Catalysts and Catalysis

The definition of a catalyst is that it is something that speeds up a reaction without being used up itself. Therefore every reaction that takes place in the body that requires a catalyst/enzyme will do so, but the catalyst will remain intact at the end. Therefore the body does not have to keep making enzymes all the time. It only needs to replace the ones that are oxidized or otherwise degraded.

(A catalyst can also slow down a reaction.)

a catalyst provides a different path for a reaction to occur

To lower the activation energy of a reaction

Reduces the activation energy of the reaction, which speeds up the progress of the reaction

It increases the rate of a chemical reaction. However a true catalyst is not consumed in the reaction.

The presence of a catalyst affect the enthalpy change of a reaction is that catalysts do not alter the enthalpy change of a reaction. Catalysts only change the activation energy which starts the reaction.

An example of an inhibitor is a preservative.

Preservatives are added to foods to slow down the growth of bacteria and fungi. The preservatives prevent bacteria and fungi from producing substances that can spoil food.

Some antibiotics are examples of inhibitors also. For example, penicillin prevents certain kinds of bacteria from making a cell wall .So, the bacteria die.

Muscle enzymes are proteins produced by muscles that help regulate various physiological processes. They are released into the bloodstream when muscle tissue is damaged, either due to injury or certain medical conditions. Measuring the levels of these enzymes in the blood can help diagnose muscle-related disorders or injuries.

A catalyst increases the rate of a chemical reaction by providing an alternative pathway with lower activation energy. It does not change the equilibrium state or the overall thermodynamics of the reaction. This allows the reaction to proceed faster without being consumed in the process.

Yes, enzymes are catalysts found in every cell in the body. They play a crucial role in facilitating chemical reactions by speeding up the conversion of substrates into products without being consumed in the process. This allows the body to efficiently carry out essential biological functions.

Enzyme are proteins, and, thus, have the same building blocks. They are made up of amino acids.

By definition a catalyst cannot affect equilibrium because although a catalyst can speed up a chemical reaction, it cannot change the thermodynamics of it, and equilibrium is determined solely by thermodynamics. A catalyst may help a system reach equilibrium more quickly, but it will not change it. One possible way a catalyst could affect equilibrium is by introducing a catalyst that affects a different reaction involving the substrate or products of the original reaction, but this would be cheating since the system would no longer be closed.

Yes, enzymes can be reused multiple times because they are not consumed in the reactions they catalyze. However, their activity and efficiency might decrease over time due to factors like denaturation or loss of cofactors. Regular maintenance and optimization are typically needed to ensure their continued effectiveness.

When two molecules react with each other they must form a transition state. The higher the energy of the transition state the less likely it is for the two molecules to react with each other.

Catalysts lower the energy of the transition state. This makes it more likely for molecules to react with one another, which speeds up the overall reaction.

Entropy is unrelated. Reactions that break apart molecules increase entropy. Reactions that combine molecules together diminish entropy. Both types of reactions can be sped up by catalysts.

Enzymes are biological catalysts. This means they break down substances without being changed themselves. This is why they can be used over and over again. Enzymes are made from amino acids joined together by different bonds, one of the type of bonds being hydrogen bonds. As enzymes have hydrogen bonds it means they are sensitive to pH and temperature. A temperature too low will mean that the molecules (substrate) which should fit to an area on the enzyme called the active site cannot do so as hydrogen bonds are stronger in colder conditions. (Enzymes change slightly as the substrate fits on to it) This would mean that the enzyme is less able to change shape slightly because the stronger hydrogen bonds make the enzyme less flexible. Temperatures which are too high for the enzyme (if they exceed the perfect temperature, called the optimum temperature, of the enzyme) denature the enzymes, meaning that they are unable to catalyse chemical reactions, this is due to the high temperature causing the hydrogen bonds which bond the amino acids together to beak, causing the enzymes active site to change shape, meaning that the substrate can no longer fit into the active site meaning that the rate of reaction of the chemical reaction is lower. There is a point when the hydrogen bonds, once broken, are no longer able to re-bond, meaning the enzyme could never "re-nature". This is very bad if the chemical reaction is necessary. If the pH which the enzyme is exposed to is not its optimum the rate of reaction will be slower as the pH changes the molecular shape of the enzyme, and can have an effect on the intermolecular forces of the Hydrogen bonds (it can weaken or strengthen them)

A catalyst for an organic chemistry reaction would be any substance that speeds up the reaction. This would include metals such as platinum, palladium, mercury, zinc, and even certain acids. It must be noted that the catalyst varies for every reaction. An organically based catalyst (a catalyst made of carbon) would be an enzyme, coenzyme, or a vitamin. You can be an organic catalyst by being the change you wish to see in the world.

