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SUMMARY:Electrostatically Gated Enzyme Dynamics During Catalysis
DTSTART;VALUE=DATE-TIME:20250922T143000Z
DTEND;VALUE=DATE-TIME:20250922T150000Z
DTSTAMP;VALUE=DATE-TIME:20260525T195619Z
UID:indico-contribution-1831@lindico453.srv.lu.se
DESCRIPTION:Speakers: Mark Wilson (University of Nebraska–Lincoln)\nAbst
 ract: Enzyme catalysis is essential for life and is a central phenomenon i
 n biochemistry. The advent of time-resolved serial crystallography\, initi
 ally enabled by X-ray free electron lasers (XFELs) and now expanding to sy
 nchrotron X-ray sources\, allows enzyme catalysis to be observed catalysis
  in real time\, in near-physiological conditions\, and at atomic resolutio
 n. I will describe our work using mix-and-inject serial crystallography (M
 ISC) to observe catalysis by isocyanide hydratase (ICH).  MISC allowed us 
 to observe formation of an unusual thioimidate intermediate and to watch I
 CH’s conformational dynamics respond to changes in active site ionizatio
 n during catalysis.  We also used an engineered ICH mutant to enrich for r
 are conformations during catalysis\, permitting a clearer view of later st
 eps in the reaction.  ICH exemplifies a class of enzymes whose non-equilib
 rium dynamics are gated by changes in active site electrostatics\, which i
 s a potentially common enzymological phenomenon.\n\nhttps://lindico453.srv
 .lu.se/event/583/contributions/1831/
LOCATION:LINXS at The Loop
URL:https://lindico453.srv.lu.se/event/583/contributions/1831/
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