• Login
    View Item 
    •   Oxy Scholar Home
    • Chemistry
    • Chemistry URC Student Scholarship
    • View Item
    •   Oxy Scholar Home
    • Chemistry
    • Chemistry URC Student Scholarship
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Engineered P450 Cytochromes for Bioelectrochemical Catalysis

    Thumbnail
    Author
    Fung, Chi
    Issue
    urc_student; urc_student
    Date
    2009-01-01 0:00
    Metadata
    Show full item record
    URI
    https://scholar.oxy.edu/handle/20.500.12711/529
    Abstract
    The growing demand for environmentally benign Technologies presents significant challenges for the petrochemicals industry. This is especially true for chemical conversions involving oxidation as the reactive transition metal catalysts often employedcan be highly toxic and difficult to dispose of. Additionally, their synthetic limitations and complex syntheses further underscore the need for alternative strategies. As such, the P450 cytochromes present an attractive solution: their ability to regio- and stereospecifically oxidize an array of compounds under ambient conditions continues to fuel research into exploiting these?green? biocatalysts for commercial applications. However, a significant obstacle for practical applications using P450s is the expensive NAD(P)H cofactor, required in stoichiometric quantities for activity. The proposed work will seek to overcome this challenge by replacing NAD(P)H with the electrochemically recyclable hydride transfer complex Cp*Rh(bpy)(H2O)Cl2 (Rh), which can efficiently regenerate flavin cofactors in solution. The system will be developed for P450 BM3 which contains hydroxylase and flavin-containing reductase domains on a single polypeptide. As the protein-bound flavins hinder efficient reaction with Rh, a mutation library will be made to generate enzyme variants displaying improved activity with various similar organometallic cmpounds. In addition to catalysis, as there is no crystal structure of the reductase domain, mutants displaying activity will provide key insights into the mediator-flavin domain interaction which can be used for subsequent targeted mutagenesis to explore structure-function relationships.
    Collections
    • Chemistry URC Student Scholarship

    Browse

    All of Oxy ScholarCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsJournal TitleJournal IssueThis CollectionBy Issue DateAuthorsTitlesSubjectsJournal TitleJournal Issue

    My Account

    LoginRegister

    DSpace software copyright © 2002-2021  DuraSpace
    Contact Us | Send Feedback
    DSpace Express is a service operated by 
    Atmire NV