Comparison of the Kinetics and Spectral Properties of AuCl4- Binding by Methanobactins from Methylosinus trichosporium OB3b and Methylocystis Strain SB2: Evidence of Exciton Disruption between Intramolecular Chromophores

dc.contributor.advisor Alan DiSpirito
dc.contributor.author Turpin, Erick
dc.contributor.department Biochemistry, Biophysics and Molecular Biology
dc.date 2018-08-11T14:59:41.000
dc.date.accessioned 2020-06-30T03:08:12Z
dc.date.available 2020-06-30T03:08:12Z
dc.date.copyright Fri Jan 01 00:00:00 UTC 2016
dc.date.embargo 2001-01-01
dc.date.issued 2016-01-01
dc.description.abstract <p>Methanobactin (Mb) is the first characterized example of a chalkophore or copper</p> <p>binding protein. Mbs are produced by most aerobic methane oxidizing bacteria for Cu</p> <p>recruitment to the cell and eventually incorporation into the central metabolism. In addition to</p> <p>the biological purpose of Cu binding, mbs bind a number of transition and near transition metals.</p> <p>Within this text, the metal binding properties are explored and compared between two mbs,</p> <p>which represent two distinct groups of mbs, mb from Methylosinus trichosporium OB3b and mb</p> <p>from Methylocystis strain SB2. The Cu binding properties of these mbs have been previously</p> <p>explored, however, herein, the binding and displacement properties of each mb are presented for</p> <p>a number of transition metals.</p> <p>The binding properties of the metals able to displace Cu from Cu bound mb (Cu-mb) are</p> <p>of particular interest due to the extremely high affinity with which mbs bind Cu. Mercury is one</p> <p>such example, and the binding properties of Hg, in the forms Hg2+, Hg(CN)2, and CH3Hg+, are</p> <p>examined for mb from Methylocystis strain SB2. Each form was bound slightly differently by</p> <p>mb-SB2. Chapter 2 presents the characterization of the Hg binding, in each form, for mb-SB2.</p> <p>Au also displaces Cu-mb for both mb-OB3b and SB2. In the final chapter, the Au</p> <p>binding properties of mb-OB3b and mb-SB2 are compared. Previously collected CD spectra of</p> <p>mb-SB2 titrated with Au(III) suggested that an exciton transfer exists between the chromophores</p> <p>of mb-SB2. Herein, stopped flow UV-vis kinetic traces of mb-OB3b titrated with Au(III)</p> <p>demonstrate that an exciton transfer is present between the chromophores of mb-OB3b.</p>
dc.format.mimetype application/pdf
dc.identifier archive/lib.dr.iastate.edu/etd/16029/
dc.identifier.articleid 7036
dc.identifier.contextkey 11169577
dc.identifier.doi https://doi.org/10.31274/etd-180810-5656
dc.identifier.s3bucket isulib-bepress-aws-west
dc.identifier.submissionpath etd/16029
dc.identifier.uri https://dr.lib.iastate.edu/handle/20.500.12876/30212
dc.language.iso en
dc.source.bitstream archive/lib.dr.iastate.edu/etd/16029/Turpin_iastate_0097M_16184.pdf|||Fri Jan 14 20:54:07 UTC 2022
dc.subject.disciplines Biochemistry
dc.title Comparison of the Kinetics and Spectral Properties of AuCl4- Binding by Methanobactins from Methylosinus trichosporium OB3b and Methylocystis Strain SB2: Evidence of Exciton Disruption between Intramolecular Chromophores
dc.type article
dc.type.genre thesis
dspace.entity.type Publication
relation.isOrgUnitOfPublication faf0a6cb-16ca-421c-8f48-9fbbd7bc3747
thesis.degree.discipline Biochemistry
thesis.degree.level thesis
thesis.degree.name Master of Science
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