Carbon Compounds in Cells

Chapter 3
 Importance of Carbon

Carbon permeates the world of life—

from the energy-requiring activities and
structural organization of cells, to
physical and chemical conditions that
span the globe and influence
ecosystems everywhere.
Humans and Global Warming
• Fossil fuels are rich in carbon

• Use of fossil fuels releases CO2 into

atmosphere

• Increased CO2 may contribute to global

warming
Organic Compounds
Hydrogen and other elements
covalently bonded to carbon

Carbohydrates
Lipids
Proteins
Nucleic Acids
 Carbon’s Bonding Behavior
• Outer shell of
carbon has 4
electrons; can
hold 8

• Each carbon atom

can form covalent
bonds with up to 4
atoms
Methane: Simplest Organic
Compound
H
Ball-and-stick
H C H model
H

Structural formula

Space-filling
model

Figure 3.2
Page 36
 Bonding Arrangements
• Carbon atoms can
form chains or rings

• Other atoms project

from the carbon
backbone Glucose
(ball-and-stick model)

In-text figure
Page 36
Hemoglobin Molecular Models

Ball-and-stick model Space-filling model

Figure 3.3
Ribbon model Page 37
 Functional Groups
• Atoms or clusters of atoms that are
covalently bonded to carbon backbone

• Give organic compounds their different

properties
 Examples of Functional
Groups
Methyl group - CH3
Hydroxyl group - OH
Amino group - NH3+
Carboxyl group - COOH
Phosphate group - PO3-
Sulfhydryl group - SH
Types of Reactions

Functional group transfer

Electron transfer
Rearrangement
Condensation
Cleavage
 Condensation Reactions
• Form polymers from subunits

• Enzymes remove -OH from one

molecule, H from another, form bond
between two molecules

• Discarded atoms can join to form water

Condensation

enzyme action at functional groups

enzyme action at functional groups

Figure 3.7a
Page 39
 Hydrolysis
• A type of cleavage reaction
• Breaks polymers into smaller units
• Enzymes split molecules into two or
more parts
• An -OH group and an H atom derived
from water are attached at exposed
sites
 Hydrolysis

enzyme action at functional groups

Figure 3.7b
Page 39
 Carbohydrates
Monosaccharides
(simple sugars)

Oligosaccharides
(short-chain carbohydrates)

Polysaccharides
(complex carbohydrates)
 Monosaccharides
• Simplest
carbohydrates
• Most are sweet
tasting, water
soluble
• Most have 5- or 6-
carbon backbone

Structure of glucose
 Disaccharides
glucose fructose
• Type of
oligosaccharide
• Two
monosaccharides
covalently bonded + H2O

• Formed by
sucrose
condensation reaction

Figure 3.8b
Page 40
 Polysaccharides
• Straight or
branched chains
of many sugar
monomers
• Most common are
composed entirely
of glucose
Starch chain
Figure 3.9
Page 40
 Cellulose & Starch
• Differences in bonding patterns between
monomers yield different properties

amylose (a starch)
cellulose

Figure 3.10
Page 41
 Glycogen
• Sugar storage form in animals
• Large stores in muscle and liver cells

Figure 3.10
Page 41
 Chitin
• Polysaccharide
• Nitrogen-containing groups attached to
glucose monomers
• Structural material for hard parts of
invertebrates, cell walls of many fungi
 Lipids
• Most include fatty acids
– Fats
– Phospholipids
– Waxes
• Sterols and their derivatives have no
fatty acids
• Tend to be insoluble in water
 Fatty Acids
• Carboxyl group at
one end
• Carbon backbone
• Saturated or
unsaturated

stearic acid oleic acid linolenic

Figure 3.12
acid
Page 42
 Fats
• Fatty acid(s)
attached to glycerol
• Triglycerides are
most common

Figure 3.13
Page 42
 Phospholipids

• Main component of
cell membranes
• Hydrophobic head
• Hydrophilic tails

Fig. 3.14a,b
Page 43
 Sterols and Derivatives
• No fatty acids
• Rigid backbone of
four fused-together
Cholesterol
carbon rings
• Cholesterol - most
common type in
animals
Figure 3.15a
In-text p43
 Waxes

• Long-chain fatty acids linked to

long-chain alcohols or carbon
rings

• Firm consistency, repel water

• Important in water-proofing
 Amino Acid Structure

Carboxyl
group
Amino
group R group

Figure 3.16 tryptophan

Page 44 (trp)
Figure 3.17
Page 44
 Protein Synthesis
• Peptide bond
– Condensation reaction links amino group of
one amino acid with carboxyl group of next

Water forms as a by-product

Fig. 3.18a
Page 45
 Primary Structure
• Sequence of amino acids
• Unique for each protein
• Two linked amino acids = dipeptide
• Three or more = polypeptide
• Backbone of polypeptide has N atoms:
-N-C-C-N-C-C-N-C-C-N-
 Second and Third Levels
• Hydrogen bonding
produces helix or
sheet
• Domain formation

Tertiary structure

Secondary Figure 3.19a

structure Page 46
 Fourth Level Structure
Some proteins
are made up of
more than one
polypeptide
chain

Figure 3.20 HLA-A2 quaternary structure

Page 47
 Hemoglobin
alpha chain beta chain

beta chain alpha chain

 One Wrong Amino Acid
• Single amino acid change in beta chain
can cause sickle-cell anemia

HbS

valine histidine leucine proline threonine valine glutamate

Fig. 3.21c,d
Page 48
 Sickle Cell Anemia
• Caused by two mutated copies (HbS) of
Hb gene
• Low oxygen causes red blood cells to
clump
• Clumping prevents normal blood flow
• Over time, may damage tissues and
organs throughout the body
 Nucleotide Structure

• Sugar
ATP
• At least one
phosphate group
• Nitrogen-
containing base

Figure 3.23a
Page 50
Nucleotide Functions
• Energy carriers
• Coenzymes
• Chemical messengers

• Building blocks for

nucleic acids
 DNA
• Double-stranded
• Sugar-phosphate
backbone
• Covalent bonds in
backbone
• H bonds between
bases

Figure 3.25
Page 51
 RNA
• Usually single strands
• Four types of nucleotides
• Unlike DNA, contains the base uracil in
place of thymine
• Three types are key players in protein
synthesis