Download How many molecules of adenosine triphosphate (ATP) can be

How many molecules of adenosine triphosphate (ATP) can be synthesized from the complete oxidation of
one molecule of glucose to CO2 and H2O? State how many of these ATP molecules were synthesized as a
result of glycolysis, the citric acid cycle, or reactions linking glycolysis and the citric acid cycle. State what
form the energy was in for the synthesis of the ATP molecules. In other words, break down how many ATP
(or GTP), NADH and FADH2 molecules were synthesized as a result of glycolysis, the citric acid cycle, or
reactions linking glycolysis and the citric acid cycle and how the final number of ATP molecules was
calculated.
Although the enzymes pyruvate dehydrogenase and glyceraldehyde 3-phosphate dehydrogenase both use
NAD+ as a substrate, they do not compete for the same NAD+ molecules in a cell. Explain why this is the
case.
Coordination between glycolysis and gluconeogenesis is illustrated by the Cori cycle. Explain the Cori cycle
and the metabolic benefit of the Cori cycle to humans.
A significant percentage of our population has diabetes, a result of defective insulin synthesis in the
pancreas. Describe some clinical symptoms you would expect the person to have and give the
biochemical basis for your prediction of those symptoms.
Vitamin deficiencies can have a profound effect on metabolism. Name two enzymes of the TCA cycle that
would be affected by a deficiency of niacin. How about thiamine? Why?
What is the only enzyme of the citric acid cycle that is membrane-bound? Describe where the enzyme is
with respect to what membrane. Why is it important that this enzyme is membrane-bound?
Glycogen synthesis and degradation are reciprocally regulated. Explain what is meant by reciprocal
regulation and give a specific example illustrating reciprocal regulation of glycogen synthesis and
degradation.
Describe the clinical symptoms you would expect to find in someone with a liver glycogen phosphorylase
deficiency. What symptoms would you expect such an individual to exhibit? Explain using your
biochemical knowledge of glycogen phosphorylase.
Anaerobic metabolism of glucose produces lactate in actively contracting muscle tissue. What is the fate of
lactate? Explain how the fate of lactate is beneficial to our bodies.
Describe how, when, and why a germinating seed utilizes the glyoxylate cycle.
Describe three general strategies a cell uses to regulate, or control, the activity of enzymes. Then describe
in detail a specific example for each of the general strategies you listed that comes from glycolysis or the
citric acid cycle.
We discussed in class two enzymes with similar names, phosphofructokinase-1 and phosphofructokinase-2.
We also discussed two molecules with similar names, fructose 1,6-bisphosphate and fructose 2,6bisphosphate. Explain the function of these two enzymes and these two molecules in glycolysis.
The quinone portion of ubiquinone (coenzyme Q) undergoes oxidation and reduction in oxidative
phosphorylation. The isoprenoid portion of coenzyme Q remains unchanged. What is the function of the
isoprenoid chain? What would you predict would happen to coenzyme Q and metabolism if the
isoprenoid chain was absent?
What is the enzyme that is responsible for the production of the bulk of adenosine triphosphate (ATP) in
eukaryotic cells? Describe briefly where this enzyme is located, the structural features of the protein,
and the process whereby ATP is synthesized.
How many ATP are synthesized from the electrons from one NADH molecule donating its pair of electrons
to oxidative phosphorylation in the mitochondrial matrix? How many ATP are synthesized from the
electrons from one FADH2 molecule donating its pair of electrons to oxidative phosphorylation in the
mitochondrial matrix? Using your knowledge of electron transport and oxidative phosphorylation,
explain the biochemical rationale for your answers.
What property of FADH2 prevents it from transferring its electrons to complex I of the electron transport
chain?
List molecules, coenzymes, and ions that serve as electron carriers in cellular oxidation-reduction reactions.
Name enzymes that use these molecules, coenzymes, and ions in catalysis.
What prosthetic group do cytochromes contain? What role do the prosthetic groups play in metabolism?
Which of the protein components of the electron transport chain is not a proton pump?
The transfer of electrons from NADH to molecular oxygen through the respiratory chain yields energy. How
is the energy conserved? What energy-rich molecule is synthesized as a result of oxidative
phosphorylation? What enzyme synthesizes this energy-rich molecule?
What amino acid(s) are critical for coordination of iron atoms in iron-sulfur complexes of electron transfer
proteins.
What is the role of ubiquinone (Coenzyme Q)? How does the structure of ubiquinone help it fulfill its
function?
What is the role of each of the following in electron transfer?
flavin nucleotides
cytochrome c
copper
heme
iron
oxygen
Describe the structure of ATP synthase. What is the source of energy for ATP synthesis by ATP synthase
Describe the role of complex I, II, III, and IV in oxidative phosphorylation.
Follow the overall flow of electrons from NADH and from sucinate. How many protons are pumped in each
case and how many ATP can be synthesized from the protons pumped?
Where in a eukaryotic cell are the proteins of oxidative phosphorylation located?
What is the role of proteases in metabolism?