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dc.contributor.authorBreece, Robert
dc.date.accessioned2011-08-30T22:35:47Z
dc.date.available2011-08-30T22:35:47Z
dc.date.issued2011-08-30
dc.date.submittedJuly 2011
dc.identifier.urihttp://hdl.handle.net/1928/13125
dc.description.abstractIn an effort to probe the structure and mechanism of metallo-b-lactamases, the metal-binding behaviors of several enzymes were studied using EXAFS (Extended X-ray Absorption Fine Structure). Three members of the metallo-b-lactamase subclass B1, BcII from Bacillus cereus, Bla2 from Bacillus anthracis and CcrA from Bacillus fragilis, were compared to examine metal-binding behavior within a subclass. Each system exhibits different metal-binding behavior including cooperative binding (BcII), sequential binding (CcrA), and differential binding between zinc(II) and cobalt(II) forms (Bla2). The metal-binding behavior of subclass B3 of L1 from Stenotrophomonas maltophilia was explored with RFQ (rapid-freeze quenched) EXAFS and site selective metal substitution. RFQ EXAFS show the metal coordination at 10 ms in the reaction in the native enzyme including a zinc-zinc distance (3.72Å) greater than is present in either the resting or product-bound states. Metal substitution incorporates cobalt(II) into the Zn2(DHH) of the enzyme and showed the metal-binding at each metal site.en_US
dc.language.isoen_USen_US
dc.subjectMetallo-b-lactamaseen_US
dc.subject.lcshBeta lactamases.
dc.subject.lcshMetalloenzymes.
dc.subject.lcshBinding sites (Biochemistry)
dc.titleStructural characterization of metal binding in metallo-b-lactamases using x-ray absorption spectroscopyen_US
dc.typeDissertationen_US
dc.description.degreeChemistryen_US
dc.description.levelDoctoralen_US
dc.description.departmentUniversity of New Mexico. Dept. of Chemistryen_US
dc.description.advisorKirk, Martin
dc.description.committee-memberTierney, David
dc.description.committee-memberGuo, Hua
dc.description.committee-memberTimmins, Graham
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