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DTSTART;TZID=America/Los_Angeles:20210203T160000
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DTSTAMP:20260618T165952
CREATED:20210107T222555Z
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UID:13415-1612368000-1612368000@www.chemistry.ucla.edu
SUMMARY:Special Bio-Inorganic Chemistry Seminar
DESCRIPTION:“Structural Evidence for Dynamic Nitrogenase Metalloclusters” \nAbstract: Nitrogenase catalyzes dinitrogen reduction to ammonia and is the only enzyme capable of supplying the world with a reduced form of ‘N’ that can be directly incorporated into biomolecules such as DNA and proteins. The most well-studied nitrogenase\, molybdenum nitrogenase\, consists of two component proteins\, the Fe protein (a homodimer with a 4Fe4S cluster) and the MoFe protein (a heterotetramer with two complex metalloclusters per heterodimer). During catalysis\, the two proteins associate\, allowing ATP-dependent electron transfer from the Fe protein to the MoFe protein. In the as-isolated state\, the MoFe protein active site (FeMo-cofactor) has an overall composition of [7Fe:9S:1C:1Mo]-R-homocitrate. This form of the FeMo-cofactor does not bind substrate and requires activation (by the Fe protein) prior to substrate binding. As a result\, only recently have ligand bound states of the protein bound FeMo-cofactor been crystallographically determined. Selenium can function as a sulfur-surrogate\, exchanging with labile sulfide groups under various conditions\, resulting in Se-incorporated metalloclusters. In my talk\, I will present crystallographic evidence for Se-incorporation into the nitrogenase metalloclusters and discuss the mechanistic implications of these findings.
URL:https://www.chemistry.ucla.edu/seminars/special-bio-inorganic-chemistry-seminar-5/
CATEGORIES:Other,Seminars
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