After reviewing the basics of enzymes and catalysis, we take a dive into the wonderful world of catalase. Beginning with establishing a base line of just how much hydrogen peroxide there is in 5.0mL of the reacted solution; to figuring out exactly how much actually reacted after 300 seconds of catalyzed reaction. Follow the experiment from the beginning steps right to the end as you see where the students went wrong, interpretation of the results, and great answers to work sheet questions. Now, dive into the amazing world of catalase catalysis.
Enzymes are catalytic proteins, meaning they speed up – but do not create – chemical reactions, without being used up or altered permanently in the process. Although various enzymes use different methods, all accomplish catalysis by lowering the free energy of activation – activation energy – for the reaction, thus allowing it to occur more easily.
Enzymes employ a variety of methods for performing catalysis. Some provide a micro environment within the active site where some of the side chains are H+ or OH- donors or receivers. Other enzymes work by bringing together substrates that would not normally meet outside the enzyme, or orienting them in a manner in which they would otherwise not occur. Still other enzymes stress the bonds of substrate molecules in order to make them easier to break; some take this a step further by actually forming temporary covalent bonds with the substrate molecules. Regardless of how it is done, all enzyme catalyzed reactions are reversible and will turn around when necessary.
Each enzyme has a unique and highly complex structure, which is given rise to through the four levels of protein organization. The specific arrangement of the amino acids via polypeptide bonds is the primary structure of the protein. Formed by ribosomes and encoded in mRNA, the primary structure gives rise to all other levels of organization. Secondary structure is formed...
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