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1.
Rolle, Clarence J.
Selective aerobic oxidations catalyzed by manganese(III) complexes using redox-active ligands.
Degree: PhD, Chemistry and Biochemistry, 2011, Georgia Tech
URL: http://hdl.handle.net/1853/42827 
► Selective oxidations are important for the functionalization of compounds in organic synthesis and chemical industry. Using O2 as a terminal e- acceptor would be ideal…
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▼ Selective oxidations are important for the functionalization of compounds in organic synthesis and chemical industry. Using O2 as a terminal e- acceptor would be ideal because it is cheap and environmentally friendly, but aerobic oxidations are often prone to unselective free radical autoxidation. Recently developed palladium catalysts use O2 as a selective multi-electron oxidant for various organic transformations. Although these methods are powerful and sophisticated, the lower cost of base metals makes them attractive as potential alternatives. The challenge is to develop methods for effecting multi-electron transformations at metals that typically prefer one electron changes. To this end, the development of manganese(III) complexes containing redox-active ligands as catalysts for selective oxidase-type oxidation of organic substrates was pursued. Bis(tetrabromocatecholato) manganese(III) complexes were shown to aerobically oxidize catechols to form quinones and H2O2. This reactivity was extended to other alcohol and amine substrates. In these reactions, the non-innocent tetrabromocatecholate ligands may impart a multi-electron character to the metal. To directly probe the intermediacy of ligand-centered radicals in catalytic turnover, a series of structurally similar manganese(III) complexes with aminophenol-derived ligands were prepared and characterized. The capacity of these ligands to undergo low-energy redox changes, allowed for isolation of an electron transfer series spanning two redox states without a change in oxidation state at the metal center. The ligand-centered redox events were a key feature in aerobic homocoupling of Grignard reagents.
Advisors/Committee Members: Jake Soper (Committee Chair), Angus Wilkinson (Committee Member), Christoph Fahrni (Committee Member), Christopher Jones (Committee Member), Kent Barefield (Committee Member).
Subjects/Keywords: Oxidation chemistry; Metal catalysts; Metalloenzymes; Manganese; Manganese catalysts; Oxidases; Oxidation
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APA (6th Edition):
Rolle, C. J. (2011). Selective aerobic oxidations catalyzed by manganese(III) complexes using redox-active ligands. (Doctoral Dissertation). Georgia Tech. Retrieved from http://hdl.handle.net/1853/42827
Chicago Manual of Style (16th Edition):
Rolle, Clarence J. “Selective aerobic oxidations catalyzed by manganese(III) complexes using redox-active ligands.” 2011. Doctoral Dissertation, Georgia Tech. Accessed January 16, 2021.
http://hdl.handle.net/1853/42827.
MLA Handbook (7th Edition):
Rolle, Clarence J. “Selective aerobic oxidations catalyzed by manganese(III) complexes using redox-active ligands.” 2011. Web. 16 Jan 2021.
Vancouver:
Rolle CJ. Selective aerobic oxidations catalyzed by manganese(III) complexes using redox-active ligands. [Internet] [Doctoral dissertation]. Georgia Tech; 2011. [cited 2021 Jan 16].
Available from: http://hdl.handle.net/1853/42827.
Council of Science Editors:
Rolle CJ. Selective aerobic oxidations catalyzed by manganese(III) complexes using redox-active ligands. [Doctoral Dissertation]. Georgia Tech; 2011. Available from: http://hdl.handle.net/1853/42827
Georgia Tech
2.
McRae, Reagan.
Investigating metal homeostasis in mammalian cells using high resolution imaging techniques.
Degree: PhD, Chemistry and Biochemistry, 2010, Georgia Tech
URL: http://hdl.handle.net/1853/41197
► The primary aim of the work presented in this thesis is to elucidate novel information regarding the uptake, storage, distributions, and functions of both copper…
(more)
▼ The primary aim of the work presented in this thesis is to elucidate novel information regarding the uptake, storage, distributions, and functions of both copper and zinc in mammalian cells by predominantly using a combination of the high resolution imaging modalities, synchrotron radiation X-ray fluorescence microscopy (SXRF) and standard fluorescence imaging. Results from studies using cell permeable, metal ion selective fluorescent probes suggested the presence of labile pools of copper and zinc localized within the mitochondria and Golgi apparatus. Furthermore, SXRF imaging of a cell line defective in the copper transporter, Atox1, revealed intriguing differences in the Cu distribution of Atox1-/- cells compared to the corresponding wild-type cells. Finally, spatially well-resolved SXRF elemental maps of single, adherent mouse cells revealed remarkable changes in the distributions of both zinc and copper as the cells progressed through the cell cycle. Taken together, findings suggested major roles for copper and zinc within a native biological setting.
