test 1 ch 3 Flashcards
(57 cards)
What is the point of bioenergetics?
Cells are highly organized systems
The laws of thermodynamics explain why energy is
needed to create order in cells
Understanding energy from this perspective sets up
discussion of energy flow in biological systems,
including cell respiration and photosynthesis
first law of thermodynamics states that
- Energy cannot be created or destroyed, can only be transformed into different forms of energy
-Physical World: potential to kinetic to electrical
-Biological World: light energy(photosynthesis) to bond energy (glucose) to bond
energy (ATP) and heat
-Energy used to do work
second law of thermodynamics states that
Entropy of the universe is always
increasing
- Entropy is the tendency to disorder
- Every energy transformation results in increase in entropy.
- Energy transformations not 100% efficient. Some energy lost as heat.
-Biological example in photosynthesis
-Glucose is much more ordered than CO2 and H2O from which it is made.
-Energy (in the form of light) must be added and heat is released. Release of heat causes more disorder (increased thermal motion) in the environment.
How do cells create order in a cell?
Convert forms of energy into energy in
chemical bonds
All chemical reactions must:
-Obey laws of thermodynamics
-Result in more disorder
- No energy created or destroyed
Energetically favorable reactions result in loss in free energy, deltaG
energetically favorable reactions happen
spontaneously. These are reactions that release energy when they happen.
Because energy is released, nature loves these reactions—they just go without needing extra help.
Why are they spontaneous?
Nature prefers low-energy, stable states. If a reaction moves things toward a more stable, lower-energy state, it will happen on its own (spontaneous).
creating bonds requires
energy
standard free energy: deltaG
Intrinsic energy of a reaction
Measured at “standard” conditions
- all molecules=1 M, 25o C, pH 7.0
Negative deltaG means products of reaction have lower energy than reactants (will move to the right)
Negative deltaG means that under “standard” conditions, the reaction is thermodynamically
favorable
deltaG is
represents the amount of energy available to do work in a biological system.
free energy change
Change in free energy under non-standard conditions (e.g. in a cell)
it Depends on deltaG and concentration of products and
reactants
Negative deltaG means reaction is spontaneous at a
given condition
G= deltaG+ RT ln [products]/[reactants]
- R=gas constant, T=absolute temp
-RT at 37o C = 2.58
- Units = kJ/mole
with A and B what happens as you make more product?
As you make more product, B gets bigger and as B gets bigger it’s going to be more favorable to go back the other way.
Calculation of free energy change problem
do the problem
chemical equilibrium constant:K
Chemical equilibrium is reached
when the concentration effect just
balances the push by Go.
When the ratio of
[products]/[reactants]=K, there is
no longer any net change in the
reaction
deltaG= -5.94 log K
K=10 -deltaGº/5.94 (no units)
equilibrium
the point where push from -deltaG in one direction= the push from deltaG in the other direction
chemical equilibrium problem
do it
enzymes do what?
They lower the activation energy
enzyme function
they catalyze reactions
explain enzymes
-Usually proteins (name ends in –ase or –zyme)
-Lower the activation barrier so that an energetically favorable reaction can proceed (speeds up reaction)
-Enzymes do NOT make energetically unfavorable reactions occur.
Enzymes do NOT change deltaG or K
Enzymes do not change ΔG or K for a reaction itself. However, by speeding up reactions, they can shift the balance between reactants and products more quickly. In some cases, enzymes participate in coupled reactions, indirectly influencing the ΔG of a larger process.”
what are enzyme kinetics?
Used to measure how tightly an enzyme binds to a
substrate
To measure follow the rate of product formation (or
substrate consumption)
In lab activity:
- Enzyme: Alkaline Phosphatase
-Substrate: p-nitrophenol-phosphate (clear)
-Product: p-nitrophenol (yellow)
- Measure product formation by using a spectrophotometer to
measure amount of yellow product formed
Vmax
-is when the enzyme is working at maximal efficiency (it is the max velocity an enzyme can reach)
-Units are in velocity, change in product (or
substrate) concentration per minute (e.g. mM/min)
-The only way to increase Vmax for a particular
enzyme is to increase the amount of enzyme present (concentration).
Km
is the Michaelis constant defined as the concentration of substrate at which the enzyme is working at ½ Vmax
-Units are in concentration (e.g. mM)
-Lower Km means the enzyme binds the substrate at a lower concentration and is thus
more efficient.
Use Ek to identify type of inhibitor: competitive or noncompetitive
Competitive: Vmax does not change
Non-competitive: Km does not change
do a practice problem
Driving unfavorable reactions
Energetically unfavorable reactions occur in the cell by being coupled to an energetically favorable reaction.
Coupled Reactions
A + B⟶ C +5 kJ/mole
D + C ⟶ E -13 kJ/mole
-8 kJ/mole
- Have net negative deltaG
- A product of one reaction must be used as a reactant in the
other reaction. (“C” is used as a product in the first reaction and a reactant in the second one
Activated carriers
-Energetically unfavorable reaction coupled to
-Hydrolysis of ATP or Acetyl CoA
-Oxidation of NADH or NADPH
look at model for how activated carriers work
look at model