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Cell structure
1. Prokaryotes
Small
Unicellular
No membrane-bounded nucleus
No organelles
Include Bacteria & Archaebacteria
2. Eukaryotes
Large
Unicellular or multicellular
Membrane-bounded nucleus
Many organelles, some resembling prokaryotic cells
Animal cells: no cell wall (plants and fungi have cell walls made of
cellulose)
3. Organelles
Organelles in detail:
Advantages of compartmentation:
Enclosed system can maintain local concentrations of compounds
that would diffuse otherwise
Concentrated substances can react more readily, leading to
increased efficiency for many chemical reactions
Endocytosis (Phagocytosis)
1. Lipid Bilayer
Temperature
higher temp increases mobility
2. Membrane Proteins
Peripheral proteins:
Are embedded within the membrane and extend outward on one
side only
Integral proteins:
Extended through the entire bilayer
Permeability
Membrane Transport
Active Transport
c) pumps (Sodium-Potassium Pump)
move against concentration gradient (low concentr. to high
concentr.)
a) Channels
b) Transport Proteins
c) Pumps
For specific types of solutes
Solute move up concentration gradient
Transport is one-way only
Cell must spend energy (ATP reaction): the energetically favorable
ATP reaction drags along unfavorable transport reaction (active
transport)
Bioenergetics
1. Energy
1. Law of Thermodynamics
Enthalpy:
potential energy measured as heat
Entropy (S)
a measure of disorder or randomness (technically, a measure of how
dispersed the heat is
left picture: high order, low entropy
right picture: low order, high entropy
A reaction tends to proceed if the products are more disordered than the
reactants (if entropy increases)
G = H TS
4. Metabolic Reactions
All cells must obtain raw materials (Carbon source, Nitrogen, metals
etc)
All cells must find a source of free energy (sunlight, chemical
energy)
1. What Enzymes Do
When reactants react, old bonds must break so that new bonds can be
formed. This requires input of energy (activation energy)
The reacting molecules represent a range of energy levels. Relatively few
molecules randomly achieve the higher energy level necessary for them to
react
Thus, few molecules react per unit time (rate of reaction is slow)
If catalyst is present to help break old bonds and form new bonds, then
the reactants need less energy in order to react (activation energy is lower)
Relatively more reactant molecules have the required energy to react, so
the rate of the reaction is higher
Enzyme provides alternate chemical environment for the reaction
Enzymes are proteins and therefore are sensitive to agents that alter protein
structure:
pH
Temperature
Salt concentration
3. Enzyme Regulation
Most enzymes are regulated. Cells can turn enzyme activity up or down
by
Making more enzyme molecules or fewer enzyme molecules
Competitive inhibitors to block enzyme activity
Allosteric regulators to block enzyme activity (noncompetitive)
Allosteric regulators to increase enzyme activity
Monosaccharides, amino acids, and fatty acids are all broken down
to 2-carbon fragments (acetyl-CoA)
The citric acid cycle converts acetyl groups to 2 CO2
The chemical energy of the original fuel molecule is eventually
converted to the chemical energy ATP
Stages of Catabolism
1. Polymer monomer
2. Glycolisis (or fatty acid oxidation, amino acid catabolism)
3. Citric acid cycle
4. Electron transport/oxidative phosphorylation
Picture explained:
Stage 1: Catabolism begins with digestion (hydrolysis of carbs, fats,
proteins)
Stage 2 : Molecules are converted to acetyl CoA
Stage 3 and 4: Acetyl CoA enters citric acid cycle and produces reduced
coenzymes
whose energy is stored in ATP
3. Glycolysis
Glycolysis steps:
Step 1:
Phosphorylation of glucose to glucose-6-phosphate
