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

Acknowledgements

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.

Once published, please let us know via an email to umn-btc@umn.edu.

Schedule | Location: 1-123 Nils Hasselmo Hall