Facilitated diffusion acts independently of the level of intracellular ATP. Therefore, a change in ATP concentration will not affect the rate of facilitated diffusion.

If the Hill coefficient of the Hill plot is equal to 1, then binding is non-cooperative. If the Hill coefficient is greater than 1, binding is positively cooperative; if less than 1, binding is negatively cooperative. The Hill plot does not make any conclusions about the rate of a reaction, which involves Michaelis-Menten kinetics. 

To answer this question, we need to understand what enzyme efficiency is and how it's calculated.

Enzyme efficiency refers to how much substrate a given enzyme can convert into product for a given amount of substrate. In other words, an enzyme that is very efficient can convert substrate into product very quickly, even when there is not very much of that substrate around.

To calculate an enzyme's efficiency, we need to take into account these two factors by considering the variables they are associated with.

The  for a given enzyme represents the "turnover number." This value is a rate constant that is unique to a particular enzyme at a certain temperature (generally under physiological conditions). This rate constant refers to the maximum amount of substrate that an enzyme can convert into product in a given amount of time. Or, put another way, the rate constant gives the maximum reaction rate for a particular enzyme when that enzyme is completely saturated with substrate.

On the other hand, the  of an enzyme tells us the amount of substrate that needs to be present in order for the reaction rate to be at exactly half of its maximal value. This is almost the same as saying how much attraction a given enzyme has for its substrate. In fact, under certain conditions, we can use the  of an enzyme as an accurate measure of the affinity that the enzyme has for its substrate.

Relating these two values back to enzyme efficiency, we can calculate its value by taking the ratio of the two. In other words,

So, the greater the  and the lower the , the greater the enzyme's efficiency will be.

From the answer choices shown, we can see that the ratio is greatest for the enzyme that has a  of  and a  of , which gives an efficiency value of .

Where  is Faraday's constant ,  is the charge of a chloride ion, which is , and  is  or . Be sure to keep units consistent.

This question is asking us to identify a coenzyme that functions by transferring one-carbon groups. So let's take a look at each answer choice to determine what it does.

Nicotinamide Adenine Dinucleotide () and Flavin Adenine Dinucleotide () both function as carriers of high-energy electrons. Both of these coenzymes are heavily involved in taking high-energy electrons from various compounds as they are broken down during catabolic reactions. Once collected, these coenzymes deposit their high-energy electrons into the electron transport chain, allowing for a great deal of ATP to be generated for energy.

Pyridoxal Phosphate () is a coenzyme that is primarily involved in transamination reactions. These are reactions that take an amino group from amino acids, and transfer that amino group to an alpha-keto acid, converting it into an amino acid in the process. Thus, this coenzyme transfers amino groups.

Thiamine Pyrophosphate () is a coenzyme responsible for transferring two-carbon groups. For instance,  serves as a coenzyme for the pyruvate dehydrogenase complex, which is responsible for converting pyruvate into acetyl-CoA.

Finally, S-Adenosyl Methionine () is a coenzyme mainly responsible for transferring one-carbon groups in their most reduced form, as methyl groups. As the most potent methyl group donor in biological systems,  functions as a coenzyme for many methyltransferase enzymes.

Ornithine transcarbamylase catalyzes the reaction between the substrates ornithine and carbamoyl phosphate to form citrulline and phosphate. This process occurs primarily in the hepatic mitochondria, and to a lesser extent in the mitochondria of the renal cells.

Lesch-Nyhan syndrome is an x-linked deficiency of the enzyme hypoxanthine-guanine phosphoribosyltransferase (HGPRT). HGPRT plays a central role in the generation of purine nucleotides through the purine salvage pathway. Cell breakdown products cannot be reused, and are therefore degraded. This gives rise to increased uric acid, a purine breakdown product. This build-up of uric acid is associated with severe gout and kidney problems, poor muscle control and mental retardation, usually in the first year of life. In the second year of life a common sign is self-mutilating behaviors.

Because collagen is a protein, it must be broken down by a protease. Proteases exert their effects by hydrolyzing peptide bonds. The specific enzyme that breaks down collagen, predictably, is called collagenase.

The other classes of enzymes listed have actions unrelated to protein breakdown. An isomerase rearranges bonds to form an isomer, a polyermase adds nucleotides to DNA, a lipase breaks down fats, and a ligase creates a chemical bond.

Aminotransferases do not release amino groups, but rather transfer them to other amino acids. The reactions catalyzed by aminotransferases are reversible. Their blood concentrations can be used as clinical indicators for damage to liver or muscle.

Glutaminase synthetase is present predominately in the brain, liver and kidneys.The importance of the reaction catalyzed by glutamine synthetase is that excess nitrogen (in the form of toxic ammonia) from protein degradation can be removed from tissues, especially the brain. The reaction catalyzed by glutamine synthetase is irreversible. It converts glutamate to glutamine.