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Originally published In Press as doi:10.1074/jbc.M503492200 on July 27, 2005
J. Biol. Chem., Vol. 280, Issue 46, 38776-38786, November 18, 2005
A New Type of Sulfite Reductase, a Novel Coenzyme F420-dependent Enzyme, from the Methanarchaeon Methanocaldococcus jannaschii*
Eric F. Johnson and
Biswarup Mukhopadhyay ¶1
From the
Virginia Bioinformatics Institute and Departments of Biochemistry and ¶Biology, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061
Methanocaldococcus jannaschii is a hypertheromphilic, strictly hydrogenotrophic, methanogenic archaeon of ancient lineage isolated from a deep-sea hydrothermal vent. It requires sulfide for growth. Sulfite is inhibitory to the methanogens. Yet, we observed that M. jannaschii grows and produces methane with sulfite as the sole sulfur source. We found that in this organism sulfite induces a novel, highly active, coenzyme F420-dependent sulfite reductase (Fsr) with a cell extract specific activity of 0.57 µmol sulfite reduced min-1 mg-1 protein. The cellular level of Fsr protein is comparable to that of methyl-coenzyme M reductase, an enzyme essential for methanogenesis and a possible target for sulfite. Purified Fsr reduces sulfite to sulfide using reduced F420 (H2F420) as the electron source (Km: sulfite, 12 µM; H2F420, 21 µM). Therefore, Fsr provides M. jannaschii an anabolic ability and protection from sulfite toxicity. The N-terminal half of the 70-kDa Fsr polypeptide represents a H2F420 dehydrogenase and the C-terminal half a dissimilatory-type siroheme sulfite reductase, and Fsr catalyzes the corresponding partial reactions. Previously described sulfite reductases use nicotinamides and cytochromes as electron carriers. Therefore, this is the first report of a coenzyme F420-dependent sulfite reductase. Fsr homologs were found only in Methanopyrus kandleri and Methanothermobacter thermautotrophicus, two strictly hydrogenotrophic thermophilic methanogens. fsr is the likely ancestor of H2F420 dehydrogenases, which serve as electron input units for membrane-based energy transduction systems of certain late evolving archaea, and dissimilatory sulfite reductases of bacteria and archaea. fsr could also have arisen from lateral gene transfer and gene fusion events.
Received for publication, March 30, 2005
, and in revised form, July 18, 2005.
* This work was supported by a start-up fund (to B. M.) from the Virginia Bioinformatics Institute, Virginia Polytechnic and State University. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The on-line version of this article (available at http://www.jbc.org) contains supplemental Table 1S.
1 To whom correspondence should be addressed: Virginia Bioinformatics Institute, Bioinformatics I, Virginia Polytechnic Institute and State University, 0477 Washington St., Blacksburg, VA 24061. Tel.: 540-231-8015; Fax: 540-231-2606; E-mail: biswarup{at}vt.edu.

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Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.
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