Biochemistry
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In photosynthesis, if photosystem II absorbs 12 photons, how many molecules of would be produced?
Explanation
Absorbing four photons by photosystem II creates one oxygen molecule, so absorbing 12 would produce 3 molecules of .
Which of these describes the protein myoglobin?
It is the primary oxygen-carrying protein of muscle tissues.
Myoglobin can bind four oxygen atoms.
Myoglobin does not contain a heme group.
Myoglobin's highest level of protein structure is quaternary.
Explanation
Myoglobin and hemoglobin are not the same molecule; their functions are similar but different in several ways. Myoglobin is an oxygen-binding protein of muscle tissues. In contrast, hemoglobin is the oxygen-transport protein found in blood. Hemoglobin can bind four oxygen atoms, while myoglobin can only bind one. Both hemoglobin and myoglobin contain heme groups, with hemoglobin containing four and myoglobin containing one. These iron-containing groups are responsible for binding the oxygen atom(s).
If an uncoupler allows for excess buildup of protons inside of the mitochondrial matrix, which of the following processes will be inhibited?
None of these will be inhibited
Pyruvate dehydrogenase complex
Electron transport chain
Glycolysis
Krebs cycle
Explanation
With the excess buildup of protons in the matrix, the only thing that will be inhibited is the generation of ATP by ATP synthase. The other processes in cellular respiration focus more on creation of high energy electron carriers, and therefore will continue as normal.
What is the role of ubiquinone in the electron transport chain?
Ubiquinone carries electrons from the first enzyme complex to the second enzyme complex
Ubiquinone carries electrons from the third enzyme complex to the fourth enzyme complex
Ubiquinone accepts electrons directly from
Ubiquinone accepts electrons directly from
Ubiquinone is the final step in which oxygen is reduced to water
Explanation
Ubiquinone functions to carry electrons in oxidative phosphorylation from the first enzyme complex to the second enzyme complex. It does not receive electrons from nor
directly.
What term is used to describe enzymes that have different chemical structures but which catalyze the same reactions?
Isozymes
Coenzymes
Apoenzymes
Holoenzymes
None of these
Explanation
The correct answer choice is isozymes, also called isoenzymes. Even though these enzymes can catalyze the same reaction, they often have differences in their kinetic parameters or in the way they're regulated. Coenzymes are a type of cofactor. They are generally complex organic molecules that are usually derived from vitamins, and they serve the purpose of assisting the enzyme to which they are bound. Examples include pyridoxal phosphate, biotin, coenzyme A, etc. Apoenzymes are enzymes that normally require a cofactor, but are in a state in which they lack that cofactor. Holoenzymes are apoenzymes that have their cofactor bound.
Amino acids are connected via bonds, which occur between the carboxyl group of one amino acid and the amino group of another.
peptide
ionic
hydrogen
double
amino
Explanation
A peptide bond connects two amino acids. This is the result of a condensation reaction (water is lost) and a new nitrogen-carbon bond forms between two amino acids. Note that amino acid synthesis occurs in the direction. Peptide bonds are covalent bonds that are responsible for the primary structure of amino acids.
Select the most accurate description of alpha-linolenic acid.
Is a precursor for eicosapentaenoic acid (EPA)
Can be synthesized de novo in the body
Is a twenty-carbon chain omega-3 fatty acid
Is a precursor for arachidonic acid (AA)
Is an eighteen-carbon chain omega-6 fatty acid
Explanation
Alpha-linolenic acid is an essential fatty acid that must be consumed in the diet (cannot be synthesized by the body). It is an eighteen-carbon omega-3 fatty acid that is used to synthesize eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA), two important long chain polyunsaturated fatty acids. Alpha-linoleic acid is the precursor to arachodonic acid (AA).
Sickle cell anemia is caused by a point mutation in hemoglobin, where a glutamate residue is changed to a valine. Based on this mutation mechanism, what level of protein structure is affected by sickle cell anemia?
Primary structure
Secondary structure
Tertiary structure
Quaternary structure
Explanation
Because an amino acid has been altered in sickle cell anemia, we can say that the amino acid sequence for hemoglobin has been changed. The amino acid sequence is defined as the primary structure for a protein, so that is the level that has been altered. It should be noted that the subsequent levels of protein structure would be altered as well, but the manipulation of the amino acid sequence is a changing of the primary structure first.
Which reaction in beta oxidation does hydroxyacyl-CoA dehydrogenase catalyze?
Oxidation of the beta hydroxyl group
Reduction of the beta hydroxyl group
Oxidation the gamma carbon
Dehydration of the beta carbon
Dehydration of the carbonyl carbon
Explanation
Hydroxyacyl-CoA dehydrogenase oxidizes the beta hydroxyl group, forming a carbonyl.

Which of the following metabolic processes directly requires oxygen?
Electron transport system
Glycolysis
Citric acid cycle
Tricarboxylic acid cycle
Pyruvate dehydrogenase complex
Explanation
The electron transport system is the only metabolic process listed that directly requires molecular oxygen. Oxygen is the final electron acceptor (it is one of the most electronegative atoms in our bodies) in the electron transport chain. This is the same as saying that oxygen has the highest reduction potential, and is capable of receiving electons. If oxygen is not present to accept the electron from the final enzyme complex in the inner mitochondrial membrane, then electron transport will be inhibited and thus no ATP will be produced via chemiosmosis.
Note that the Krebs cycle, citric acid cycle, and tricarboxylic acid cycle (TCA cycle) all refer to the same process, and do not directly require oxygen (oxygen is neither a reactant nor a product in any of the steps). However, oxygen is indirectly required, as there is no point to this cycle without subsequent oxidative phosphorylation. Thus in the absence of oxygen, of the choices shown, only glycolysis will proceed uninhibited.