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Dibenzothiophene (DBT) is a typical sulfur-containing compound found in fossil fuels. This compound and its derivatives are resistant to the hydrodesulfurization method often used in industry, but they are susceptible to enzymatic desulfurization via the 4S pathway, which is a well-studied biochemical pathway consisting of four enzymes. DBT monooxygenase (DszC) from Rhodococcus erythropolis is involved in the first step of the 4S pathway. We determined the crystal structure of DszC, which reveals that, in contrast to several homologous proteins, the C-terminus (410-417) of DszC participates in the stabilization of the substrate-binding pocket. Analytical ultracentrifugation analysis and enzymatic assays confirmed that the C-terminus is important for the stabilization of the active conformation of the substrate-binding pocket and the tetrameric state. Therefore, the C-terminus of DszC plays a significant role in the catalytic activity of this enzyme.

Original publication




Journal article



Publication Date





2733 - 2743


College of Life Sciences, Nankai University, Tianjin, China.


Rhodococcus, Thiophenes, Oxidoreductases, Bacterial Proteins, Recombinant Proteins, Ultracentrifugation, Crystallography, X-Ray, Amino Acid Substitution, Sequence Alignment, Enzyme Stability, Amino Acid Sequence, Catalytic Domain, Conserved Sequence, Protein Conformation, Sequence Homology, Amino Acid, Molecular Weight, Models, Molecular, Molecular Sequence Data, Databases, Protein, Mutant Proteins