BIOL1000

LECTURE 6 & 7
CHAPTER 8 (TEXTBOOK)
ENERGY & ENZYMES

KEY TERMS
Enthalpy (H) - The total energy in a molecule. includes the potential energy of the molecule, often referred to as heat
content, plus the effect of the molecule on the pressure and volume of its surroundings.
- to warm within
- internal/system energy
- measures the internal energy / system energy
- total energy associated with a system
- associated with motion (train in motion, water in waterfall top contains most kinetic energy, when one atom
bumps into another atom, it puts it into motion)
- thermal energy (energy contained in system responsible for its temperature)
- a type of kinetic energy, due to particle movement and motion in system
- heat is flow of thermal energy
- any object that contains temperature contains thermal energy
- can be potential, kinetic, or thermal energy

Entropy (S)- Another factor that changes during a chemical reaction is the amount of disorder or entropy (symbolized
by S). When the products of a chemical reaction become less ordered than the reactant molecules were, entropy increases
and ΔS is positive. The second law of thermodynamics, in fact, states that total entropy always increases in a system
that includes the surroundings as well as the products of the reaction
- describes how energy will be distributed into the system
- measure of energy dispersal
- i.e. heating water beaker, water is heated and dispersed into surrounding (entropy
increases) into system and surroundings)
- water will have higher thermal state, environment will have lower thermal state
- how does entropy increase? when energy becomes more spread out
i. e. more in volume (phase change), more in number (catabolic change)(number of molecules
increases in system; energy becomes more spread out into each molecule), more molecular motion
(i.e. heating an object; each molecule takes more energy state)
- the part of system energy associated with system and unavailable for work
- a measure of energy dispersion in a system
- energy conversion can never be 100% because entropy increase in energy transformation

Endorgenic - Reactions are nonspontaneous when ΔG is greater than zero. Such reactions are termed endergonic.
When ΔG is equal to zero, reactions are at equilibrium.
- energy reaction - energy required, nonspontaneous reaction
- ∆G > 0
- reactant carries lower free energy and product contains higher free energy
- energy required to be put into system

Exergonic - Chemical reactions are spontaneous when ΔG is less than zero. Such reactions are said to be exergonic
- energy released spontaneously (∆G < 0 )
- i.e. rock at top of mountain vs after it rolls down hill (∆H < 0) (∆S > 0)
- Negative ∆G = energy releases in reaction = exergonic reacion = reaction begins in higher state and
ends in lower state

Free Energy (G) - Portion of a systems energy that is available to do work (convertible energy)
- Gibbs free energy performs all the work for a life
- free energy is determined by enthalpy (H) (internal system energy) and entropy (S)
(associated with system)
- To determine whether a chemical reaction is spontaneous, it’s necessary to assess the amount of
energy in the reaction available to do work—what chemists call Gibbs free energy (symbolized by G). This is
accomplished by determining the change in Gibbs free energy (ΔG) in the reaction, which is based on changes
in enthalpy and entropy as shown in the standard free-energy change equation:
∆G = ∆H - T∆S
Convertible energy (G) = System internal energy (H)(enthalpy) - (system associated energy
(nonconvertible)) (S= entropy)
T = temperature in kelvin
 CHANGE IN FREE ENERGY
∆G = G(final state) - G (initial state)
OR
∆G = G in products - G in reactants

∆ = Delta (change)
∆G = process of energy that changes

Chemical reactions
∆G = ∆H - T∆S
where ∆G - G(final) - G (initial)
∆H = H(final)- H(initial)
∆S = S(final) - S(initial)
T stands for temperature measured on the Kelvin scale (see BioSkills 1). To convert Celsius to Kelvin, you add 273.15°.
In words, the change in Gibbs free energy in a reaction is equal to the change in enthalpy minus the product of the change
in entropy and the temperature. Thermal energy increases the amount of disorder in the system, so the TΔS term simply
means that the faster molecules are moving, the more important entropy becomes in determining the change in Gibbs free
energy.

