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Energy The capacity to do work or cause particular changes Life is sustained by the trapping and use of energy Use of energy is made possible by the action of enzymes

Energy The capacity to do work or cause particular changes Life is sustained by the trapping and use of energy Use of energy is made possible by the action

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Energy

The capacity to do work or cause particular changes

Life is sustained by the trapping and use of energy

Use of energy is made possible by the action of enzymes

Energy and work

Chemical work

The synthesis of complex biological molecules from simpler precursors

Energy and work

Transport work

The ability to transport molecules against a concentration gradient (uptake of nutrients, elimination of waste, maintenance of ion balance)

Energy and work

Mechanical work

Changing the location of organisms, cells and structures within cells

The flow of carbon and energy

Source of most biological energy is sunlight

Phototrophs trap light energy during photosynthesis

The flow of carbon and energy

Chemolithoautotrophs derive energy from the oxidation of inorganic molecules

Energy from photosynthesis and chemolithoautotrophy can then be used to transform CO2 into organic molecules

The flow of carbon and energy

Chemoheterotrophs can use organic molecules as carbon and energy sources

Energy is released as organic molecules are oxidized to CO2

Oxidation and reduction

Loss of electrons is oxidation (LEO)

Gain of electrons is reduction (GER)

Aerobic respiration is when O2 acts as the final electron acceptor (O2 H2O)

Adenosine 5´-triphosphate (ATP)

ATP serves as the major energy currency of cells

Contains 2 high energy bonds

ATP ADP + Pi + Energy

Energy + ADP +Pi ATP

Pi = orthophosphate

Energy cycle

The laws of thermodynamics

1. Energy can neither be created or destroyed

The total amount of energy in the universe remains constant (although it can be redistributed)

The laws of thermodynamics

2. Physical and chemical processes proceed in such a way that the randomness of the universe increases to the maximum possible

Entropy

A measure of the randomness or disorder of a system

The greater the disorder the greater the entropy

Free energy and reactions

G = H - T x S

G = change in free energy (amount of energy available to do work)

H = change in enthalpy (heat content)

T = temperature in Kelvin (C + 273)

S = change in entropy

Free energy and reactions

G = H - T x S

A reaction with a large positive change in entropy will result in a negative G value and will occur spontaneously

The change in free energy has an effect on the direction of a reaction

Free energy and reactions

G = H - T x S

When G is determined under standard conditions of, pressure, pH and temperature the G is called the standard free energy change (G )

If the pH is set to 7, the standard free energy change is indicated by the symbol G ´

Free energy and reactions

The change in free energy has an effect on the direction of a reaction

Keq = the equilibration constant

Free energy and reactions

When G ´ is negative, the Keq is greater than 1 and the reaction goes to completion as written

The reaction is said to be exergonic

Free energy and reactions

When G ´ is positive, the equilibrium constant is less than 1 and the reaction is not favored

The reaction is said to endergonic

ATP and metabolism

A major role of ATP is to drive endergonic reactions to completion

ATP links energy-yielding reactions with energy-using reactions

Oxidation-reduction reactions

The release of energy normally involves oxidation reduction reactions (redox reactions)

Electrons move from an electron donor to an electron acceptor

Acceptor +ne- donor

(n = number of electrons transferred)

Oxidation-reduction reactions

2H+ + 2e- H2

The equilibrium constant of a redox reaction is called the standard reduction potential (E)

The reference standard for reduction potentials is the hydrogen system with an E ´ of - 0.42 volts

Each hydrogen atom provides 2 protons and 2 electrons

Oxidation-reduction reactions

Redox couples with more negative reduction potentials will donate electrons to couples with more positive potentials (and a greater affinity for electrons)

Oxidation-reduction reactions

Electron tower with most negative reduction potentials at the top

Electrons move from donors to acceptors from more negative to more positive potentials

Electron carriers

Various carriers serve to transport electrons to different parts of the cell

Example - Nicotinamide adenine dinucleotide

NADH + H+ + 1/2 O2 H2O + NAD+

NAD+/ NADH is more negative than 1/2 O2/ H2O, so electrons will flow from NADH (donor) to O2 (acceptor)

Electron carriers

Structure of NAD

Flavin adenine dinucleotide (FAD)

Proteins bearing FAD (or FMN) are referred to as flavoproteins

Coenzyme Q (CoQ) or ubiquinone

Transports electrons and protons in respiratory electron transport chains

Cytochromes

Cytochromes use iron atoms to transport electrons by reversible oxidation and reduction reactions

Iron atoms in cytochromes are part of a heme group

Nonheme iron proteins carry electrons but lack a heme group (e.g. Ferrodoxin)

Enzymes

Enzymes can be defined as protein catalysts

Increase rate of reactions without being permanently altered

Reacting molecules = substrates

Substances formed = product

Structure of enzymes

Some enzymes are composed purely of protein

Some enzymes contain both a protein and a nonprotein component

The protein component = apoenzyme

The nonprotein component = cofactor

Apoenzyme + cofactor = holoenzyme

Structure of enzymes

Cofactor tightly attached to apoenzyme = prosthetic group

Loosely bound cofactor = coenzyme

Classification of enzymes

Enzymes can be placed in one of six classes

Usually named in terms of substrates and reactions catalyzed

Mechanisms of enzyme activity

Enzymes serve to speed up the rate at which a reaction proceed to equilibrium by lowering the activation energy

Activation energy required to from the transition state (AB)

Mechanisms of enzyme activity

The enzyme may be rigid and shaped to precisely fit the substrate

Binding to substrate positions it properly for reaction

Referred to as the lock-and-key model

Mechanisms of enzyme activity

Some enzymes change shape when they bind their substrate so that the active site surrounds and precisely fits the substrate

Referred to as the induced fit model