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Mitochondria Fumarate Lab Report

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Introduction: The mitochondria are a vital organelle in eukaryotes, they are key in ATP production via the Electron Transport Chain. This chain is a series of 4 different protein complexes, which pump Hydrogen ions against their concentration gradient while obtaining electrons, and a complex called ATP Synthase, which is a turbine like complex which gains energy through the passage of Hydrogens, this energy is used to bind ADP and inorganic phosphate to form ATP. This chain can be easily disrupted with various enzymes, a few of which were tested in this lab. The purpose of the lab was to measure the reaction rate of succinate to fumarate, in the isolated mitochondria of cauliflower cells. This reaction is not visible to the naked eye, and thus an artificial electron acceptor DCIP was …show more content…

When it was omitted from tube 7, the reaction slowed substantially. This indicated that substrate concentration and enzyme catalyzation are directly proportional, meaning that without the succinate there is no binding to the active site and thus no catalyzation of fumarate. But a small reaction with a velocity of -0.0068 (abs/min) still occurred, due to there being small traces of succinate present in mitochondria. This is significant because it shows that mitochondria may store, or at least hold some, succinate for use in the electron transport chain, but not enough to drive a strong or indefinitely long reaction. Based on all of the data collected, it is evident that as the concentration of succinate dehydrogenase is increased within a cell, the rate of the reaction where succinate is oxidized to fumarate increases (up to a point where enzyme conc. > substrate). This is the exact opposite of the effect of raising the concentration of malonate or sodium azide, which would decrease the rate of reaction because of the competition for active sites with succinate

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Experiment 1: Questions and Hypothesis In this experiment, we were tasked to measure the amount of mitochondria in various cell fractions by looking for a biochemical marker within mitochondria called succinate dehydrogenase or SDH. This is an enzyme that catalyzes the conversion of succinate and FAD into fumarate and FADH2. The reduced electron carrier, FADH2, then carries the newly acquired electrons that it received in the Citric Acid Cycle and takes them to Ubiquinone in the mitochondrial electron transport chain (Leicht and McAllister, 2017). Measuring for the presence of this SDH can be tough so we have to get help from an artificial electron acceptor called DCIP.

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The competitive inhibitor that was added was lactose. We predicted this because competitive inhibitors block and bind to the active site so it will slow down the binding of the desired substrate. An alternative hypothesis that came up was that the reaction of substrate would stay consistent as if no inhibitor was added. The enzyme could reject the inhibitor if it does not fit in the active site, causing the substrate to bind as it normally would. Our results showed that with the addition of lactose, the reaction did slow down a considerably

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Both have cytochrome complexes and quinone molecules that carry electrons. Respiration consumes oxygen and forms water, whereas photosynthesis splits water and forms oxygen. Complexes I III and IV in the mitochondrial ETC pump hydrogens outside of the mitochondrial matrix, where only plastoquinone pumps protons. The mitochondrial ETC oxidizes NADH and FADH¬¬2 to pump hydrogen, where photosynthesis makes use of energy from photons and reduces water to get electrons. In the process of transporting electrons, ubiquinone does not pump hydrogen molecules out of the mitochondrial matrix as plastoquinone does into the thylakoid lumen for photosynthesis.

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Abstract The purpose of this experiment is to test for mitochondrial activity by isolating different organelles using the differential centrifugation process. Studying mitochondria is extremely important because they control the death and life of the cell by regulating the apoptotic signals (Frezza et al 2007). Also they are responsible for the metabolic reactions (aerobic respiration) and the production of ATP (Frezza et al 2007). Three hypotheses were formed based on my knowledge.

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The mitochondria is an organelle that is located in all eukaryotic cells. The mitochondria’s job is to convert glucose into adenosine triphosphate (ATP) by performing cellular respiration. The parts of the mitochondria are the matrix, mitochondrial ribosomes, cristae, mitochondrial DNA, the inner and outer membrane, the intermembrane space, and the ATP synthase. The matrix is located inside the inner membrane and contains the parts of the mitochondria inside of it.

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Every organism’s cells holds the responsibility for energy exchanges that are necessary to maintain itself. Each cell in every organism accomplishes many different tasks by breaking down molecules to create adenosine triphosphate,in other words, ATP, which is used to facilitate cellular activity. Cellular respiration creates energy to power metabolism, which is essential to life. This is done by converting ADP to ATP. The process of cellular respiration in eukaryotic cells are held in the mitochondria.

