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

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Turpin, Erick
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Alan DiSpirito
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Biochemistry, Biophysics and Molecular Biology

The Department of Biochemistry, Biophysics, and Molecular Biology was founded to give students an understanding of life principles through the understanding of chemical and physical principles. Among these principles are frontiers of biotechnology such as metabolic networking, the structure of hormones and proteins, genomics, and the like.

The Department of Biochemistry and Biophysics was founded in 1959, and was administered by the College of Sciences and Humanities (later, College of Liberal Arts & Sciences). In 1979 it became co-administered by the Department of Agriculture (later, College of Agriculture and Life Sciences). In 1998 its name changed to the Department of Biochemistry, Biophysics, and Molecular Biology.

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  • Department of Biochemistry and Biophysics (1959–1998)

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Biochemistry, Biophysics and Molecular Biology

Methanobactin (Mb) is the first characterized example of a chalkophore or copper

binding protein. Mbs are produced by most aerobic methane oxidizing bacteria for Cu

recruitment to the cell and eventually incorporation into the central metabolism. In addition to

the biological purpose of Cu binding, mbs bind a number of transition and near transition metals.

Within this text, the metal binding properties are explored and compared between two mbs,

which represent two distinct groups of mbs, mb from Methylosinus trichosporium OB3b and mb

from Methylocystis strain SB2. The Cu binding properties of these mbs have been previously

explored, however, herein, the binding and displacement properties of each mb are presented for

a number of transition metals.

The binding properties of the metals able to displace Cu from Cu bound mb (Cu-mb) are

of particular interest due to the extremely high affinity with which mbs bind Cu. Mercury is one

such example, and the binding properties of Hg, in the forms Hg2+, Hg(CN)2, and CH3Hg+, are

examined for mb from Methylocystis strain SB2. Each form was bound slightly differently by

mb-SB2. Chapter 2 presents the characterization of the Hg binding, in each form, for mb-SB2.

Au also displaces Cu-mb for both mb-OB3b and SB2. In the final chapter, the Au

binding properties of mb-OB3b and mb-SB2 are compared. Previously collected CD spectra of

mb-SB2 titrated with Au(III) suggested that an exciton transfer exists between the chromophores

of mb-SB2. Herein, stopped flow UV-vis kinetic traces of mb-OB3b titrated with Au(III)

demonstrate that an exciton transfer is present between the chromophores of mb-OB3b.

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