Bio 214 Lab
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the major energy producing process in eukaryotic cells
structure of mitochondria
- outer membrane
- folded inner membrane
- fluid-filled compartments
houses the many enzymes essential to the chemical rxns of respiration
with FAD what rxn does succinate dehydrogenase catalyze?
Succinate to Fumerate
flavin adenine dinucleotide
where are succinate dehydrogenase and coenzyme FAD located?
tightly bound to inner membrane of mitochondria
What does FAD do to succinate in the electron transport chain
- removes 2 hydrogens/electrons
- transfers to coenzyme Q
- go to ATP
what is used to visualize and measure the rate of succinate dehydrogenase/FAD rxn?
artificial electron acceptor
what happens when DCIP changes from blue to colorless?
it accepts electrons from E-FADH2
what is the product of succinate dehydrogenase/FAD rxn?
What needs to happen for the DCIP to successfully compete for the electrons from E-FADH2?
- normal pathway of electrons is blocked by sodium azide in electron transport chain
- blocks the final transfer of cytochrome a3 -> O2
poison used to block electrons
what are we measuring in the succinate dehydrogenase/FAD rxn
the decrease of oxidized DCIP(blue) to colorless absorbance at 600nm over 35 minutes
The kinetics related to succinate dehydrogenase/FAD rxn
explain Michaelis-Menton Kinetics
Velocity of rxn increases proportionally to an increase in enzyme concentration
all factors constant
what suspension will we be using for enzyme(succinate dehydrogenase) concentrations
slope of the Michaelis-Menton kinetics graph
Absorbance v Time graph
additional enzyme concentration/competitive inhibitor test for succinate
a structure that is similar to the substrate
competes for binding to active site on enzyme
a liquid; floating on the surface above a sediment or precipitate
where is the mitochondria found after the 1st centrifuge
where is mitochondria found after the second centrifuge
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