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    Eur J Biochem. 1992 Apr 1;205(1):111-5.

    The third subunit of desulfoviridin-type dissimilatory sulfite reductases.

    Pierik AJ, Duyvis MG, van Helvoort JM, Wolbert RB, Hagen WR.

    Department of Biochemistry, Agricultural University, Wageningen, The Netherlands.

    In addition to the 50-kDa (alpha) and 40-kDa (beta) subunits, an 11-kDa polypeptide has been discovered in highly purified Desulfovibrio vulgaris (Hildenborough) dissimilatory sulfite reductase. This is in contrast with the hitherto generally accepted alpha 2 beta 2 tetrameric subunit composition. Purification, high-ionic-strength gel-filtration, native electrophoresis and isoelectric focussing do not result in dissociation of the 11-kDa polypeptide from the complex. Densitometric scanning of SDS gels and denaturing gel-filtration indicate a stoichiometric occurrence. A similar 11-kDa polypeptide is present in the desulfoviridin of D. vulgaris oxamicus (Monticello), D. gigas and D. desulfuricans ATCC 27774. We attribute an alpha 2 beta 2 gamma 2 subunit structure to desulfoviridin-type sulfite reductases. N-terminal sequences of the alpha, beta and gamma subunits are reported.

    PMID: 1555572 [PubMed - indexed for MEDLINE]

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