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dc.contributor.authorde Oliveira, Jonas A.
dc.date.accessioned2015-09-08T01:37:52Z
dc.date.available2015-09-08T01:37:52Z
dc.date.issued2013-08
dc.identifier.urihttps://hdl.handle.net/2144/12980
dc.descriptionPoster presentation at REU Summer's End Research Symposium, 2013, by REU participant Jonas A, de Oliveira, MassBay Community College - Sean Elliott group, Evan Judd lab mentoren_US
dc.description.abstractM. tuberculosis possesses a sulfite reductase (MtsirA) that is over-expressed when the bacteria is in its dormant stage of infection. MtSirA catalyzes the six-electron reduction of sulfite to sulfide. Previous kinetic studies of MtsirA have used methyl viologen (MV), a chemical reductant, as an electron donor. The goal of this work is to purify and characterize a ferredoxin from M. tuberculosis (MtFd) and determine if MtFd can act as an electron donor to mtSirA, with the ultimate goal of using it as a more physiologically relevant electron donor in kinetic studies of mtSirA. We have found that that MtFd purifies without a cluster and must be chemically reconstituted. MtFd likely contains a [4Fe-4S] cluster, and may be able to donate electrons to mtSirA.en_US
dc.description.sponsorshipNSF-REUen_US
dc.language.isoen_USen_US
dc.rightsCC0 1.0 Universal*
dc.rights.urihttp://creativecommons.org/publicdomain/zero/1.0/
dc.title2013 REU Poster: Purification and Characterization of a Ferredoxin from Mycobacterium tuberculosisen_US
dc.typePresentationen_US


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