In times of sulfur starvation, the two-component alkanesulfonate monooxygenase (SsuD/E) is expressed to attain sulfur from organosulfonated compounds. SsuE reduces flavin to its flavin reductase, FMNH2, which is expressed to SsuD. An alkanesulfonate is then oxidized to its corresponding aldehyde and sulfite in the presence of oxygen (O2). Molecular dynamics simulations have been carried out to examine the conformations of the SsuD system in the presence of reaction substrates. Multiple combinations of flavin cofactors (e.g., FMNH2 and C4a-peroxyflavin) and ligands (e.g., octanesulfonate) have been modeled into a reported crystal structure with a newly modeled loop region previously unresolved in the structure. Principal component analysis (PCA) has been used to identify the resultant interactions within the active site region. The role of a potential salt bridge between Arg297 and Asp111 or Glu20 in the �open� and �closed� active site conformations of the enzyme is discussed.

Investigating substrate-induced conformational changes in alkanesulfonate monooxygenase using molecular dynamics simulations

245th National Meeting (2013)

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