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BEGIN:VEVENT

CATEGORIES:Natural Sciences
CATEGORIES:Lectures/Conferences
CATEGORIES:Utilities
CATEGORIES:Lecture/Talk
CATEGORIES:Main
CONTACT;X-BEDEWORK-UID=00f1fcdb-0f068baf-010f-068baf83-00000004:None
CREATED:20230827T191648Z
DESCRIPTION:The Department of Chemistry is excited to host R. David Britt 
 (UC Davis)\nTo learn more about the Britt lab's work\, please visit their
  research page: http://brittepr.ucdavis.edu/ \n\n\nEPR Studies of the Enz
 ymatic Synthesis of the Organometallic H-Cluster of [FeFe] Hydrogenase\n\
 nThe [FeFe] hydrogenase enzymes are well suited to H2 formation\, produci
 ng up to 10000 H2 molecules per second\, and have therefore generated muc
 h interest for renewable energy applications.  The H-cluster consists of 
 a binuclear [2Fe]H subcluster which is linked via a bridging cysteine to 
 a [4Fe-4S]H cluster. This [2Fe]H subcluster contains the organometallic e
 lements of the H-cluster:  the two irons each have a CO and a CN- termina
 l ligand and are bridged by a third CO and a unique SCH2NHCH2S azadithiol
 ate (adt) moiety. The H+ and H2 substrates are proposed to bind to and re
 act at this [2Fe]H unit. In addition to the relative rarity of enzymes ca
 rrying out organometallic reactions\, biosynthesis of the H-cluster poise
 s some specific challenges. Of course\, free CO and CN- molecules are tox
 ic. In addition\, the bridging adt moiety is known to be unstable in solu
 tion. The H-cluster biosynthesis is performed by a set of three "maturase
 " proteins\, HydE\, HydF\, and HydG\, each containing Fe-S clusters. Two 
 of these\, HydE and HydG\, are members of the radical SAM superfamily of 
 enzymes\, while HydF is a GTPase. Our approach to developing a viable mec
 hanistic proposal for H-cluster synthesis includes chemical biology techn
 iques such as cell free synthesis\, isotope sensitive spectroscopy such a
 s electron paramagnetic resonance\, and the use of synthetic clusters tha
 t can serve as functional substitutes for enzyme intermediates.\n\nHosted
  by David Beratan
DURATION:PT1H
DTSTAMP:20230925T205357Z
DTSTART;TZID=America/New_York:20231030T114000
LAST-MODIFIED:20230925T205357Z
LOCATION;X-BEDEWORK-UID=18832edc-1b27e154-011b-28282e22-00000037:French Fa
 mily Science Center 2237
STATUS:CONFIRMED
SUMMARY:Chemistry Seminar Presented by Prof. R. David Britt: EPR Studies o
 f the Enzymatic Synthesis of the Organometallic H-Cluster of [FeFe] Hydro
 genase
UID:CAL-8a02906b-8a0a73d8-018a-386d6907-00006a79demobedework@mysite.edu
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 c-user/Topics/Natural Sciences
X-BEDEWORK-STUDENT-CONTACT;X-BEDEWORK-PARAM-EMAIL=chem-office@duke.edu:Che
 m Admin Office
X-BEDEWORK-SPEAKER:R. David Britt\, University of California\, Davis
X-BEDEWORK-IMAGE-X1:134
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X-BEDEWORK-IMAGE-ALT-TEXT:Dave Britt
X-BEDEWORK-SUBMITTEDBY:lao26 for Chemistry (agrp_ArtsandSciences_Chemistry
 )
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