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656 Words | 3 Pages

Adding the borate buffer stops the reaction as it increases the pH from 4.5 (Phosphate-Citrate Buffer) to pH 9.8 (Borate Buffer). Enzymes each have specific optimal pHs in which the enzyme functions optimally. The pH 9.8 is too basic and the change in pH causes the enzyme to denature, changing its shape; which prevents the substrate from binding effectively, at which time it causes the enzyme to be no longer functional. Another way to denature the enzyme would be to expose the enzyme to extreme temperatures, causing the enzyme to be out of its optimal temperature range, thus denaturing

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Introduction: There are a number of environmental parameters that can affect enzyme activity and its process. Enzymes are substances made in by an organism that serves as a catalyst and quickens the biochemical reaction to occur. When a catalyst is brought into the picture, it speeds up the time needed for said reaction to occur, making the enzyme a “helper” for reactions. Enzymes and substrates are closely related in the sense that both join together to help bring the end result of the reaction much faster.

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Human mitochondrial diseases affect people of all ages and can infect any organ in the body. To date, there is no cure for mitochondrial diseases, however there are treatments available to reduce the symptoms and the suffering of those infected. Mitochondrial disease arise when mutations occur in either mt DNA or nuclear genes that encode the mitochondrial proteins essential for the generation of ATP. Furthermore, recent research shows, that dysfunctional mitochondria in one tissue can have an effect on the whole organism (Nunnari & Suomalainen,

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After, finding so much information on my topic I was well prepared to present what I learned to my peers. However, due to extensive scientific vocabulary, I saw myself reading from the slides for proper pronunciation of the enzyme that are involved in my pathway. Overall, my analyzes and description for my pathway were very thorough and accurate because my presentation contains all the required criteria. One aspect of my presentation that was especially successful was my explanation of the transportation process of Acetyl CoA from mitochondria to cytosol, and why it is so important. Another aspect of a successful presentation was my reasoning of why NADPH+ oxidized to NADP+ in second step reduction because NADPH is present in the cytosol while NADH is present in the

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The supernatant was then used as enzyme extract. • Hydrogen peroxide (H2O2, 2mM) in phosphate buffer (3.0ml) was taken in an experimental cuvette, followed by the rapid addition of 40μl of enzyme extract and mixed thoroughly. • The time required for a decrease in absorbance by 0.05 units was recorded at 240nm in a spectrophotometer (Genesys 10-S, USA). • The enzyme solution containing H2O2-free phosphate buffer

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ABSTRACT: The purpose of the experiments for week 5 and week 6 support each other in the further understanding of enzyme reactions. During week 5, the effects of a substrate and enzyme concentration on enzyme reaction rate was observed. Week 6, the effects of temperature and inhibitor on a reaction rate were monitored. For testing the effects of concentrations, we needed to use the table that was used in week 3, Cells.

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It is believed that an endosymbiotic event occurred where an organism capable of oxidative phosphorylation was consumed by another cell. This theory is backed up by the DNA, double membrane and mitochondrial specific transcription and translation mechanisms used to allow such a phenomenon to occur. Mitochondria still secure their characteristic double membrane structure and are still the primary source of ATP production, from their ancestors. Yet, their overall form has been altered, they have acquired innumerable new functions within the cell.

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Ornthine is then carried back in the mitochondrial matrix and the cycle is complete. There are two nitrogens in urea. One nitrogen came from the ammonia produced in the mitochondrial matrix captured in the form of carbamoyl phosphate. The second nitrogen came from the α−amino group of the aspartate substrate in the reaction involving argininosuccinate synthetase. The carbon of the bicarbonate was the sole carbon of urea.

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911 Words | 4 Pages

Because the entire structure of the mitochondria is optimized for the production of a proton gradient, a more accurate description of these organelles would be "the cell's batteries". Specifically, mitochondria are the site of aerobic respiration, where sugars and fatty acids are broken down in the presence of oxygen to produce energy in the form of ATP. Carbon dioxide is formed as a byproduct. As we shall see, far more ATP is generated by the mitochondria than by the cytosolic enzymes responsible for anaerobic glycolysis. Glycolysis, or anaerobic respiration, is the first phase of sugar breakdown at the cellular level.

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