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2015 | 2 | 1 |

Article title

Functional investigation of Bacillus subtilis YrkF’s
involvement in sulfur transfer reactions


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Sulfur incorporation into the molybdenum
cofactor (Moco) in the Gram-negative bacterium
Escherichia coli involves six enzymes. The initial
reaction includes the cysteine desulfurase IscS, the
sulfurtransferase TusA, and the rhodanese domaincontaining
protein YnjE. The Gram-positive bacterium
Bacillus subtilis contains no direct homologs for IscS,
but rather four distinct cysteine desulfurases (YrvO, NifS,
NifZ, SufS) and YrkF, a two-domain rhodanese protein
with an N-terminal domain similar to TusA. Bioinformatic
analysis was used to identify potential enzymes involved
in the B. subtilis Moco thiolation pathway and in vitro
reactions demonstrated that YrkF can accept sulfur from
and enhance the activity of YrvO.








Physical description


20 - 1 - 2016
5 - 12 - 2015
6 - 8 - 2015


  • Department of Chemistry,
    Wake Forest University
  • Department of Chemistry,
    Wake Forest University
  • Wake Forest University,
    1834 Wake Forest Road, Winston Salem, North Carolina, 27106


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Publication order reference


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