Reaction is unfavorable, thus is coupled with the hydrolysis of ATP to
ADP
Step 2:
Isomerization of glucose-6-phosphate to fructose 6-phosphate
Step 3:
Phosphorylation (energy-absorbing rxn), driven by ATP hydrolysis to
form fructose 1,6-biphosphate
Step 4:
Cleavage of 6-carbon chain to form two 3-C products (constitutional
isomers)
Steps 5:
Isomerization to glyceraldehyde 3-phosphate
Step 6:
Oxidation and Phosphorylation: Oxidizing agent NAD+ is reduced to
NADH
Step 7:
ATP is formed
Three major products are formed in glycolysis: ATP, NADH, and pyruvate
4. Fermentation
8 enzyme-catalyzed steps
Entire pathway acts as catalyst
Based in mitochondria
Acetyl groups of acetyl-CoA are oxidized to carbon dioxide
Cycle begins when 2 C of acetyl CoA react with 4 C substrate to form
Citrate
Two carbons are removed to form 2 molecules of CO2 (Step 3,4)
4 molecules of reduced coenzymes NADH and FADH2 are formed
(Steps 3,4,5)
These molecules serve as carrier of electrons to electron transport
chain
One mole of GTP is synthesized (step 5)
By step 4 2 Carbons are lost as CO2 and 2 molecules of NADH are
formed
Net results:
2 molecules of CO2
4 molecules of reduced coenzymes (3 NADH and 1 FADH2)
1 molecule of GTP
Main function of citric acid cycle:
To produce reduced coenzymes that enter the electron transport chain and
ultimately produce ATP
Glucose becomes oxidized, NAD and FAD become reduced to NADH and
FADH2
Reoxidation of NADH and FADH2 drives more ATP production by an
oxygen-dependent process called oxidative phosphorylation
4. ATP Synthase
The flow of H+ ions down their gradient through ATP synthase powers
the synthesis of ATP from ADP + P
Protons hitching a ride on ATP synthase trigger conformational changes
in protein
As ATP synthase changes shape, it binds ATP and P, and then releases
ATP
ATP synthesis is an uphill reaction
It is oxidative phosphorylation because it depends on the energy of
redox reactions
Muscles:
1. Carbohydrate Metabolism
a) Gluconeogenesis
Starting materials: lactate, some amino acids, glycerol (no fatty
acids)
Pyruvate glucose pathway requires 6 ATP
Only liver and kidneys can do this, then glucose travels in blood to
other tissues
Anabolic pathway; synthesizes glucose from pyruvate
Happens when body used all glycogen and glucose (starvation,
fasting)
b) Glycogen synthesis
Condensation reaction is uphill, so glucose is first activated by
reacting UTP
Additional enzymes are needed to deal with branch points
Ultimately, the process costs 2 ATP equivalents (2 bonds to
phosphate groups are broken)
2. Lipid Metabolism
a) Glycerol metabolism
Triacylglycerol catabolism begins with hydrolysis
Glycerol backbone can be converted to glycolytic intermediate
Glycerol therefore yields acetyl-CoA or glucose
b) beta Oxidation
Fatty acids come from triacylglycerol or membrane lipid breakdown
Fatty acid is first activated by reaction with ATP and linked
Coenzyme A
Beta Oxidation pathway yields acetyl-CoA, NADH, FADH2
Acetyl-CoA enters citric acid cycle, reduced cofactors go to electron
transport chain
Result: A lot of ATP
c) FattyAcid Sythesis
Fatty acid chain is built from acetyl-CoA molecules
2 C are added at a time, to the tioester (CoA) end
Reactions are similar to beta oxidation, but in synthesis NADPH is
oxidized to NADP
Fatty acids are then linked to glycerol to form triacylglycerol
Liver and adipose tissue are the main sites of fatty acid synthesis
and storage
d) Ketone Bodies
When glucose (and glycogen) have been depleted, body uses
stored fat as fuel and liver makes glucose form glycerol and
amino acids
Brain requires constant supply of glucose and does not use fatty
acid fuels
To avoid breaking down bodys proteins for gluconeogenesis,
liver converts fatty acids to ketone bodies
Ketogenesis also occurs in other situations where glucose is in
short supply