Advisors/Committee Members: Christoph J. Fahrni (Committee Chair), Donald Doyle (Committee Member), Jake Soper (Committee Member), Nael A. McCarty (Committee Member), Uwe Bunz (Committee Member).
Subjects/Keywords: Microscopy; Imaging; Synchrotron based X-ray fluorescence; Copper; Zinc; Synchrotron radiation
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APA (6th Edition):
McRae, R. (2010). Investigating metal homeostasis in mammalian cells using high resolution imaging techniques. (Doctoral Dissertation). Georgia Tech. Retrieved from http://hdl.handle.net/1853/41197
Chicago Manual of Style (16th Edition):
McRae, Reagan. “Investigating metal homeostasis in mammalian cells using high resolution imaging techniques.” 2010. Doctoral Dissertation, Georgia Tech. Accessed January 16, 2021.
http://hdl.handle.net/1853/41197.
MLA Handbook (7th Edition):
McRae, Reagan. “Investigating metal homeostasis in mammalian cells using high resolution imaging techniques.” 2010. Web. 16 Jan 2021.
Vancouver:
McRae R. Investigating metal homeostasis in mammalian cells using high resolution imaging techniques. [Internet] [Doctoral dissertation]. Georgia Tech; 2010. [cited 2021 Jan 16].
Available from: http://hdl.handle.net/1853/41197.
Council of Science Editors:
McRae R. Investigating metal homeostasis in mammalian cells using high resolution imaging techniques. [Doctoral Dissertation]. Georgia Tech; 2010. Available from: http://hdl.handle.net/1853/41197
Georgia Tech
3.
Jenson, David L. Jenson.
Proton-coupled electron transfer and tyrosine D of phototsystem II.
Degree: PhD, Chemistry and Biochemistry, 2009, Georgia Tech
URL: http://hdl.handle.net/1853/29667
► EPR spectroscopy and isotopic substitution were used to gain increased knowledge about the proton-coupled electron transfer (PCET) mechanism for the reduction of the tyrosine D…
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▼ EPR spectroscopy and isotopic substitution were used to gain increased knowledge about the proton-coupled electron transfer (PCET) mechanism for the reduction of the tyrosine D radical (YD*) in photosystem II. pL dependence (where pL is either pH or pD) of both the rate constant and kinetic isotope effect (KIE) was examined for YD* reduction. Second, the manner in which protons are transferred during the rate-limiting step for YD* reduction at alkaline pL was determined. Finally, high field electron paramagnetic resonance (EPR) spectroscopy was used to study the effect of pH on the environment surrounding both the tyrosine D radical and the tyrosine Z radical (YZ*).
At alkaline pL, it was determined that the proton and electron are both transferred in the rate-limiting step of YD* reduction. At acidic pL, the proton transfer occurs first followed by electron transfer. Proton inventory experiments indicate that there is more than one proton donation pathway available to YD* during PCET reduction at alkaline pL. Additionally, the proton inventory experiments indicate that at least one of those pathways is multiproton. High field EPR experiments indicate that both YD* and YZ* are hydrogen bonded to neutral species. The EPR gx component for YD* is invariant with respect to pH. Analysis of the EPR gx component for Yz* indicates that its environment becomes more electropositive as the pH is increased. This is most likely due to changes in the hydrogen bond strength
Advisors/Committee Members: Bridgette Barry (Committee Chair), Ingeborg Schmidt-Krey (Committee Member), Jake Soper (Committee Member), Nils Kroger (Committee Member), Wendy Kelly (Committee Member).
Subjects/Keywords: Photosynthesis; Photosystem II; Proton inventory; Tyrosine; Proton coupled electron transfer; Kinetic isotope effect; Histidine; Proton transfer reactions; Oxidation-reduction reaction; Tyrosine
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APA (6th Edition):
Jenson, D. L. J. (2009). Proton-coupled electron transfer and tyrosine D of phototsystem II. (Doctoral Dissertation). Georgia Tech. Retrieved from http://hdl.handle.net/1853/29667
Chicago Manual of Style (16th Edition):
Jenson, David L Jenson. “Proton-coupled electron transfer and tyrosine D of phototsystem II.” 2009. Doctoral Dissertation, Georgia Tech. Accessed January 16, 2021.
http://hdl.handle.net/1853/29667.
