Chapter 8 Introduction to Metabolism
Feb 24, 2016
Chapter 8Introduction to Metabolism
Think Tank Question…
Using the concepts of energy, entropy, and metabolism answer the following:
Does the concept of evolution violate the 2nd law of thermodynamics? Explain.
Metabolism Metabolism is the sum of all of the chemical reactions
in a biological organism A metabolic pathway is a series of defined steps
resulting in a certain product, each step catalyzed by an enzyme
Catabolic pathway – release energy by breaking down complex molecules into simpler compounds; energetically “downhill”; example – cellular respiration
Anabolic pathway – consume energy to build complicated molecules from simple ones; energetically “uphill”; example - photosynthesis
The energy released from a catabolic pathway is stored and used to complete an anabolic pathway
Energy Energy – the capacity
to cause change or do work
Kinetic energy – energy of motion
Potential energy – stored energy, the energy in an object currently not moving
Thermodynamics Thermodynamics – the study of energy
transformations that occur in a collection of matter
1st law – energy can be transferred and transformed, but cannot be created or destroyed
2nd law – every energy transfer or transformation increases the entropy of the universe Entropy is a measure of randomness or disorder in
the universe Disorder = randomness caused by the thermal motion of
particles; the energy is so dispersed it is unusable.
Back to the tank…
Does evolution violate the 2nd law???
NOPE.① The construction of complex molecules
(metabolism) generates disorder.② Life requires as constant input of energy to
maintain order.
The Laws of Thermodynamics
Free Energy Free energy – the energy available to do work ΔG = ΔH - T ΔS ; the Gibbs-Helmholtz equation
ΔG = the change in free energy, the maximum amount of usable energy that can be harvested
ΔH = enthalpy or total energy in biological systems T = temperature in Kelvin ΔS = change in entropy
Significance Indicates the maximum energy available to do work Indicates whether a reaction will occur spontaneously
or not At equilibrium ΔG = 0
Reaction typesExergonic
Chemical products have less free energy than the reactants
Energetically downhill Spontaneous Loses free energy ΔG is negative - ΔG is the max amount of work the reaction can perform
Endergonic Products have more free energy than reactants Energetically uphill Non-spontaneous Requires energy ΔG is positive + ΔG is the minimum amount of work required to drive
the reaction
Applying Concepts…REACTION REACTANTS PRODUCTS ΔG
Hydrolysis of sucrose Sucrose + H2O Glucose + Fructose 7.0
Triglyceride attachment Glycerol + fatty acid Monoglyceride 3.5
Photosynthesis 6CO2 + 6H2O Glucose + 6O2 686
The table shows some reactions and the absolute values of their associated free energy changes (ΔG).1. For each reaction, would you expect ΔG to
be positive or negative?2. Which reactions will be spontaneous?
Explain your answers.
Cellular Work ATP powers cellular work by coupling exergonic
and endergonic reactions Cell conducts 3 main types of work: mechanical,
transport, and chemical ATP – Adenosine triphosphate
ATP Hydrolysis Breaking of the bonds between phosphate groups ATP + H2O ADP + Pi ΔG = -7.3 kcal/mol or -30.5 kJ/mol (under standard
conditions
Energy Coupling Example
How ATP Performs Work
Regeneration of ATP Organisms at work are constantly using ATP, but
ATP can be regenerated with the addition of a phosphate to ADP
Requires energy; ΔG = +7.3 kcal/mol or +30.5 kJ/mol
Enzymes Enzyme – biological catalysts or catalytic protein (a
chemical agent that speeds up a reaction without being consumed by the reaction) All reactions require an initial investment of energy for starting a
reaction called the activation energy (EA) Enzymes reduce this activation energy
How Enzymes Work
Induced Fit Model Substrate – enzyme reactant Active site – pocket or groove on enzyme that
binds to substrate Enzyme substrate complex – enzyme flexes
and molds to the shape of the substrate
Induced Fit Model
Enzyme Specificity Enzymes function in a
very specific range of environmental conditions including temperature and pH
Some enzymes require ions or other molecule partners: Cofactors – inorganic
nonprotein helpers, ex: zinc, iron, copper
Coenzymes – organic cofactors, ex: vitamins
Enzyme Inhibitors
Competitive inhibitors – block active site, direct competition with substrate
Noncompetitive inhibitors – bind away from the active site, not in direct competition with substrate
Allosteric Regulation
Allosteric regulation can be described as any case in which a protein’s function at one site is affected by the binding of a regulatory molecule to a separate site
Activation, inhibition, and cooperativity
Feedback Inhibition
In feedback inhibition a metabolic pathway is switched off by the binding of its end product to an enzyme that acts early in the pathway
Applying Concepts…
The Scenario: In the boy’s locker room a bacteria is found
growing on some old socks made of a synthetic polymer.
You make a protein extract from the bacteria and isolate the probable enzyme that can cleave the monomers from the polymer.
You also synthesize a dipeptide glycine-glycine to test as a possible inhibitor of the enzyme.
Applying Concepts…
EXPERIMENT CONDITION RATE OF POLYMER CLEAVAGE
1 No enzyme 0.505
2 Enzyme 825.0
3 Enzyme pre-boiled at 100 C 0.520
4 Enzyme + RNA 799.0
5 Enzyme + dipeptide 0.495
1. Explain the results of each experiment.2. How do you think the dipeptide works? How
would you test your hypothesis?