Spontaneous chemical reactions run in the direction that lowers the free energy of the system. Exergonic reactions are
spontaneous and release energy; endergonic reactions are non
spontaneous and require an input of energy to proceed

- reactions in a closed system eventually reach equilibrium and can then do no work
- Negative ∆G = energy releases in reaction = exergonic reacion = reaction begins in higher state and ends in lower
state

Activated Carrier Molecule - - include ATP, FADH2, NADH

- facilitate anabolic reaction

Activation Energy (E) - Even if the reaction is spontaneous, a certain amount of kinetic energy—called the activation
energy—is required to strain the chemical bonds in substrates so they can achieve the transition state. How do enzymes
help clear the activation energy hurdle? Enzymes Lower the Activation Energy Reactions happen when reactants
have enough kinetic energy to overcome the activation energy barrier. The kinetic energy of molecules, in turn, is a
function of their temperature.
- include ATP, FADH2, NADH
- facilitate anabolic reaction
- in order to start, you have to break chemical bond and make it unstable then react
- initial energy required to break the barrier (old bond)
- initial energy invested to start a reaction
- energy required to get a reactant to the transition state to start a reaction
- can be achieved by heating to achieve chemical reaction (ie heating wood)
- enzymes can lower activation energy

Active Site
Substrate
Reactants
Catalysis - to increase the rate of chemical reaction
- can make reaction faster and are not destroyed during chemical reaction
- can be used for many parts of the reaction
Cofactor - metals ie. copper, zinc, iron
Coenzyme - some enzymes require cofactor / coenzymes
- organic molecules ie. vitamins
Enzyme inhibitor
Competitve - inhibiting molecule binds to active site, preventing binding of substrate
- inhibiting molecule COMPETES with substrate for active site
- if there are more of inhibitors than substrate, you prevent binding
- if you have more substrate than inhibitor, you reverse the effect
Noncompetitve - molecule binds to enzyme but NOT the active site, binds to
allosteric site
Allosteric site - site on the enzyme that allows substrate to bind when non-competitve inhibitor binds
 - non competitve binding of molecules to enzyme to increase affinity of
substrate-allosteric activator activates the enzyme (makes the enzyme more
effective)

- allosteric inhibitor is non-competitve binding of molecules to enzyme to decrease

affinity of substrate-enzyme interaction (makes enzyme less effective)

Feedback inhibition

Which reaction(s) proceed without external input of energy?

- diffusion and oxidation
- will react spontaneously (without need of external energy)

What is energy?
- active working
- the capacity to do work
- the ability to move or elicit change
- based on mass-energy equation (E=MC squared), any object that has mass carries energy. Everything
has energy! photon is a packet of light energy but NO MASS

POTENTIAL VS KINETIC ENERGY

Potential energy - stored energy due to location / structure (chemical bonds, i.e. specific
arrangements of atoms)

LAWS OF THERMODYNAMICS
1. Energy cannot be created or destroyed, only transferred
2. Entropy of a system and the surroundings will increase - energy will always become more spread
out
a) Energy spontaneously disperses from being localized to becoming spread out if it is not
hindered from doing so
b) Why does it do this? because it tries to reach an equilibrium (become more evenly
distributed)

Which of the following cell structures would you expect to be present in bacterium except
____________
a) peptidoglycan layer
b) nuclear membrane - dont have bacterium
c) plasma membrane
d) ribosomes

Which of the following cell structures would you expect to be most important in the growth of
bacteria on the surface of your teeth?
a) cell wall
b) fimbriae - based on cell structure
c) flagella
d) cillia

Which of the cell structures would you expect to be required for the function of eukaryotic cells (i.e.
making a large number of membrane proteins?
a) ER
b) peroxisome
c) lysosome
d) mitochondria

Which molecules will move the nucleus througfh the nuclear pore complex?
a) mRNA
b) Ribosome subunits
c) rRNA
d) tRNA
e) Nuclear proteins - made in the cytoplasm, will have nuclear localization signal (serves as post code
to which cells transport proteins back into nucleus to perform function)

Which of the following supports that mitochondrion evolved from bacteria?

a) mitochondrion contains a circular DNA
b) mitochondrion contains its own ribosomes
c) mitochondrion cell division resembles binary fission
d) All the above

