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Chapter 8: Energy and Enzymes

I) Energy
-- the capacity to do work (physics)
-- the capacity to cause change (biochemistry)

A) Two basic types:


1) Potential Energy stored energy
Examples:

- position
- state
- composition

2) Kinetic Energy energy of movement; energy doing work or making change


Examples:

- falling object
- expanding spring
- change in protein conformation
(e.g. muscle contraction)

Energy neither created or destroyed (1st Law of Thermodynamics)


-- changed from one form to another
Ex: Food

With every conversion of energy from one form/state to another, some energy
becomes unusable

(2nd Law of Thermodynamics)

-- conversions not 100% efficient

Entropy amount of disorder in a system (tends to increase)


unusable energy

B) Total Energy = Usable Energy + Unusable Energy


H = G + TS
G = H TS

Greaction = Gproducts Greactants


if G is negative ( G <0), free energy released
If G is positive ( G >0), free energy absorbed

C) Exergonic vs Endergonic Chemical Rxns


1) Exergonic reaction releases free energy (G)
-- Ex: complex molecules simple molecules + free energy

2) Endergonic reaction consumes free energy (+G)


-- Ex: simple molecules + free energy complex molecules

II) Metabolism
-- all the chemical rxns occurring in cell/organism

A) Anabolic / Synthetic
-- build larger, more complex molecules from simpler ones
-- requires energy stored in chemical bonds
-- Example:

B) Catabolic / Degradative
-- breakdown larger molecules to smaller, simpler ones
-- releases energy from chemical bonds
-- Example:

Glucose + O2 CO2 + H2O + Energy


Most chemical rxns are reversible; depends on
In living systems at body temp, most metabolic rxns would occur too slow
How speed up?

III) Enzymes
-- proteins that catalyze chemical rxn without being consumed in rxn
-- lower Activation Energy
-- often end ase
Catalyze
Catalyst
Catalysis

A) Lowering Activation Energy


-- reactants at stable state need input of energy to get started
-- overall, rxn may be exergonic

B) Enzymes are Specific


-- enzymes bind substrate at Active Site allows recognition
substrate
product

C) How Do Enzymes Work?

D) Enzymes Usually Work in Sequence


-- allows organization of the many biochem rxns in body
-- Metabolic Pathways product of one rxn is substrate for next rxn in sequence

E) Measuring Enzyme Activity


A + B

measure: i) production of C
ii) decrease of A and/or B

1) Effects of Temperature or (2) pH on Enzyme Activity

3) Effects of Enzyme and Substrate Concs

Michaelis-Menten curve

F) Targeting Enzymes (Medical applications)


-- many drugs (and poisons) target/inhibit enzymes
Ex: cyclooxygenase and aspirin

COX1, COX2
Arachidonic Acid
(20C, polyunsat. fatty acid)

Prostaglandins (signal pain)


Thromboxanes (bld clot formation)
Leukotrienes (inflammation)

G) Enzyme Inhibition
1) Irreversible inhibitor irreversibly binds enz (Ex: Sarin binds cholinesterase)
2) Reversible inhibitor binds/unbinds; used by cells themselves to regulate enzs
a) Competitive
b) Non-competitive

H) Cofactors
-- required by enzymes for activity
1) Inorganic (non-carbon): Cu, Fe, Mg, Zn

2) Organic (= coenzymes) converted vitamins (Vit B1, Vit B2)


Ex: porphoryn in hemoglobin

Coenzyme
Ex 2: Niacin (Vit B3)
Riboflavin (Vit B2)

NAD
FAD

Redox Reactions
Oxidation
Reduction

Fatty Acid + NAD


(reduced)

(oxidized)

Fatty Acid + NADH + H


(oxidized)

(reduced)

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