Ch6 Study Guide and Practice Questions

This chapter gives you the basics in retrieval of energy in chemical reactions, which is applied to
cellular respiration (Chapter 7). So, on test 2, one question can have concepts introduced in both
Ch6 and Ch7.

Concepts to grasp
Energy
Definition
How organisms are classified by the method of obtaining both energy and carbon
Metabolism
You have to understand this in terms of getting or giving energy
Metabolism consists of catabolism and anabolism.
Potential vs. kinetic energy
Define, recognize and compare potential and kinetic energy.
We can retrieve energy by moving things. An example is flowing water, imagine how to
generate hydropower from water stored in a dam.
The first law of thermodynamics
Energy is not created or destroyed but it does change it form, which allows us to get energy
(creating ATP) from food. Energy on the left side (of a chemical equation) “” is the same as
that on the right side.
The second law of thermodynamics
A degree of disorder (entropy) increases when energy transforms. Imagine a situation where
you see a polymer (one molecule) that becomes a bunch of monomers (many molecules).
One becomes many; that is, an increase in a degree of disorder. Know that you will always
lose some energy as heat when energy transforms.
Gibbs free energy (G) --- Usable energy in a molecule
In my class, we ignore TS (energy that escapes as heat that is discussed in the book). You do
have to know which side in a chemical reaction has more energy. This allows you to figure
out if the DG is negative or positive.
Endergonic and exergonic reactions (be able to define and use these terms)
Of course, you have to grasp this with Gibbs free energy (G). Know the relationship between
the change in G and the energy available in reactants vs. products.
Connect to energy available to do work vs. energy needed to drive the reaction
Connect to spontaneous vs. non-spontaneous reactions
Polymers (big chemical molecules) have more energy per molecule than monomers
(smaller molecules).
Energetic Coupling
How can you determine if the hydrolysis of ATP can drive an endergonic reaction?
Enzymes --- biological catalysts
The major role of enzymes is to reduce the activation energy of a transient state from
reactants to products. This can be obtained by stabilizing transient chemical bonds formed in
intermediate products (ES complex) between reactants and products. Most chemical
reactions go through transient molecules (or intermediates) between reactants and products.
Active site of enzyme is created in the tertiary structure
Inhibition and activation of enzymes by “fake” substrates and other molecules - inhibitors.
You must understand the difference between competitive and non-competitive
inhibition.
Activators vs. Inhibitors
Reversible vs. Irreversible Inhibitors
Allosteric vs. Competitive Inhibitors
Feedback loops or regulation, positive or negative --- This is a very important concept to
allow biological reactions as to operate as efficiently as possible. This will be
connected to those in Ch7.
This type of regulation often occurs through allosteric effects.

Practice Questions

Q1: When reactants have more energy than products in a chemical reaction what is DG (positive
or negative)?

Q2: A proton gradient created as shown in Fig. 5.13 has (potential/kinetic) energy. (Choose
one)

Q3: Chemical reactions always have an unstable state called the (A) state even in exergonic (or
spontaneous) reactions. This state has an amount of energy called (B), so we have to provide
additional energy to push the reaction forward to get products from reactants. In the cell, (C)
help reduce (B) so that chemical reactions go faster. Since (C) themselves do not change, (C) are
also called (D).

Q4: Enzymes are remarkable biological molecules that catalyze chemical reactions. The site for
chemical reactions in an enzyme is called an (A) site and consists of several amino acids. In
many cases, these amino acids are not next to each other in its (B) structure, but assemble in one
functional unit in its (C) structure. Therefore, folding enzymes into the right configuration is
essential.

Q5: Threonine dehydratase is the first enzyme in the process of making isoleucine from
threonine. The activity of this enzyme is regulated positively and negatively. This is a typical
example of regulatory loops, which helps us understand how the cell (or the body) controls
biological chemical reactions. The enzyme has two (A) sites, one for threonine, and the other for
isoleucine. To make a balance of threonine and isoleucine, the enzyme becomes more active
when the cell has excess of threonine because binding of threonine to one of (A) sites stimulate
the catalytic activity of threonine dehydratase. On the other hand, when isoleucine accumulates
in the cell, the enzyme becomes less active because binding of isoleucine to the other (A) sites
inhibits the catalytic activity of this enzyme. Threonine and isoleucine are called (B) regulators.
The effect of isoleucine on threonine dehydratase is also called (C).
For Q10 and Q11, you have to understand the fundamental difference between
competitive and non-competitive inhibitions in terms of inhibitor’s binding site with
respect to enzymes’ active sites.

Q10: The table below explains how competitive inhibition works. Fill the blank cells with 0, 25,
50, 75, or 100. Assume the number of enzymes is the same in all conditions.

Number of substrate Number of inhibitor molecules Enzyme activity (Products

molecules made)

100 0 100
50 50 50
25 75 25
100 100
100 300
150 50

The inhibitor in this question is a competitive inhibitor. So, a ratio of inhibitors to

substrates determines a degree of inhibition.

Q11: The table below explains how non-competitive inhibition (allosteric) works. Fill the blank
cells with 0, 25, 50, 75, 100. Assume the number of enzymes is the same in all conditions.

Number of substrate molecules Number of inhibitor molecules Enzyme activity

200 0 100
100 50 50
50 100 0
100 100
200 100
300 100
200 50

The inhibitor in this question is a non-competitive inhibitor. So, an absolute amount of

inhibitors determines a degree of inhibition regardless of an amount of substrates.