Abstract

Inorganic sulfate is the preferred sulfur source for the growth of most microorganisms but, in its absence, many organosulfur compounds can be degraded microbially to provide sulfur. Desulfurization of dibenzothiophene (DBT) by Rhodococcus sp. and of aromatic sulfonates by Pseudomonas sp. has considerable biotechnological potential. Both these pathways require non-flavin-containing FMNH2-dependent monoxygenases (DszC/DszA and SsuD, respectively). FMNH2 is provided from the freely diffusible FMNH2 pool in the cell, and is replenished by specific NAD(P)H:FMN oxidoreductases (DszD and SsuE). Overexpression of the DszD FMN reductase in a heterologous system increases the efficiency of DBT desulfurization but is detrimental to cell growth at high levels. Expression of the sulfonatase that cleaves aromatic sulfonates (surfactants, dyes) is accompanied by synthesis of a thiol-specific antioxidant protein, which may protect the cell from superoxide radicals generated by autoxidation of the reduced flavin. Effective application of DBT desulfurization in the biodesulfurization of crude oil, and of arylsulfonate desulfonation in bioremediation, may require optimization of both flavin reductase levels and antioxidant protection systems within the cell.

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