Figure 8.

Enzymes
Catalyze

the chemical reactions of life

Enzymes: an example of catalysts, chemicals

that increase the rate of a chemical reaction

without becoming part of the products or being
consumed in the reaction

Activation energy is the energy required to bring all molecules

in a chemical reaction into the reactive state

Enzymes overcome activation energy

How Enzymes Lower Ea

By increasing concentrations of substrates at active site

of enzyme
By orienting substrates properly with respect to each
other in order to form the transition-state complex
Increasing thermal energy to increase molecular
velocity
Induced fit model for enzyme-substrate interaction

Enzyme Structure

Most- protein
Can be classified as simple or conjugated
Simple enzymes- consist of protein alone
Conjugated enzymes- contain protein and non-

protein molecules

Conjugated enzyme/Holoenzyme
Apoenzyme
protein component of an enzyme

Cofactor
nonprotein component of an

enzyme
prosthetic group firmly attached
coenzyme loosely attached, can
act as carriers/shuttles

Holoenzyme

= apoenzyme +

cofactor
7

Cofactors: Supporting the Work of

Enzymes

Metallic cofactors
Include Fe, Cu, Mg, Mn, Zn, Co, Se
Metals activate enzymes, help bring the active site and

substrate close together, and participate directly in

chemical reactions with the enzyme-substrate complex

Coenzymes
Organic compounds that work in conjunction with an

apoenzyme to perform a necessary alteration of a

substrate
Removes a chemical group from one substrate molecule
and adds it to another substrate
Vitamins: one of the most important components of
coenzymes

conjugated enzyme (holoenzyme)

Location and Regularity of Enzyme

Action
Either

inside or outside of the cell

Exoenzymes break down molecules outside
of the cell
Endoenzymes break down molecules inside
of the cell

Figure 8.5

Rate of Enzyme Production

Enzymes

are not all produced in the cell in

equal amounts or at equal rates
Constitutive enzymes: always present and in

relatively constant amounts

Regulated enzymes: production is either
induced or repressed in response to a change in
concentration of the substrate

Figure 8.6

14

Synthesis and Hydrolysis Reactions

Transfer Reactions by
Enzymes

Oxidation-reduction reactions

A compound loses electrons (oxidized)

A compound receives electrons (reduced)
Common in the cell
Important components- oxidoreductases

Other enzymes that play a role in necessary

molecular conversions by directing the transfer of
functional groups:

Aminotransferases
Phosphotransferases
Methyltranferases
Decarboxylases

The Sensitivity of Enzymes to Their

Environment

Enzyme activity is highly influenced by the

cells environment
Enzymes generally operate only under the
natural temperature, pH, and osmotic pressure
of an organisms habitat
When enzymes subjected to changes in normal
conditions, they become chemically unstable
(labile)
Denaturation: the weak bonds that maintain
the native shape of the apoenzyme are broken

 Energy

in Cells

Exergonic reaction: a reaction that releases

energy as it goes forward

Endergonic reaction: a reaction that is driven
forward with the addition of energy

19

Figure 8.13

How does a cell produce

ATP?

3 types of Phosphorylation
Substrate

level phosphorylation
Oxidative phosphorylation
Series of redox reactions occurring during the

final phase of the respiratory pathway

Photophosphorylation
ATP is formed through a series of sunlight-

driven reactions in phototrophic organisms

Oxidative
phosphorylation
and
Photophosphorylation
use
the
Electron Tranport Chain via proton
motive force to produce ATP

Electron Carriers
located

in plasma membranes of
chemoorganotrophs in bacteria and archaeal
cells
located in internal mitochondrial
membranes in eukaryotic cells
examples of electron carriers include NAD,
NADP, and others
24

Electron Transport Chain

(ETC)
Electron carriers
organized into ETC
first electron carrier

having the most negative

Eo
the potential energy
stored in first redox
couple is released and
used to form ATP
first carrier is reduced
and electrons moved to
the next carrier and so on
25

Electron Carriers
NAD
nicotinamide

adenine
dinucleotide
NADP
nicotinamide

adenine
dinucleotide
phosphate
26

Electron Carriers
FAD
flavin adenine

dinucleotide
FMN
flavin

mononucleotide
riboflavin phosphate
coenzyme

Q (CoQ)

a quinone
riboflavin
also called
27

ubiquinone

Electron Carriers
Cytochromes
use iron to transfer

electrons

iron is part of a heme

group

Nonheme

iron-sulfur

proteins
e.g., ferrodoxin
use iron to transport

electrons

28

iron is not part of a

heme group

Figure 8.15

The Embden-Meyerhof
Pathway
Occurs

in cytoplasmic matrix of most

microorganisms, plants, and animals
The most common pathway for glucose
degradation to pyruvate in stage two of
aerobic respiration
Function in presence or absence of O2
Two phases
Six carbon phase
Three carbon phase
30

31

Summary of Glycolysis
glucose + 2ADP + 2Pi + 2NAD+

2 pyruvate + 2ATP + 2NADH + 2H+

32

Figure 8.17

The Tricarboxylic Acid Cycle

Also

called citric acid cycle and Krebs

cycle
Common in aerobic bacteria, free-living
protozoa, most algae, and fungi
Major role is as a source of carbon
skeletons for use in biosynthesis

34

35

The Respiratory Chain: Electron

Transport and Oxidative
Phosphorylation
The

final processing mill for electrons

and hydrogen ions
The major generator of ATP
A chain of special redox carriers that
receives electrons from reduced carriers
(NADH and FADH2) and passes them in a
sequential and orderly fashion from one
redox molecule to the next

Figure 8.18

Glycolysis

2 ATPs
2 NADH

Krebs Cycle
2 ATPs
8 NADH

Total net ATPs

Bacteria = 32
Eukaryotes = 30

2 FADH2
ETC

10 NADH X 2.5 = 25 ATPs

2 FADH2 X 1.5 = 3 ATPs