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PowerPoint® Lecture

Presentations prepared by
Mindy Miller-Kittrell,
North Carolina State
University

CHAPTER 2
The
Chemistry of
Microbiology

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Atoms

• Matter—anything that takes up space and


has mass
• Atoms—the smallest chemical units of matter

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Atoms

• Atomic Structure
• Electrons—negatively charged subatomic particles
circling a nucleus
• Nucleus—structure containing neutrons and protons
• Neutrons—uncharged particles
• Protons—positively charged particles

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Atoms

• Atomic Structure
• Element—composed of a single type of atom
• Atomic number—equal to the number of protons in the
nucleus
• Atomic mass (atomic weight)—sum of masses of
protons, neutrons, and electrons

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Atoms

• Isotopes
• Atoms of a given element that differ in the number of
neutrons in their nuclei
• Stable isotopes
• Unstable isotopes
• Radioactive isotopes
• Release energy during radioactive decay

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Atoms

• Electron Configurations
• Only the electrons of atoms interact, so they determine
atom’s chemical behavior.
• Electrons occupy electron shells.
• Valence electrons—electrons in outermost shell that
interact with other atoms

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Chemical Bonds

• Valence—combining capacity of an atom


• Positive if atom has electrons to give up
• Negative if atom has spaces to fill
• Stable when outer electron shells contain eight
electrons
• Chemical bonds—atoms combine by sharing or
transferring valence electrons
• Molecule—two or more atoms held together by
chemical bonds
• Compound—a molecule composed of more than
one element

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Chemical Bonds

• Covalent bond—sharing of a pair of electrons by


two atoms
• Electronegativity—attraction of atom for
electrons
• The more electronegative an atom, the greater the pull
its nucleus exerts on electrons.

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Chemical Bonds

• Nonpolar Covalent Bonds


• Shared electrons spend equal amounts of time around
each nucleus.
• Atoms with similar electronegativities
• No poles exist.
• Carbon atoms form four nonpolar covalent bonds with
other atoms.
• Organic compounds contain carbon and hydrogen atoms.

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Chemical Bonds

• Polar Covalent Bonds


• Unequal sharing of electrons due to significantly
different electronegativities
• Most important polar covalent bonds involve hydrogen.
• Allow for hydrogen bonding

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Chemical Bonds

• Ionic Bonds
• Occur when two atoms with vastly different
electronegativities come together
• Atoms have either positive (cation) or negative (anion)
charges.
• Cations and anions attract each other and form ionic
bonds (no electrons shared).
• Typically form crystalline ionic compounds known
as salts

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Chemical Bonds

• Hydrogen Bonds
• Electrical attraction between partially charged H+ and full
or partial negative charge on same or different molecule
• Weaker than covalent bonds but essential for life
• Help to stabilize 3-D shapes of large molecules

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Table 2.2 Characteristics of Chemical Bonds

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Chemical Reactions

• The making or breaking of chemical bonds


• Involve reactants and products
• Biochemistry involves chemical reactions of
living things.

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Chemical Reactions

• Synthesis Reactions
• Involve the formation of larger, more complex
molecules
• Require energy (endothermic)
• Common type is dehydration synthesis
• Water molecule formed
• All the synthesis reactions in an organism are
called anabolism.

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Figure 2.11a Two types of chemical reactions in living things.

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Chemical Reactions

• Decomposition Reactions
• Break bonds within larger molecules to form smaller
atoms, ions, and molecules
• Release energy (exothermic)
• Common type is hydrolysis
• Ionic components of water are added to products.
• All the decomposition reactions in an organism are
called catabolism.

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Figure 2.11b Two types of chemical reactions in living things.

