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Exergonic Reaction
Entropy is a measure of disorder. To achieve the order in the organization of organisms requires an input of energy. Eventually this energy is converted to heat (high entropy) and dissipates. Therefore, a continual input of energy is necessary to maintain organisms.
ATP: Energy for Cells Structure of ATP ATP is adenosine plus 3 phosphate groups. ATP is a high energy molecule because the 3rd phosphate group is easily removed.
Videos: What ATP is and How it Works < http://www.youtube.com/watch?v=bbtqF9q_pFw>. Coupled Reactions <http://www.youtube.com/watch?v=7IqgrcBkGRU>. Questions 1. What is metabolism? Metabolism is the sum of all the chemical reactions that occur in a cell. These reactions use substances known as reactants to form new substances known as products. 2. Under what conditions do reactions occur spontaneously? A reaction will occur spontaneously if it increases the entropy, or disorder, of the universe. A reaction will also occur spontaneously if it is exergonic. This means that the products have less free energy than the reactants, resulting in a negative G (change in free energy). 3. What is free energy, and how is it better than entropy when considering reactions? Free energy is the amount of energy available to do work after a chemical reaction has occurred. It is better than entropy because biologists can determine the spontaneity of a reaction without having to consider the entire universe. 4. Use and + and mention which ones go with exergonic and endergonic reactions. Add in the correct letter and symbol for free energy. Exergonic reactions: energy is released, free energy of products < free energy of reactants (G) Endergonic reactions: an input of energy is required, free energy of products > free energy of reactants (+G) 5. What are some benefits of using ATP over glucose in terms of energy? When ATP becomes ADP + (P), the amount of energy released is sufficient for the biological purpose, so little energy is wasted. Glucose is an unstable high-energy molecule, so the amount of
energy released when it breaks down is a lot more than needed for the biological purpose, and much goes to waste. One glucose can be used to make 36 ATP, providing energy for 36 reactions. This is more efficient than having 1 glucose molecule provide energy for 1 reaction. 6. How are exergonic and endergonic reactions related to coupled reactions? Relate this to ATP? Coupling requires that the exergonic and the endergonic reactions be closely tied, so that the energy released by one can be used to drive the other. ATP breakdown is an exergonic reaction, so it is coupled with endergonic reactions to minimize energy loss. 7. What are the 3 functions of ATP in terms of work? Chemical work: ATP supplies the energy needed to synthesize macromolecules that make up the cell and, therefore, the organism. Transport work: ATP supplies the energy to pump substances across the plasma membrane. Mechanical work: ATP supplies the energy needed to permit muscles to contract, cilia and flagella to beat, chromosomes to move, etc. 8. What is a coupled reaction? A coupled reaction occurs when the energy released by an exergonic reaction is used to drive an endergonic reaction.
Metabolic pathways are linked reactions that begin with a reactant and end with a product.
An enzyme is a protein that speeds up chemical reactions because it causes substrates to react. A pathway involving A B C would require an enzyme to help A B and another enzyme to help B C.
Video: Enzyme <http://www.youtube.com/watch?v =V4OPO6JQLOE>. Energy of Activation Energy that must be added to cause molecules to react is called the energy of activation (Ea). Enzymes lower the energy of activation, making it more likely that substrates will meet.
Video: Bioenergetics <http://www.youtube.com/watch?v=nDCxIpiI7-Y>. Enzyme-Substrate Complexes The equation E + S ES E + P shows that the enzyme and the substrate form a complex. Enzymes are named for their substance because they are specific; the shape of the enzymes active site and the shape of the substances are complementary to one another. A process called induced fit assures that an enzyme-substrate complex will form.
Lock-and-key model: The shape of the substrate fits exactly in the active site of the unbound enzyme, like a key fits a lock. Induced-fit model: However, it is now known that the active site undergoes a slight change in shape in order to accommodate the substrate(s).
Coupled Reactions In coupled reactions, an exergonic reaction drives an endergonic reaction. The breakdown of ATP drives many coupled reactions.
Function of ATP ATP breakdown releases energy that drives reactions in cells (eg. synthetic reactions, muscle contraction, nerve conduction). Factors Affecting Enzymatic Speed Substrate Concentration As substrate concentration increases, there are more collisions between substrate molecules and enzymes. The reaction rate increases up to a maximum point (flat line). Beyond the point of saturation, increasing the substrate concentration no longer increases the rate of reaction because all of the available enzymes are already being used.
