Bruker Elexsys continuous wave E500 low temperature Electron Paramagnetic Resonance Spectrometer
Bruker Elexsys continuous wave E500 low temperature Electron Paramagnetic Resonance Spectrometer

For study of:

  • metalloproteins and metalloenzymes, flavoenzymes 
  • radical-based enzymes 
  • organic radical species
  • bioinorganic inorganic model species
  • small molecule complexes designed to mimic the reactivity and/or structure of enzyme metal centers - mixed metal complexes that form covalent metal-metal bonds for novel catalysts and models for enzymes such as nitrogenase and hydrogenase

Equipped with:

  • 9 inch electromagnet
  • X-band (9GHz) and Q-band (35 GHz) microwave bridges
  • power-dependence studies 
  • ITC 503S temperature controller with VC-30 flow controller
  • variable temperature capability (2 K to 50 K) using liquid helium cooling 
  • Oxford ESR 910 cavity capable of perpendicular and parallel (integer spin species) data collection 
  • cavity can be light-irradiated
  • cavity can accept 4 mm OD / 23 cm quartz EPR tubes (cryogenic data collection) or capillary cells (room temperature data collection) 
  • full instrument digital upgrade (Nov 2018)
  • Linux workstation with Xepr EPR Software Package for data collection and analysis 

Select publications of instrument use

Integer-spin EPR studies of the fully reduced methane monooxygenase hydroxylase component. Michael P. Hendrich, Eckard Munck, Brian G. Fox, and John D. Lipscomb (1990) JACS 112:5861-5865

A family of diiron monooxygenases catalyzing amino acid beta-hydroxylation in antibiotic biosynthesis. Thomas M. Makris, Mrinmoy Chakrabarti, Eckard Münck, and John D. Lipscomb (2010) PNAS 107:15391-6

Trapping and spectroscopic characterization of an FeIII-superoxo intermediate from a nonheme mononuclear iron-containing enzyme. Mbughuni MM, Chakrabarti M, Hayden JA, Bominaar EL, Hendrich MP, Münck E, Lipscomb JD (2010) PNAS 107:16788-93

Simultaneous binding of nitric oxide and isotopically labeled substrates or inhibitors by reduced protocatechuate 3,4-dioxygenase. Orville AM, Lipscomb JD (1993) JBC 268:8596-607

Hydrogen peroxide dependent cis-dihydroxylation of benzoate by fully oxidized benzoate 1,2-dioxygenase. Neibergall MB, Stubna A, Mekmouche Y, Münck E, Lipscomb JD (2007) Biochemistry 46:8004-16

Salicylate 5-Hydroxylase: Intermediates in Aromatic Hydroxylation by a Rieske Monooxygenase. Rogers MS, Lipscomb JD (2019) Biochemistry 58:5305-5319

Equilibrating (L)FeIII-OOAc and (L)FeV(O) Species in Hydrocarbon Oxidations by Bio-Inspired Nonheme Iron Catalysts Using H2O2 and AcOH. Oloo WN, Banerjee R, Lipscomb JD, Que L Jr. (2017) JACS 139:17313-17326


The BTC should be acknowledged in any publications arising from the data analyzed in the BTC with the following text:

Experiments reported in this paper were performed at the Biophysical Technology Center, University of Minnesota Department of Biochemistry, Molecular Biology, and Biophysics.

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