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1251 Wescoe Hall Drive B033 Malott Hall University of Kansas Lawrence, KS 66045 Phone: (785) 864-3968 Fax: (785) 864-5396 Email: taj@ku.edu |
Bioinorganic Chemistry, Biomimetic Chemistry, Biophysical Chemistry
Nature uses metalloenzymes containing Mn, Fe, or Cu and oxidants such as molecular oxygen and hydrogen peroxide to carry out remarkable oxidative transformations that are both vital for life and fascinating from a fundamental perspective. The study of such transformations lies at the heart of bioinorganic chemistry. Our research focuses on unraveling the reactivity of manganese-dependent enzymes that catalyze oxidative degradation reactions using molecular oxygen or hydrogen peroxide as oxidants. These reactions also provide the inspiration for our synthetic projects, which include the design of small molecule bleaching catalysts for use in fabric and/or textile applications.
Our laboratory uses a combination of i) reactivity studies of metal ion complexes and enzymes, ii) detailed spectroscopic characterization of transition metal species, particularly unstable intermediates that cannot be characterized using X–ray crystallographic methods, and iii) computational chemistry (see scheme). Spectroscopic methods used in our research include electronic absorption (UV-vis), electron paramagnetic resonance (EPR), and magnetic circular dichroism (MCD) spectroscopies. These tools are particularly powerful when used in conjunction with computational methods, as they permit the characterization of the geometric and electronic structures of fleeting intermediates too unstable to be characterized using standard crystallographic methods. By applying this three-pronged approach to both metalloenzymes and transition metal complexes, we will gain detailed insight into how nature uses molecular oxygen and manganese to oxidize substrates and develop transition metal complexes that can perform “green” oxidation reactions.
Klinker, E. J.; Jackson, T. A.; Jensen, M. P.; Juhasz, G.; Münck, E.; Que, L., Jr. A Tosylimido Analogue of an Oxoiron(IV) Complex. Angew. Chem. Int. Ed. 2006, 45, 7394-7397.
Jackson, T. A.; Que, L., Jr. “Structural and Functional Models for Oxygen-Activating Nonheme Iron Enzymes” In Concepts and Models in Bioinorganic Chemistry; Kraatz, H.-B., Metzler-Nolte, N., Eds.; Wiley-VCH: Weinheim, 2006.
Jackson, T. A.; Karapetian, A.; Miller, A.-F.; Brunold, T. C. Probing the Geometric and Electronic Structures of the Low Temperature Azide Adduct of Oxidized Manganese Superoxide Dismutase and the Product-Inhibited Complex. Biochemistry 2005, 44, 1504-1520.
Jackson, T. A.; Karapetian, A.; Miller, A.-F.; Brunold, T. C. Spectroscopic and Computational Studies of the Azide-Adduct of Manganese Superoxide Dismutase: Definitive Assignment of the Ligand Responsible for the Low-Temperature Thermochromism. J. Am. Chem. Soc. 2004, 126, 12477-12491.
Jackson, T. A.; Brunold, T. C. Combined Spectroscopic / Computational Studies on Fe- and Mn-Dependent Superoxide Dismutases: Insights into Second-Sphere Tuning of Active-Site Properties. Acc. Chem. Res. 2004, 37, 461-470.
Jackson, T. A.; Yikilmaz, E.; Miller, A.-F.; Brunold, T. C. Spectroscopic and Computational Study of a Non-Heme Iron {Fe-NO}7 System: Exploring the Geometric and Electronic Structures of the Nitrosyl Adduct of Iron Superoxide Dismutase. J. Am. Chem. Soc. 2003, 125, 8348-8363.
Jackson, T. A.; Xie, J.; Yikilmaz, E.; Miller, A.-F.; Brunold, T. C. Spectroscopic and Computational Studies on Iron and Manganese Superoxide Dismutases: Nature of the Chemical Events Associated with Active Site pKs. J. Am. Chem. Soc. 2002, 124, 10833-10845.
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