    y Thermodynamics- the study of energy transformations that occur in a collection ofmatter

    y According to the first law of thermodynamics- energy can be transferred andtransformed, but it cannot be created or destroyed(principle of conservation of energy)

    y According to the second law of thermodynamics- every energy transfer oftransformation increases the entropy of the universe

    y Entropy- a measure of disorder, or randomnessy For a process to occur spontaneously, it must increase the entropy of the universe

    Biological Order and Disorder

    y Universe- the system plus its surroundingsThe free-energy change of a reaction tells us whether the reaction occurs spontaneously

    Free- Energy Change, (G

    y Free energy- measures the portion of a systems energy that can perform work whentemp and press. are uniform, as in a cell

    y The change in free energy, Gduring a biological process, can be calculated for anyspecific chemical reaction w/ this formula:

    G = H TS

    y H symbolizes the change in the systems enthalpy(= total energy), S is the change inthe systems entropy, and T is the absolute temp on Kelvin(K)

    Free Energy, Stability, and Equilibrium

    y Organisms live at the expense offree energyy During a spontaneous change free energy decreases and the stability of a system

    increases

    y Equilibrium- term for a state of maximum stability

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    Free Energy and Metabolism

    Exergonic andEndergonic ReactionsinMetabolism

    y Exergonic reaction- proceeds with a net release of free energy and is spontaneous

    y Endergonic reaction- absorbs free energy from its surroundings and is nonspontaneous

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    Equilibrium and Metabolism

    y Reactions in a closed system eventually reach equilibrium and can then do work

    y Cells in our body- experience a constant flow of materials in and out, preventingmetabolic pathways from reaching equilibrium

    y An analogy for cellularrespiration:

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    ATP powers cellular work by coupling exergonic reactions to endergonic reactions

    y A cell does three main kinds of work Mechanical- such as the beating of cilia Transport- pumping of substances across membranes C

    hemical-

    the pushing of endergonic reactionsy Energy coupling- the use of an exergonic reaction to drive an endergonic oneThe Structure and Hydrolysis ofATP

    y ATP (adenosine triphosphate)- cells energy shuttle, provides energy for cellularfunctions

    y Energy is released from ATP when the terminal phosphate bond is broken:

    y ATP hydrolysis can be coupled to other reactions:

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    How ATP Performs Work

    y ATP drives endergonic reactions by phosphorylation, transferring a phosphate to othermolecules

    y The three types of cellular work are powered by the hydrolysis of ATP:

    The Regeneration ofATP

    y Catabolic pathways drive the regeneration of ATP from ADP and phosphate:

    Enzymes speed up metabolic reactions by lowering energy barriers

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    y A catalyst is a chemical agent that speeds up a reaction without being consumed by thereaction

    y An enzyme is a catalytic proteinThe Activation Barrier

    yEvery chemical reaction between molecules involves both bond breaking and bondforming

    y The activation energy, EA, or free energy of activation- energy required to contort thereactant molecules so the bonds can change, its supplied in form of heat from

    surroundings

    y The energy profile for an exergonic reaction:

    How Enzymes Lower the EA Barrier

    y An enzyme catalyzes reactions by lowering the EA barriery The effect of enzymes on reaction rate:

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    Substrate Specificity of Enzymes

    y Substrate- reactant an enzyme acts ony enzyme-substrate complex formed when the enzyme binds to its substratey A

    ctive site-

    region on the enzyme where the substrate binds(a)

    y Induced fit of a substrate- brings chemical groups of the active site into positions thatenhance their ability to catalyze the chemical reaction(b)

    Catalysis in the Enzymes Active Site

    y The catalytic cycle of an enzyme:

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    y The active site can lower an EA barrier by:o Orienting substrates correctlyo Straining substrate bondso Providing a favorable microenvironmento C

    ovalently bonding to the substrateEffects of Local Conditions on Enzyme Activity

    Effects of Temperature and pH

    y Each enzyme has an optimal temperature in which it can function:

    y And an optimal pH in which it can function:

    y Cofactors- nonprotein enzyme helpersy Coenzymes- organic cofactors

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    y Competitive inhibitors bind to the active site of an enzyme, competing with thesubstrate:

    y Noncompetitive inhibitors bind to another part of an enzyme, changing the function

    Regulation of enzyme activity helps control metabolism

    Allosteric Regulation of Enzymes

    y Allosteric regulation- term used to describe any case in which a proteins function atone site is affected by binding of a regulatory molecule at another site

    y Most allosterically regulated enzymes are constructed from one or more polypeptidechains

    y They change shape when regulatory molecules bind to specific sites, affecting function

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    y Cooperativity- a form of allosteric regulation that can amplify enzyme activity

    y Feedback inhibition- The end product of a metabolic pathway shuts down the pathway


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