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Water, Acids, Bases, and Salts

• Water
• Most abundant substance in organisms
• Many special characteristics due to two polar
covalent bonds:
• Cohesive molecules—generate surface tension
• Excellent solvent
• Remains liquid across wide range of temperatures
• Can absorb significant amounts of heat energy
without changing temperature
• Participates in many chemical reactions

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Water, Acids, Bases, and Salts

• Acids and Bases


• Dissociated by water into component cations and
anions
• Acid—dissociates into one or more H+ and one or
more anions
• Base—binds with H+ when dissolved in water; some
dissociate into cations and OH–
• Concentration of H+ in solution expressed using the
pH scale

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Figure 2.13 Acids and bases.

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Figure 2.14 The pH scale.

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Organic Macromolecules

• Functional Groups
• Contain carbon and hydrogen atoms
• Atoms often appear in arrangements called
functional groups.
• Macromolecules—large molecules used by all
organisms:
• Lipids
• Carbohydrates
• Proteins
• Nucleic acids
• Monomers—basic building blocks of
macromolecules

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Table 2.3 Functional Groups of Organic Molecules and Some Classes of
Compounds in Which They Are Found

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Organic Macromolecules

• Lipids
• Not composed of regular subunits
• Are all hydrophobic
• Four groups:
• Fats (triglycerides)
• Phospholipids
• Waxes
• Steroids

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Figure 2.15 Fats (triglycerides).

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Figure 2.16 Phospholipids.

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Organic Macromolecules

• Lipids
• Waxes
• Contain one long-chain fatty acid covalently linked to
long-chain alcohol by an ester bond
• Lack hydrophilic head
• Completely insoluble in water

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Figure 2.17 Steroids.

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Organic Macromolecules

• Carbohydrates
• Organic molecules composed of carbon, hydrogen,
and oxygen (CH2O)n
• Functions:
• Long-term storage of chemical energy
• Ready energy source
• Part of backbones of nucleic acids
• Converted to amino acids
• Form cell wall
• Involved in intracellular interactions between
animal cells

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Organic Macromolecules

• Carbohydrates
• Types:
• Monosaccharides
• Disaccharides
• Polysaccharides

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Figure 2.18 Monosaccharides (simple sugars).

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Figure 2.19 Disaccharides.

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Figure 2.20 Polysaccharides.

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Organic Macromolecules

• Proteins
• Composed mostly of carbon, hydrogen, oxygen,
nitrogen, and sulfur
• Functions:
• Structure
• Enzymatic catalysis
• Regulation
• Transportation
• Defense and offense

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Organic Macromolecules

• Proteins
• Amino acids
• The monomers that make up proteins
• Most organisms use only 21 amino acids in protein
synthesis.
• Side groups affect how amino acids interact with one
another and how a protein interacts with other
molecules.
• A covalent peptide bond is formed between
amino acids.

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Figure 2.21 Amino acids.

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Figure 2.23 The linkage of amino acids by peptide bonds via a dehydration
reaction.

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Figure 2.24 Levels of protein structure.

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Organic Macromolecules

• Nucleotides and Nucleic Acids


• Deoxyribonucleic acid (DNA) and ribonucleic
acid (RNA) are the vital genetic material of cells
and viruses.
• RNA also acts as enzyme, binds amino acids, and
helps form polypeptides.

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Organic Macromolecules

• Nucleotides and Nucleic Acids


• Nucleotides and nucleosides
• Nucleotides
• Monomers that make up nucleic acids
• Composed of three parts:
• Phosphate
• Pentose sugar—either deoxyribose or ribose
• One of five cyclic nitrogenous bases
• Nucleosides are nucleotides lacking phosphate.

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Figure 2.25 Nucleotides.

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Organic Macromolecules

• Nucleic Acids
• Nucleic acid structure
• Three H bonds form between C and G.
• Two H bonds form between T and A (DNA) or U and A
(RNA).
• DNA is double stranded in most cells and viruses.
• The two strands are complementary.
• The two strands are antiparallel.

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Figure 2.26 General nucleic acid structure.

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Table 2.5 Comparison of Nucleic Acids

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Figure 2.27 ATP.

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