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SUMMARY:High-Field EPR on Oxalate Decarboxylase\, and New Applications for
  EPR
DTSTART:20110707T160000
DTSTAMP:20260916T050606Z
UID:aa6ae415e1797dd681d687108bda8356eafc30ce8ef7723192bb56a1
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Alex Angerhofer\, University of Florida\nOxalate decarbo
 xylase (OxDC) is a Mn-dependent bicupin enzyme which catalyzes the redox-n
 eutral heterolytic carbon-carbon cleavage of the protonated oxalate monoan
 ion. \nOur goal is to elucidate the\nenzymatic mechanism that causes this 
 difficult reaction. One of the important questions is the location of the 
 active site near either the N- or the C-terminal location of the\nMn(II) i
 ons. We are using a multifrequency approach (including very high fields) t
 o the EPR of the Mn(II) sites to distinguish them spectroscopically\, coup
 led with site-directed mutants that allow us to identify the location of t
 he spectroscopic sites. This approach is coupled with other EPR techniques
  such as electron nuclear double resonance (ENDOR) and spin trapping. We a
 lso employ mass spectrometric tools such as membrane-inlet mass spectromet
 ry (MIMS) to follow the kinetics of gas production and consumption.\nResul
 ts will be presented that support the N-terminal site as the active site o
 f the enzyme and a flexible protein loop as the gate-keeper for substrate 
 trafficking.\nThe presentation will also touch on new applications of EPR 
 using microscopic resonators that are currently being developed.
LOCATION:BM6204
STATUS:CONFIRMED
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