Bio 2100 Final Exam 2 Questions And
Actual Verified Answers (2025-2026)
Updated.
exergonic - Answer free energy of products is lower than free energy of reactants
endergonic - Answer free energy of reactants is lower than free energy of products
ways that enzymes help catalyze a reaction - Answer 1. bind to substrate and strain bonds
2. bind 2 substrates together and make orientation more advantageous for reaction
3. transiently - accept/donate protons, etc. (temporary)
rate vs. concentration relationship of enzymes - Answer lower concentrations mean lower
rates
Michaelis constant - Answer found where rate of reaction is at half of maximum velocity
how does adding a competitive inhibitor change the rate v. concentration graph? - Answer
slope is less steep, maximum velocity is same value, Michaelis constant is higher
competitive inhibitor - Answer competes with substrate for active site
how does adding non-competitive inhibitors change rate v. concentration graph? - Answer
maximum velocity is less, Michaelis constant is less
non-competitive inhibitors - Answer changes shape of enzyme
increase in entropy is favorable to exergonic/endergonic - Answer exergonic
during coupled exergonic/endergonic reactions, what is necessary in order for co-transport to
occur? - Answer exergonic reaction must be greater than endergonic
, what would happen if a living cell's metabolism reached equilibrium? - Answer it would die
saturation of enzymes - Answer all enzymes have active sites engaged
the only way to increase the rate of reaction at saturation would be...? - Answer add more
enzymes
allosteric regulation - Answer regulation of an enzyme by binding an effector molecule at a site
other than the enzyme's active site
feedback inhibition - Answer reaction pathway halted by inhibitor binded to enzyme
basic overview of cellular respiration energy flow - Answer glucose -> NADH -> electron
transport chain -> proton motive force -> ATP
reduced state to oxidized state is what in terms of free energy? - Answer exergonic
important steps of glycolysis - Answer 1. glucose gains phosphate from ATP which inhibits
movement through mitochondrial membrane
2. glucose-6-phosphate is isomerized to fructose-6-phosphate
3. 6 carbon structure is cleaved into two 3-carbon units
4. one unit is rearranged so it's in proper arrangement like the other
5. NAD+ reduced to NADH (drop in free energy and first step of payoff phase)
6. phosphates added to make 2 ATPs (most of final energy is in pyruvate)
draw electron transport chain/chemiosmosis - Answer
anaerobic cellular respiration - Answer final electron acceptor is replaced with sulfate/nitrate
fermentation - Answer organic final electron acceptor, regenerates NAD+ for glycolysis
relationship between pyruvate and lactic acid - Answer pyruvate reduces to lactic acid
Actual Verified Answers (2025-2026)
Updated.
exergonic - Answer free energy of products is lower than free energy of reactants
endergonic - Answer free energy of reactants is lower than free energy of products
ways that enzymes help catalyze a reaction - Answer 1. bind to substrate and strain bonds
2. bind 2 substrates together and make orientation more advantageous for reaction
3. transiently - accept/donate protons, etc. (temporary)
rate vs. concentration relationship of enzymes - Answer lower concentrations mean lower
rates
Michaelis constant - Answer found where rate of reaction is at half of maximum velocity
how does adding a competitive inhibitor change the rate v. concentration graph? - Answer
slope is less steep, maximum velocity is same value, Michaelis constant is higher
competitive inhibitor - Answer competes with substrate for active site
how does adding non-competitive inhibitors change rate v. concentration graph? - Answer
maximum velocity is less, Michaelis constant is less
non-competitive inhibitors - Answer changes shape of enzyme
increase in entropy is favorable to exergonic/endergonic - Answer exergonic
during coupled exergonic/endergonic reactions, what is necessary in order for co-transport to
occur? - Answer exergonic reaction must be greater than endergonic
, what would happen if a living cell's metabolism reached equilibrium? - Answer it would die
saturation of enzymes - Answer all enzymes have active sites engaged
the only way to increase the rate of reaction at saturation would be...? - Answer add more
enzymes
allosteric regulation - Answer regulation of an enzyme by binding an effector molecule at a site
other than the enzyme's active site
feedback inhibition - Answer reaction pathway halted by inhibitor binded to enzyme
basic overview of cellular respiration energy flow - Answer glucose -> NADH -> electron
transport chain -> proton motive force -> ATP
reduced state to oxidized state is what in terms of free energy? - Answer exergonic
important steps of glycolysis - Answer 1. glucose gains phosphate from ATP which inhibits
movement through mitochondrial membrane
2. glucose-6-phosphate is isomerized to fructose-6-phosphate
3. 6 carbon structure is cleaved into two 3-carbon units
4. one unit is rearranged so it's in proper arrangement like the other
5. NAD+ reduced to NADH (drop in free energy and first step of payoff phase)
6. phosphates added to make 2 ATPs (most of final energy is in pyruvate)
draw electron transport chain/chemiosmosis - Answer
anaerobic cellular respiration - Answer final electron acceptor is replaced with sulfate/nitrate
fermentation - Answer organic final electron acceptor, regenerates NAD+ for glycolysis
relationship between pyruvate and lactic acid - Answer pyruvate reduces to lactic acid
