Enzyme Kinetics
Enzymes are described as the organic catalysts, which increase the rate of reaction of a biochemical reaction. Enzymes are proteins that speed up the rate of reaction without being used up, and therefore they are reusable (Jonathan, 2012). The enzyme studied in this lab was succinate dehydrogenase.
Enzyme kinetics is the study of how biological catalysts increase the reaction rate in reactions. Without the catalysts, the biological procedures necessary for organisms would not continue at a rate that could sustain life. A more simpler way to model enzyme kinetics is the Michealis-Menten model (Wilkinson, 1970). This model describes the rate of enzyme reactions, by relating the reaction rate to concentration of the substrate. Reaction rates can be represented mathematically, which demonstrates how the different chemical species involved in the reaction are affected throughout the reaction (Wilkinson, 1970).
The Mitochondria and Electron Transport Chain
The mitochondria is found in the cytoplasm of almost all eukaryotic cells, and its primary function is to generate a large amount of energy in the form of ATP (adenosine triphosphate) (Morris et al., 2013). ATP is then used to carry out other cellular processes. The mitochondrial matrix contains DNA on the genome and the enzymes of the krebs cycle, which metabolizes nutrients into by-products that the mitochondria can use for energy making (Metabolism, 2014).
In the mitochondria, the conversion of succinate to fumerate (by the use of succinate dehydrogenase and FAD) is required to generate the proton gradient. Succinate is a chemical that is produced in the ATC cycle for cellular respiration, while succinate dehydrogenase (SDH) is one of the only enzymes that is used ...
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... It states that the initial velocity should be directly proportional to the volume of mitochondrial suspension (Fig. 2 & 4). There is a higher initial velocity of the reaction because of the SDH’s “want” to attract to the succinate. With the increasing amount of SDH concentrations in tubes 1 to 4 in figure 2, the binding of succinate to SDH will increase (Jonathan et al., 2012). Tube 1 has the least amount of SDH concentration and therefore shows the lowest initial velocity, whereas tube 4 had the highest SDH concentration and showed a higher initial velocity (Fig. 2).
According to the results and the data we have collected, we are able to conclude that as SDH concentration increases, the reaction rate from succinate to fumarate also increases. Figures 2 and 3 prove that with the addition of malonate and the omitted succinate and azide, slow down the reaction rate.
The rate law determines how the speed of a reaction occurs, thus allowing the study of the overall mechanism formation in reactions. In the general form of the rate law, it is A + B C or r=k[A]x[B]y. The rate of reaction can be affected by the concentrations such as A and B in the previous equation, order of reactions, and the rate constant with each species in an overall chemical reaction. As a result, the rate law must be determined experimentally. In general, in a multi-step reaction, there will be one reaction that is slower than the others.
Enzymes are proteins that increase the speed of reactions in cells. They are catalysts in these reactions which means that they increase the speed of the reaction without being consumed or changed during the reactions. Cofactors are required by some enzymes to be able to carry out their reactions by obtaining the correct shape to bind to the other molecules of the reaction. Chelating agents are compounds that can disrupt enzyme reactions by binding to metallic ions and change the shape of an enzyme. Catechol is an organic molecule present under the surface of plants. When plants are injured, catechol is exposed to oxygen and benzoquinone is released because of the oxidation of catechol. Catecholase aids in the reaction to produce
Background information:. Enzyme Enzymes are protein molecules that act as the biological catalysts. A Catalyst is a molecule which can speed up chemical reactions but remains unchanged at the end of the reaction. Enzymes catalyze most of the metabolic reactions that take place within a living organism. They speed up the metabolic reactions by lowering the amount of energy.
The [ES] complex can then undergo two different pathways; the complex can dissociate to [E] and [S], at a rate of k or it can shift equilibrium to the left with a rate constant of k2 to form [E] and product [P]1. In this model, the breakdown of the ES complex to yield P is the overall rate-limiting step. Three assumptions of a Michaelis-Menton plot are that a specific [ES] complex in rapid equilibrium between [E] and [S] is a necessary intermediate, the amount of substrate is more than the amount of enzyme so the [S] remains constant, and that this plot follows steady state assumptions. Steady state assumptions states that the intermediate stays the same concentration even if the starting materials and products are constantly changing.2 The rapid equilibrium between enzyme and substrate, and the enzyme-substrate complex yields a mathematical description regarded as the Michaelis-Menton
Molecules called enzymes help catalyze reactions. A substrate is the molecule on which the enzyme acts. Most enzymes are proteins that have grooves in them called active sites that recognizes the substrate.
