Document Type




Format of Original

11 p.

Publication Date



American Society for Biochemistry and Molecular Biology

Source Publication

Journal of Biological Chemistry

Source ISSN


Original Item ID

doi: 10.1074/jbc.275.18.13202


Direct oxidation of sulfite to sulfate occurs in various photo- and chemotrophic sulfur oxidizing microorganisms as the final step in the oxidation of reduced sulfur compounds and is catalyzed by sulfite:cytochrome c oxidoreductase (EC1.8.2.1). Here we show that the enzyme from Thiobacillus novellus is a periplasmically located αβ heterodimer, consisting of a 40.6-kDa subunit containing a molybdenum cofactor and an 8.8-kDa mono-heme cytochrome c 552 subunit (midpoint redox potential, E m8.0 = +280 mV). The organic component of the molybdenum cofactor was identified as molybdopterin contained in a 1:1 ratio to the Mo content of the enzyme. Electron paramagnetic resonance spectroscopy revealed the presence of a sulfite-inducible Mo(V) signal characteristic of sulfite:acceptor oxidoreductases. However, pH-dependent changes in the electron paramagnetic resonance signal were not detected. Kinetic studies showed that the enzyme exhibits a ping-pong mechanism involving two reactive sites. K m values for sulfite and cytochrome c 550 were determined to be 27 and 4 μm, respectively; the enzyme was found to be reversibly inhibited by sulfate and various buffer ions. The sorABgenes, which encode the enzyme, appear to form an operon, which is preceded by a putative extracytoplasmic function-type promoter and contains a hairpin loop termination structure downstream ofsorB. While SorA exhibits significant similarities to known sequences of eukaryotic and bacterial sulfite:acceptor oxidoreductases, SorB does not appear to be closely related to any knownc-type cytochromes.


Published version. Journal of Biological Chemistry, Vol. 275, No. 18 (May 5, 2000): 13202-13212. DOI. © 2000 by The American Society for Biochemistry and Molecular Biology, Inc. Used with permission.

Brian Bennett was affiliated with the CCLRC Daresbury Laboratory at the time of publication.

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