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    CHARACTERIZATION OF HEME OXYGENASE AND FERREDOXIN NADPH REDUCTASE: TWO REDOX PARTNER PROTEINS INVOLVED IN THE HEME-IRON ACQUISITION PATHWAY OF PSEUDOMONAS AERUGINOSA

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    umi-ku-2587_1.pdf (15.72Mb)
    Issue Date
    2008-08-04
    Author
    Wang, Andy
    Publisher
    University of Kansas
    Format
    259 pages
    Type
    Dissertation
    Degree Level
    Ed.D.
    Discipline
    Chemistry
    Rights
    This item is protected by copyright and unless otherwise specified the copyright of this thesis/dissertation is held by the author.
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    Abstract
    The infections from bacterial pathogen Pseudomonas aerugionsa are very difficult to cure and cause premature death of many patients with AIDs, cystic fibrosis and cancer. Bacteria need iron to infect an organism, but the concentration of free iron in mammals is very low (~10-9 M). Therefore, bacteria have developed sophisticated iron acquisition mechanisms, including the utilization of heme iron. Heme oxygenase is the only known protein used for heme degradation and iron release inside a cell. In Pseudomonas aerugionsa, once heme is internalized to the cytoplasm, heme oxygenase (pa-HO) uses heme as a cofactor and substrate and degrades it into biliverdin and releases iron and CO. This heme degration process uses three oxygen molecules and seven electrons obtained from a novel redox partner protein: ferredoxin NADPH reductase (pa-FPR). The unique heme degradation catalysis in pa-HO was studied from a global view by probing a series of hydrophobic phenylalanine (Phe) rings inside heme oxygenase. We probed the Phe rings via mutagenesis, fluorine labeling using reactivity assays and spectroscopic methods to understand the relationship of protein structure, dynamics and catalysis. The results show that the hydrophobic cluster not only maintains protein structure, but also fine-tunes protein dynamics to facilitate the channeled H-bonding network from the heme binding site to the protein periphery to sustain catalysis.
    URI
    http://hdl.handle.net/1808/4311
    Collections
    • Dissertations [4473]
    • Chemistry Dissertations and Theses [336]

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    785-864-8983
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    785-864-8983

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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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