A neutrophil (white blood cell) is suddenly unable to move, and can no longer chase bacteria. What
may have caused this?
a) increased concentration of microtubules
b) reduced number of intermediate filaments in the cell cortex
c) increased rate of cytoskeleton assembly and disassembly
d) degradation of actin protein

When a fish eye gets lighter (pigment granule vesicles distributed towards center of the cell), which
motor protein is at work?
a) kinesin - going to the plus end, where microtubules
b) dynein - center of the cell
c) microtubules
d) myosin

When a fish eye gets darker (pigment granule vesicles distributed towards plasma membrane), which
motor protein is at work?
e) kinesin - going to the plus end, where microtubules
f) dynein - center of the cell
g) microtubules
h) myosin

METABOLISM
 Catobolic Anabolic
Chemical Reactions Chemical Reactions

Breakdown: complex molecules into simpler Use simpler molecules to build more complex
compounds ones

uses energy to break down molecules uses energy to build molecules

i.e. starch broken down to glucose molecules i.e. protein synthesis (amino acids build to make
protein)
RELEASE energy (exergonic reaction)
USE ENERGY (endergonic reaction)

Enthalpy (H) decreases and Entropy (S) increases Enthalpy (H) increases and Entropy (S) decreases

∆G < 0
(is a negative value) ∆G > 0

performs spontaneous energy cannot perform spontaneously

ie. waterfall starts with high potential energy and ends
with lower potential energy)
i.e. wood burning)

ATP (adenosine triphosphate) - ‘high’ energy molecule

- catabolic and anabolic reaction
- activated to carry a molecule (energy) to drive anabolic
reaction
- contains 3 phosphate groups
- ATP can hydrolyze into ADP (anabolic)
- glutamine synthesis (anabolic reaction; requires energy),
since G is greater than 0, requires ATP to provide energy
- in a endergonic reaction coupled with exergomic reaction

Redox reactions
- reduction oxidation reactions are energetically coupled
- oxidation = loss of an electron (s), reduced compound A (reducing agent) is oxidized, losing
electrons. creating A to be oxidized compound (exorgonic reaction) (catabolic)
- reduction = gain of electron (s), oxidized compound B (oxidizing agent) is reduced, gaining electrons
(endergonic reaction) (anabolic)
- oxidation and reduction are two-half reactions, always occurring together
O = oxidation
I = is
L = lost
Oxidation is loss of electron

R = reduction
I = is
G = gaining
reduction is gaining electron

ENZYMES
- class of proteins that CATALYZE chemical reactions
- CATALYZE = to increase the rate of chemical reaction
 - are not destroyed during chemical reaction, therefore the same enzyme molecule can be
used many times
- enzymes can lower activation energy
- works to promote reactant to transition state
- reaction without enzyme = linear, runs at lower rate (velocity correlates with (S) only)
- reaction with enzyme = hyperbolic (exponential; non linear) (velocity associates with (E)(S))
- S = substrate concentration
- E = enzyme

- when you have excess substrate, rate will increase linearly with enzyme concentration (faster rate
reaction) (when S is constant in great excess of E)
- How does an enzyme work?
- substrate molecule binds to the active site of an enzyme
- usually a pocket or cleft of enzyme surface
- a region of catalysis occurs
- substrate specifically - shape of the enzyme at substrate site allows enzyme
specifically and bind substrate

1. enzyme binds to substrate at the active site

2. enzyme promotes substrates to reach the transition state
3. enzyme releases products as products have less affinity for the active site

What limits the rate of catalysis?

1. Enzyme-catalyzed reactions can be saturated
a) at high substrate concentration, enzyme-catalyzed reactions reach a maximum rate.
uncatalyzed reactions slowly increases as substrate concentration increases
b) Rate plateaus when enzyme is saturated with substrate

temperature effects enzyme activity

- enzymes have optimal temperatures to operate

pH effects enzyme activity

- enzymes have optimal pH to operate optimally (increase/decrease rate of reaction)

Enzyme can be modified after its been synthesized