Enzyme and Energy

Production
2020
Catalysis
 VIDEO

Enzyme: Most are proteins

A compound produces another compound
Enzymes are classified by the reactions they
catalyze

• Name: Urease vs Pepsin “pepsis”

• ATP+ D-glucose → ADP + D-glucose 6-phosphate

• ATP:glucose phosphotransferase
Metabolic Pathways
• A metabolic pathway has many steps reactions, each catalyzed by a
specific enzyme

Enzyme 1 Enzyme 2 Enzyme 3

A B C D

Reaction 1 Reaction 2 Reaction 3

Product
Starting
molecule
 The catalytic cycle of an enzyme
1 Substrates enter active site; enzyme
changes shape so its active site 2 Substrates held in
embraces the substrates (induced fit). active site by weak
interactions, such as
hydrogen bonds and
ionic bonds.

3 Active site (and R groups of

Substrates Enzyme-substrate its amino acids) can lower EA
complex and speed up a reaction by
• acting as a template for
substrate orientation,
6 Active site • stressing the substrates
Is available for and stabilizing the
two new substrate transition state,
Mole. • providing a favorable
microenvironment,
Enzyme
• participating directly in the
catalytic reaction.

5 Products are
Released. 4 Substrates are
Converted into
Products Products.
Energy Activation (Ea) and the Change in Free Energy (ΔG)
Rate vs Equilibrium

ΔG
Protection of an Enzyme against Denaturation by Heat

• When enzyme solutions are heated, there is a progressive loss of

catalytic activity over time due to denaturation of the enzyme.
• A solution of the enzyme urease incubated at 500C lost 60% of its
activity in 10 min, but when incubated at 500C in the presence of a
very large concentration of one of its substrates, it lost only 5% of its
activity in 10 min.
• Why thermal denaturation of urease was retarded in the presence of
one of its substrates?
• The enzyme-substrate complex is more stable than the enzyme
alone.
Metabolism :
Catabolism and Anabolism
Energy release
Two important concepts:

Reduction
Free energy
potential
(G)
(E’°)

∆ G = – n F ∆E’°
 -
• The first law of thermodynamics describes
the principle of the conservation of energy:
“In any physical or chemical change, the total
amount of energy in the universe remains constant,
although the form of the energy may change.”

• The flow of electrons (redox reaction)

provides energy for organisms.
• Electron tends to flow to more positive
reduction potential (E’°).
• Higher ∆E’° results in higher ∆G’°.
 -
• Correlation of free energy change (∆G )
and reduction potential difference (∆E’°)

∆G’° = – n F ∆E’°

∆G’° = free energy change (kJ/mol)

n = amount of transferred electron
F = Faraday constant = 96.5 kJ/V.mol
∆E’° = reduction potential difference (V)
= E’° receptor – E’° donor
- Higher ∆E’°, greater ∆G’°
- Exergonic reaction : ∆G’° < 0
 ∆G’° = – n F ∆E’°

F = 96.5 kJ/V.mol
Half-reactions : Electron acceptor = ?
Electron donor = ?
∆E’° = ?
∆G’° = ?
 Exergonic and Endergonic Reactions
Exergonic reaction has net release of free energy and is spontaneous

Reactants

Amount of
energy
released ∆G = Negative
(∆G <0)
Free energy

Energy

Products

Progress of the reaction

Figure 8.6 (a) Exergonic reaction: energy released

 Exergonic and Endergonic Reactions
Endergonic reaction absorbs free energy & non-spontaneous

Products

Amount of
energy ∆G = Positive
released
Free energy

(∆G>0)
Energy

Reactants

Progress of the reaction

Figure 8.6 (b) Endergonic reaction: energy required

 Energy production
Nutrient molecules have energy in the form of
bonds between atoms
Various catabolic reactions accumulate energy
into the bonds of ATP (adenosine
triphosphate)
ATP has “high energy” or unstable bonds which
allows the energy to be released quickly and
easily
Energy is released from ATP when the terminal
phosphate bond is broken
Provides energy for cellular functions → the
cell’s energy shuttle
The Regeneration of ATP
• Catabolic pathways drive regeneration of ATP from ADP and phosphate

