NMR Study of Interaction between Cytochrome P450cam and Putidaredoxin and Structural Study of Cytochrome P450 3A4

DSpace Repository

Show simple item record

dc.contributor.advisor Pochapsky, Susan
dc.contributor.author Yin, Ming
dc.date.accessioned 2009-05-05T13:27:47Z
dc.date.available 2009-05-05T13:27:47Z
dc.date.issued 2009
dc.identifier.uri http://hdl.handle.net/10192/23190
dc.description.abstract Cytochrome P450cam (CYP101) is a monooxygenase found in the soil bacterium Pseudomonas putida. In the presence of its electron transfer partner putidaredoxin (Pdx), CYP101 catalyzes the reaction of 5-exo hydroxylation of camphor. With a significant number of backbone resonances already assigned in this large protein in its substrate camphor- and CO-bound reduced form, we investigated the binding effect between mutant CYP101 and Pdx. Nuclear magnetic resonance (NMR) spectroscopy showed that the binding between these two proteins decreased, compared to the wild type (WT) CYP101 and Pdx. Cytochrome P450 3A4 (CYP3A4), as a member of the cytochrome P450 oxidase family, is one of the most important enzymes in the human body. It is involved in the metabolism of a large number of xenobiotics. Solution state NMR study on this membrane bound protein was accomplished by the incorporation of CYP3A4 into nanodiscs, which prevents CYP3A4 from aggregating and keeps CYP3A4 as a monomer.
dc.description.sponsorship Brandeis University, Graduate School of Arts and Sciences
dc.format.mimetype application/pdf
dc.language English
dc.language.iso eng
dc.publisher Brandeis University
dc.relation.ispartofseries Brandeis University Theses and Dissertations
dc.rights Copyright by Ming Yin 2009
dc.subject Chemistry
dc.title NMR Study of Interaction between Cytochrome P450cam and Putidaredoxin and Structural Study of Cytochrome P450 3A4
dc.type Thesis
dc.contributor.department Department of Chemistry
dc.degree.name MS
dc.degree.level Masters
dc.degree.discipline Chemistry
dc.degree.grantor Brandeis University, Graduate School of Arts and Sciences


Files in this item

This item appears in the following Collection(s)

Show simple item record

Search BIR


Browse

My Account