Enzymes catalyze reactions by lowering the activation energy needed without themselves being used up in the process. Without catalysts such as enzymes, some chemical metabolic reactions would take forever to happen or not happen at all.

a specific enzyme usually catalyzes only one kind of chemical reaction

There are two types of amylase enzymes. Salivary amylase is known as ptyalin; act upon carbohydrates in the mouth. Ptyalin begins polysaccharide digestion in the mouth; the process is completed in the small intestine by the pancreatic amylase, sometimes called amylopsin.

Because the concentration is directly proportional to the rate of reaction (the rate will increase but k will remain the same), with an increase in concentration the activation energy will stay because the activation energy does not account for the concentration.

Enzymes are proteins that act as biological catalysts. They speed up chemical reactions by lowering the activation energy required for the reaction to occur. Enzymes are highly specific in their action and can catalyze a wide range of biochemical reactions in living organisms.

Restriction enzymes (also known as restriction endonucleases) are proteins which cut DNA up at specific sequences in the genome. For example, the commonly used restriction endonuclease EcoRI recognizes every point in DNA with the sequence GAATTC, and cuts at the point between the Guanine and Adenine. Interestingly, the recognition sequences for most restriction endonucleases are genetic palindromes, e.g., the sequence reads exactly the same backwards on the complementary strand. In the case of EcoRI, the two complementary DNA strands for the recognition sequence are: 5'--GAATTC ---3'3'--CTTAAG--5'

Enzymes are biological catalysts. They speed up

metabolic reactions in the body but remain chemically unchanged

themselves. Enzymes contain an active site. This is a region to which another molecule may bind. This molecule is known as the substrate, and is usually specific to the active site of the particular enzyme, which breaks it down. Substrates

will not usually fit into any other active sites other than that of

the enzyme it is specified to. This can be explained as a lock and key

model, where the lock and key are specific to each other, only, that

there are many of the same kinds of lock and key when it come to the

enzymes. The higher the temperature, the higher the rate of

reaction up to a certain point. This is due to the fact that the

particles gain kinetic energy and subsequently move around more

vigorously. Thus, the chance of there being a successful collision

between the enzyme and substrate molecule increases as reacting

particles with collide more frequently with increased kinetic energy. Enzymes have a very specific three-dimensional shape, held together by

ionic and hydrogen bonds. If the amino acids are too vigorous in their

motion, then, these bonds will brake. Once the bonds have been broken,

the enzyme is said to have become denatured. As a result of becoming

denatured, the enzymes' rate of activity becomes less because the

enzyme loses its specific three-dimensional shape. The enzyme will

start to become denatured after around 40ºC as enzyme activity is

usually at its optimum at this temperature. After this, the rate of

reaction will probably deteriorate. After 60ºC, there is likely to be

no reaction, as the enzymes would probably be completely denatured by

then.

Enzymes work by binding to specific molecules called substrates and catalyzing chemical reactions to convert them into different products. The enzyme's active site provides a specific environment for the reaction to occur, lowering the energy required for the reaction to take place. Enzymes are highly specific and can be regulated to control the rate of reactions within cells.

Enzymes are proteins that act as biological catalysts, speeding up chemical reactions. They are highly specific, meaning they only catalyze one type of reaction. Enzymes can be affected by factors such as temperature and pH, which can impact their function.

Roman numerals indicate the oxidation state of the metal in the compound. In MnO2, manganese has an oxidation state of +4, so it is represented as manganese(IV) oxide. In Mn2O7, manganese has an oxidation state of +7, so it is named manganese(VII) oxide. Including Roman numerals ensures clarity about the oxidation state of the metal ion in the compound.

As the enzyme concentration increases, the rate of reaction will increase because there are many more enzymes present to aid break down the substrate. However, a point will be reached when no matter how much enzyme is present, the reaction will not occur any quicker. This is equilibrium. This happens because all the substrate is being broken down by the exact same amount of enzyme, so enzymes will be present which have no substrate to break down.