MLA Handbook (7th Edition):
Jenson, David L Jenson. “Proton-coupled electron transfer and tyrosine D of phototsystem II.” 2009. Web. 16 Jan 2021.
Vancouver:
Jenson DLJ. Proton-coupled electron transfer and tyrosine D of phototsystem II. [Internet] [Doctoral dissertation]. Georgia Tech; 2009. [cited 2021 Jan 16].
Available from: http://hdl.handle.net/1853/29667.
Council of Science Editors:
Jenson DLJ. Proton-coupled electron transfer and tyrosine D of phototsystem II. [Doctoral Dissertation]. Georgia Tech; 2009. Available from: http://hdl.handle.net/1853/29667
Georgia Tech
4.
Sibert, Robin S.
Redox active tyrosine residues in biomimetic beta hairpins.
Degree: PhD, Chemistry and Biochemistry, 2009, Georgia Tech
URL: http://hdl.handle.net/1853/29753
► Biomimetic peptides are autonomously folding secondary structural units designed to serve as models for examining processes that occur in proteins. Although de novo biomimetic peptides…
(more)
▼ Biomimetic peptides are autonomously folding secondary structural units designed to serve as models for examining processes that occur in proteins. Although de novo biomimetic peptides are not simply abbreviated versions of proteins already found in nature, designing biomimetic peptides does require an understanding of how native proteins are formed and stabilized. The discovery of autonomously folding fragments of ribonuclease A and tendamistat pioneered the use of biomimetic peptides for determining how the polypeptide sequence stabilizes formation of alpha helices and beta hairpins in aqueous and organic solutions. A set of rules for constructing stable alpha helices have now been established. There is no exact set of rules for designing beta hairpins; however, some factors that must be considered are the identity of the residues in the turn and non-covalent interactions between amino acid side chains. For example, glycine, proline, aspargine, and aspartic acid are favored in turns. Non-covalent interactions that stabilize hairpin formation include salt bridges, pi-stacked aromatic interactions, cation-pi interactions, and hydrophobic interactions. The optimal strand length for beta hairpins depends on the numbers of stabilizing non-covalent interactions and high hairpin propensity amino acids in the specific peptide being designed. Until now, de novo hairpins have not previously been used to examine biological processes aside from protein folding. This thesis uses de novo designed biomimetic peptides as tractable models to examine how non-covalent interactions control the redox properties of tyrosine in enzymes.
The data in this study demonstrate that proton transfer to histidine, a hydrogen bond to arginine, and a pi-cation interaction create a peptide environment that lowers the midpoint potential of tyrosine in beta hairpins. Moreover, these interactions contribute equally to control the midpoint potential. The data also show that hydrogen bonding is not the sole determinant of the midpoint potential of tyrosine. Finally, the data suggest that the Tyr 160D2-Arg 272CP47 pi-cation interaction contributes to the differences in redox properties between Tyr 160 and Tyr 161 of photosystem II.
Advisors/Committee Members: Bridgette Barry (Committee Chair), David Collard (Committee Member), Ingeborg Schmidt-Krey (Committee Member), Jake Soper (Committee Member), Mira Josowicz (Committee Member).
Subjects/Keywords: Midpoint potential; Tyrosine; Proton coupled electron transfer; Photosystem II; Tyrosine; Biomimetics; Peptides Synthesis
Record Details
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APA ·
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APA (6th Edition):
Sibert, R. S. (2009). Redox active tyrosine residues in biomimetic beta hairpins. (Doctoral Dissertation). Georgia Tech. Retrieved from http://hdl.handle.net/1853/29753
Chicago Manual of Style (16th Edition):
Sibert, Robin S. “Redox active tyrosine residues in biomimetic beta hairpins.” 2009. Doctoral Dissertation, Georgia Tech. Accessed January 16, 2021.
http://hdl.handle.net/1853/29753.
MLA Handbook (7th Edition):
Sibert, Robin S. “Redox active tyrosine residues in biomimetic beta hairpins.” 2009. Web. 16 Jan 2021.
Vancouver:
Sibert RS. Redox active tyrosine residues in biomimetic beta hairpins. [Internet] [Doctoral dissertation]. Georgia Tech; 2009. [cited 2021 Jan 16].
Available from: http://hdl.handle.net/1853/29753.
Council of Science Editors:
Sibert RS. Redox active tyrosine residues in biomimetic beta hairpins. [Doctoral Dissertation]. Georgia Tech; 2009. Available from: http://hdl.handle.net/1853/29753
. 
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