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Lecture

BIOL 201 Lecture 1-25.doc


Department
Biology
Course Code
BIOL 201
Professor
Gary Brouhard

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Lecture 1
Major Energy source for E.Coli is glucose.
preferentially uses glucose as its main carbon source
extracts energy and combines with inorganic compounds to carry out functions
for cellular growth and division
uses these building blocks to convert into AA, nt, lipids, sugars, vitamins,
macromolecules (DNA,RNA,proteins, polysaccharides)
Metabolism:
several pathways that use small fundamental components to build larger
macromolecules required for cellular processes
uses same macromolecules to break down and provide energy
governed by specific enzymes
Glucose>pyruvate and small molecules>
exergonic (catabolic) reaction producing ATP
uses ATP to build important components (Anabolic)
Energy
ability to carry out mechanical work
active transport of small molecules and ions
generate macromolecules and building blocks
Energy: Ability to do work
kinetic and potential
potential:
ochemical bonds
oconcentration gradients
ocharge separations across membranes
energy can be converted from one form to another
All chemical reactions are reversible
Equilibrium: rate forwards = rate reverse

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k_1[A][B] = k_2[C][D]
products/reactants = k1/k2 = k_eq
Free energy or G
Reaction proceeds only if ∆G<0
∆G>0, reaction from right to left
∆G = 0 , equilibrium
Standard free energy
∆Gº < 0 ; exergonic (energy releasing)
∆Gº > 0 ; endergonic (energy consuming)
∆Gº (from A to B) = -∆Gº (From B to A)
∆Gº (A to C) = ∆Gº (A to B) + ∆Gº (B to C)
Lecture 2 Metabolism II
Rate of reaction depends on reactants involved
so we must know characteristics of reactants
As reaction proceeds, concentrations of A decreases as concentratoin of B is formed
Catalysis
changes energy required to form a critical transition state
transition state of any chem reaction is when reactants come together in
favorable manner to drive the reaction to form products
enzymes or any catalysts decreases the amount of free energy to achieve
transition state between reactants
Enzymes
specific catalysts for bio reactions
act by binding to reactant(s) [substrates] in a way that reduces the energy
required to reach transtition state
enzymes affect only the rates of reaction-
oother properties (e.g. Keq and ∆G emain the same)
by forming binding pocket, substrate can interact with its enzyme
oenzyme substrate complex… we can achieve products with much less
energy input

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owe favor the formation of products
E + S<--> ES --> E + P
Rates of enzymatically catalyzed rxns approach a maximal velocity as substrate
concentration increases
i.e. any enzyme has a specific maximum velocity/capacity to form products
Vmax
Vmax is dependent on amount of enzyme in solution-so Vmax doesn't tell us
much
BUT the HALF-MAX value (i.e. Vmax/2), we have a value at which the
enzyme produces at half its maximal velocity
the HALF MAX value (Km - Michaelis constant) is a characteristic of the
enzyme
describes the affinity of the enzyme for the substrate
If we plot enzyme activity on Lineweaver-Burk plot
double reciprocal plot
y intercept = 1/Vmax
x intercept = -1/Km
slope = Km/Vmax
Energy from breakdown of food into smaller molecules is captured b coupling
specific rxns to ATP synth and through the process of OXIDATIVE
PHOSPHORYLATION
ATP generated in cell is used for many processes (i.e. mechanical)
Lecture 4 - Photosynthesis
Photosynthetic organisms (Phototrophs) capture light energy and use it to:
transfer H atoms from water to acceptor molecules
form molecular oxygen
synth ATP from ADP and P
transfer H atoms from acceptor to carbons derived from CO2 to form glucose
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