Temperature and pH Both a warm temperature and an optimal pH speed up an enzymatic reaction. A boiling temperature and an extreme pH usually cause a protein to denature, and the reaction stops. (refer to the graphs on the next page)
Enzyme Concentration When genes are active, more enzyme is present to speed up a reaction. However, the reaction rate only increases up to a certain point; after that, there is not enough substrate to react with the enzymes, so increasing the concentration of enzymes no longer has any effect (left).
Enzymes are often activated when kinases phosphorylate them (right). ATP is very useful in this case: in addition to energy, it also provides PO4 to turn on the protein.
Enzyme Inhibition Nearly every enzyme activity is regulated by feedback inhibition: A product molecules may occupy the active site in competitive inhibition. The end product may also bind to an allosteric site in allosteric inhibition. When the end product occupies this site, the shape of the active site changes and the substrate cannot fit there; thus, no more product is formed. Enzyme Cofactors Enzyme cofactors include inorganic ion cofactors and non-protein organic coenzymes. Vitamins are often components of coenzymes needed by enzymes to carry out their reactions. Coenzymes, unlike enzymes, participate in the reaction. Questions 1. Draw a metabolic pathway that begins with a reactant, has 5 intermediate steps, and ends with a final product. Use letters and numbers to symbolize your pathway. Include enzymes at each step.
2. What is the induced fit model of enzymes? The active site of the enzyme undergoes a slight alteration in shape in order to accommodate the substrate(s) and achieve optimum fit. 3. Why are enzymes named for their substrate? Give 5 examples. Enzymes are very specific: every reaction in a cell requires a particular enzyme which will only complex with their substrates. lipid lipase, urea urease, maltose maltase, ribonucleic acid ribonuclease, lactose lactase 4. Adding more substrate with a fixed amount of enzyme past a certain point no longer increases the rate of the reaction. Why? When the active sites of the enzymes are filled almost continuously with substrates, the enzymes rate of activity cannot increase any further, and the maximum reaction rate has been reached. 5. Draw 3 graphs: label the y-axis with reaction rate and the x-axis with substrate concentration, temperature, and enzyme concentration. Then draw an appropriate graph and explain to your parent/sibling why it has the shape it has. Get them to sign your graph once they understand it. 6. What is feedback inhibition, and how does it work? Discuss a simple and then a more complex example of it. Feedback inhibition occurs when the end product of a metabolic pathways binds to the first enzyme of the pathway, preventing the reactant from binding and the reaction from occurring.
When a product is in abundance, it binds competitively with its enzymes active site, preventing the substrate from binding to the active enzyme. As the product is used up, inhibition is reduced, and more product can be made. In this way, the concentration of the product is always kept within a certain range. In a more complicated type of feedback inhibition, the end product of the pathway binds to an allosteric site, which is another site on the enzyme. The binding shuts down the pathway so that no more products can be produced. 7. Why do bacteria die yet humans do not when penicillin is administered? Penicillin is an antimicrobial agent which blocks the active site of an enzyme unique to bacteria. Since enzymes are very specific and only bind to a certain kind of substrate, this drug has no effect on human enzymes. 8. Why do we need vitamins? (think 4-5 marks on a test type of answer to this question) Vitamins are often components of coenzymes, the organic, non-protein molecules which allow enzymes to function properly. We require trace amounts of vitamins in our diets to synthesize these coenzymes and maintain our health and physical fitness. For example, the vitamin niacin is part of the molecular structure of the coenzyme NAD, and B12 is part of the coenzyme FAD. A deficiency of any one of these vitamins leads to a lack of the corresponding coenzyme and, subsequently, a lack of certain enzymatic reactions. Eventually, humans may experience vitamindeficiency symptoms such as pellagra for niacin deficiency and cracks at the corners of the mouth for riboflavin deficiency.
Organelles and the Flow of Energy Chloroplasts capture the energy of the sun and carry on photosynthesis to produce carbohydrates. Mitochondria carry out aerobic cellular respiration that breaks glucose down; the energy released produces ATP molecules. Cycling molecules between chloroplasts and mitochondria allows a flow of energy from the sun through all living things.