2013 REU Poster: Purification and Characterization of a Ferredoxin from Mycobacterium tuberculosis
OA Version
Citation
Abstract
M. 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.
Description
Poster 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 mentor
License
CC0 1.0 Universal