Enzymes are an important part of all metabolic reactions in the body. They are catalytic proteins, able to increase the rate of a reaction, without being consumed in the process of doing so (Campbell 96). This allows the enzyme to be used again in another reaction. Enzymes speed up reactions by lowering the activation energy, the energy needed to break the chemical bonds between reactants allowing them to combine with other substances and form products (Campbell 100). In this experiment the enzyme used was acid phosphates (ACP), and the substrate was p-nitrophenyl phosphate.
Enzymes are proteins or RNA, ribonucleic acid. An enzyme speeds up a chemical reaction. Since the enzyme is not changed by speeding up a chemical reaction, the enzyme can speed up reactions again and again. In a process called catalysis, an enzyme takes what would have been a relatively slow reaction, and makes it faster than the reaction would have been without the enzyme. Enzymes also take the activation energy, which is the energy needed to start reactions, and shortens it. With the decrease in the amount of activation energy needed, reactions could occur more often, and less energy would be needed to begin each reaction. When an enzyme takes a substrate, which is a specific reactant, it changes the substrate in a specific way (Unity and Diversity 82). The active site on the enzyme is a specific shape, so the enzyme can only change certain substrates, the ones that fit into the enzyme’s activation site like a piece in a puzzle.
The rate equation is in terms of concentration over time and the reaction rate compares the increase/decrease
= == In relative terms enzymes are biological catalysts; control the rate of chemical reaction, different temperatures and pH’s affect their optimum rate of reaction in living organisms. In detail; enzymes are globular proteins, which catalyse chemical reactions in living organisms, they are produced by living cells – each cell has hundreds of enzymes. Cells can never run out of enzymes as they or used up in a reaction.
What is the purpose of holding the initial concentration of one reactant constant during each trial?
The mitochondria is an organelle which is generally an oval shape and is found inside the cytoplasm and is again apart of the eukaryotic cells. The main function of the mitochondria is to complete cellular respiration; in simple terms it acts like a digestive system to break down essential nutrients and to convert it into energy. This energy is usually found to in ATP which is a rich molecule taken from the energy stored in food. Furthermore, mitochondria stores calcium for signalling activities; such as heat, growth and death. They have two unique membranes and mitochondria isn’t found in human cells like the red blood cells yet liver and muscle cells are filled entirely with mitochondria.
In this lab, it was determined how the rate of an enzyme-catalyzed reaction is affected by physical factors such as enzyme concentration, temperature, and substrate concentration affect. The question of what factors influence enzyme activity can be answered by the results of peroxidase activity and its relation to temperature and whether or not hydroxylamine causes a reaction change with enzyme activity. An enzyme is a protein produced by a living organism that serves as a biological catalyst. A catalyst is a substance that speeds up the rate of a chemical reaction and does so by lowering the activation energy of a reaction. With that energy reactants are brought together so that products can be formed.
Chemical kinetics is the study and examination of chemical reactions regarding re-arrangement of atoms, reaction rates, effect of various variables, and more. Chemical reaction rates, are the rates of change in amounts or concentrations of either products or reactants. Concentration of solutions, surface area, catalysts, temperature and the nature of reactants are all factors that can influence a rate of reaction. Increasing the concentration of a solution allows the rate of reaction to increase because highly concentrated solutions have more molecules and as a result the molecules collide faster. Surface area also affects a
Energy production- The most important function of mitochondria is energy production in the form of ATP. The raw materials are food materials and tissues which are broken down in catabolism. These molecules transferred to mitochondria for further processes. In inner membrane they have electrical charges then they help in producton of ATP (Phosphorylaton) by combine with oxygen (Oxidaton) through five electron transport chain complexes. So this overall
One vital process in the human body observed in chemistry is the idea of chemical kinetics. Chemical kinetics is the study of the rate of reactions, or how fast reactions occur.1 Three factors that affect chemical kinetics are concentration, temperature, and catalysis. As the concentration of a substance increases, the rate of the reaction also increases.1 This relationship is valid because when more of a substance is added in a reaction, it increases the likelihood that the