The Effects of an Enzyme, Catechol Oxidase, on the Conversion of Four Different Substrates to Pr oduce Benzoquinone.
Amir Akhras
Lab partners: Monica Elabed, Andres Velazquez, and Roland Rencz
Biology 201
Instructor: Dr. Kara Nuss
October 28, 2014
ABSTRACT
Enzymes are catalysts that speed the reaction of substrates to produce products. They achieve this by lowering the energy of activation (EA) but they do not change the nature of the reaction. The objective of this experiment was to test which of the four substrates will produce benzoquinone based on their molecular formula and absorb the most light. Catechol oxidase was tested with four different substrates to determine which produced the most benzoquinone. After preparing the spectrophotometer, I added solutions and then I let the substrates react for five minutes. I measured the absorbance of each set by zeroing the blank and testing its corresponding test tube and recording the data in a table. Pyrogallol produced the most benzoquinone and therefore benzoquinone absorbed the most light. My …show more content…
Pyrogallol absorbed 0.146 of light and produced the most benzoquinone. Structure determines function (Reece et al., 2014). Though hydroquinone an isomer of catechol, the structure of hydroquinone places the hydroxyl groups at opposite end of the six carbon ring. The structure of benzoquinone has two double bonds with oxygen placed next to each other. The structure of pyrogallol has three hydroxyl groups which can be oxidized to produce the carbonyl groups on benzoquinone. Catechol on the other hand carries only two hydroxyl groups. When the hydroxyl groups are oxidized they produce benzoquinone but less than pryogallol. Also, the only substrates that fit the active site of catechol oxidase were pryogallol and catechol. Hydroquinone and L-tyrosine do not so benzoquinone was not
Amir Akhras
Lab partners: Monica Elabed, Andres Velazquez, and Roland Rencz
Biology 201
Instructor: Dr. Kara Nuss
October 28, 2014
ABSTRACT
Enzymes are catalysts that speed the reaction of substrates to produce products. They achieve this by lowering the energy of activation (EA) but they do not change the nature of the reaction. The objective of this experiment was to test which of the four substrates will produce benzoquinone based on their molecular formula and absorb the most light. Catechol oxidase was tested with four different substrates to determine which produced the most benzoquinone. After preparing the spectrophotometer, I added solutions and then I let the substrates react for five minutes. I measured the absorbance of each set by zeroing the blank and testing its corresponding test tube and recording the data in a table. Pyrogallol produced the most benzoquinone and therefore benzoquinone absorbed the most light. My …show more content…
Pyrogallol absorbed 0.146 of light and produced the most benzoquinone. Structure determines function (Reece et al., 2014). Though hydroquinone an isomer of catechol, the structure of hydroquinone places the hydroxyl groups at opposite end of the six carbon ring. The structure of benzoquinone has two double bonds with oxygen placed next to each other. The structure of pyrogallol has three hydroxyl groups which can be oxidized to produce the carbonyl groups on benzoquinone. Catechol on the other hand carries only two hydroxyl groups. When the hydroxyl groups are oxidized they produce benzoquinone but less than pryogallol. Also, the only substrates that fit the active site of catechol oxidase were pryogallol and catechol. Hydroquinone and L-tyrosine do not so benzoquinone was not