ATP synthesis from ATP hydrolysis to

ADP + P i requires energy ADP + P i yields energy

ATP

Energy from catabolism Energy for cellular work

(exergonic, energy yielding (endergonic, energy-
processes) consuming processes)

ADP + P i
Figure 8.12
 Electron transfer
• Reduction is the
gaining of electrons by
a molecule

• Oxidation is the
removal of electrons
from a molecule
Electron carriers
2H+ + 2e-

• In catabolic reactions, energy is NAD+ NADH + H+

extracted from molecules in the
form of electrons, which are
transferred, along with H+ ions, to
electron carriers like NAD+. This
energy is used to generate ATP
Mechanisms of ATP generation

• Substrate-level phosphorylation ANOTHER VIDEO

• Oxidative phosphorylation
• Photophosphorylation

• ATP is generated when a high-energy phosphate is transferred

directly to ADP from a phosphorylated substrate
Oxidative phosphorylation
• Electrons are transferred from organic compounds
through a series of electron carriers to O2 or other
oxidized inorganic or organic molecules
• The sequence of electron carriers is called the
electron transport chain
• The transfer of
electrons from
one carrier to the
next generates
energy which is
used to make ATP
from ADP by
chemiosmosis
Photophosphorylation
Only occurs in photosynthetic cells which contain light trapping pigments such as chlorophyll
Light causes chlorophyll to give up electrons

Energy released from the transfer

of electrons (oxidation) of
chlorophyll through a system of
carrier molecules is used to
generate ATP
How the released energy
Electron transfer in mitochondria is
conserved into ATP? coupled by H+ pump.

H+ pump generates the proton-

motive force, the simultaneous
effect of the pH gradient across the
membrane and trans-membrane
electrical potential that drives the
ATP synthesis from ADP and Pi.

Electron transport system

ATP synthase

►Mitochondria
2. Oxidation-Reduction Reactions
• The NADH dehydrogenase complex of the mitochondrial respiratory
chain promotes the following series of oxidation-reduction reactions,
in which Fe3+ and Fe2+ represent the iron in iron-sulfur centers, Q is
ubiquinone, QH2 is ubiquinol, and E is the enzyme:

• For each of the three reactions catalyzed by the NADH dehydrogenase

complex, identify (a) the electron donor, (b) the electron acceptor, (c)
the conjugate redox pair, (d) the reducing agent, and (e) the oxidizing
agent.
 (a) the electron donor, (b) the electron acceptor, (c) the
conjugate redox pair, (d) the reducing agent, and (e) the
oxidizing agent.

1. (a), (d) NADH; (b), (e) E-FMN; (c) NAD/NADH and E-FMN/FMNH2
2. (a), (d) E-FMNH2 ; (b), (e) Fe3+ ; (c) E-FMN/FMNH2 and Fe3+/Fe2+
3. (a), (d) Fe2+; (b), (e) Q; (c) Fe3+/Fe2+ and Q/QH2
Thank you
• Next week: Biological membranes and transport and Biosignaling
Problems
1. Properties of Lipids and Lipid Bilayers
Lipid bilayers formed between two aqueous phases have this important
property: they form two-dimensional sheets, the edges of which close
on each other and undergo self-sealing to form vesicles (liposomes).
a) What properties of lipids are responsible for this property of
bilayers? Explain.
b) What are the consequences of this property for the structure of
biological membranes?
2. Hot and Cool Taste Sensations
The sensations of heat and cold are transduced by a group of
temperature-gated cation channels. For examples, TRPV1, TRPV3, and
TRPM8 are usually closed, but open under the following conditions:
TRPV1 at ≥43⁰C; TRPV3 at ≥33⁰C; and TRPM8 at <25⁰C. These channels
are expressed in sensory neurons known to be responsible for
temperature sensation.
a) Propose a reasonable model to explain how exposing a sensory
neuron containing TRPV1 to high temperature leads to a sensation
of heat.
b) Capsaicin, one of the active ingredients in “hot” peppers, is an
agonist of TRPV1. Capsaicin shows 50% activation of the TRPV1
response at a concentration (i.e., it has an EC50) of 32 nM. Explain
why even a very few drops of hot pepper sauce can taste very “hot”
without actually burning you.