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Molecular mechanisms of biocatalytic desulfurization of fossil fuels

Nature Biotechnology volume 14, pages 1705–1709 (1996)Cite this article

Abstract

The development of biocatalytic desulfurization of petroleum fractions may allow its use in place of conventional hydrodesulfurization (HDS). Dibenzothiophene (DBT) is representative of a broad range of sulfur heterocycles found in petroleum that are recalcitrant to desulfurization via HDS. Rhodococcus sp. strain IGTS8 has the ability to convert DBT to 2-hydroxybiphenyl (HBP) with the release of inorganic sulfur. The conversion of DBT to HBP is catalyzed by a multienzyme pathway consisting of two mono-oxygenases and a desulfinase. The final reaction catalyzed by the desulfinase appears to be the rate limiting step in the pathway. Each of the enzymes has been purified to homogeneity and their kinetic and physical properties studied. Neither monooxygenase has a tightly bound cofactor and each requires an NADH-FMN oxidoreductase for activity. An NADH-FMN oxidoreductase has been purified from Rhodococcus and is a protein of approximately 25,000 molecular weight with no apparent sequence homology to any other protein in the databases. We describe a unique sulfur acquisition system that Rhodococcus uses to obtain sulfur from very stable heterocyclic molecules.

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  1. Kevin A. Gray: kagray@main.com

Authors and Affiliations

  1. Energy BioSystems Corporation, 4200 Research Forest Dr., The Woodlands, TX, 77381

    Kevin A. Gray, Olga S. Pogrebinsky, Gregory T. Mrachko, Lei Xi, Daniel J. Monticello & Charles H. Squires

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Gray, K., Pogrebinsky, O., Mrachko, G. et al. Molecular mechanisms of biocatalytic desulfurization of fossil fuels. Nat Biotechnol 14, 1705–1709 (1996). https://doi.org/10.1038/nbt1296-1705

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