Presentation Title

Redox titrations of cytochrome P450 BM3

Start Date

November 2016

End Date

November 2016

Location

HUB 302-32

Type of Presentation

Poster

Abstract

Cytochrome P450 is a versatile enzyme that can catalyze a variety of commercially relevant reactions (e.g., making new detergents, textiles, etc.), and is involved in the metabolism of the majority of pharmaceutical drugs. It is our goal to exploit these enzymes for commercial use. P450 has a molecule within it called a heme, which contains an iron center where all the chemistry occurs. In order to effect catalysis, the enzyme utilizes electrons from a complex electron transfer system that delivers electrons to the heme. To bypass this requirement, P450 can be trapped within surfactant films (didodecyldimethylammonium bromide, DDAB) on electrode surfaces; the electrode can then supply the needed electrons. However, we have found that the enzyme-film-electrode interaction alters the biophysical properties of P450, which renders it inactive. We have established that the heme is greatly perturbed in our enzyme-film-electrode structure compared to in solution. One clue to understanding the nature of P450 and its native activity comes from the potential of the heme center, which is an electrochemical parameter that refers to the ease of the iron center accepting electrons from external sources. Thus, the purpose is to make clear the effect of the membrane film on the heme potential by conducting redox titrations. We hope this information will lead us towards restoring native-like activity for bioelectrocatalysis.

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Nov 12th, 1:00 PM Nov 12th, 2:00 PM

Redox titrations of cytochrome P450 BM3

HUB 302-32

Cytochrome P450 is a versatile enzyme that can catalyze a variety of commercially relevant reactions (e.g., making new detergents, textiles, etc.), and is involved in the metabolism of the majority of pharmaceutical drugs. It is our goal to exploit these enzymes for commercial use. P450 has a molecule within it called a heme, which contains an iron center where all the chemistry occurs. In order to effect catalysis, the enzyme utilizes electrons from a complex electron transfer system that delivers electrons to the heme. To bypass this requirement, P450 can be trapped within surfactant films (didodecyldimethylammonium bromide, DDAB) on electrode surfaces; the electrode can then supply the needed electrons. However, we have found that the enzyme-film-electrode interaction alters the biophysical properties of P450, which renders it inactive. We have established that the heme is greatly perturbed in our enzyme-film-electrode structure compared to in solution. One clue to understanding the nature of P450 and its native activity comes from the potential of the heme center, which is an electrochemical parameter that refers to the ease of the iron center accepting electrons from external sources. Thus, the purpose is to make clear the effect of the membrane film on the heme potential by conducting redox titrations. We hope this information will lead us towards restoring native-like activity for bioelectrocatalysis.