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    Biochemistry. 1993 Dec 7;32(48):12955-8.

    The active site structure of the calcium-containing quinoprotein methanol dehydrogenase.

    White S, Boyd G, Mathews FS, Xia ZX, Dai WW, Zhang YF, Davidson VL.

    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110.

    Pyrroloquinoline quinone (PQQ), widely found in nature, serves as the redox cofactor in bacterial methanol dehydrogenase (MEDH), a heterotetrameric enzyme that oxidizes methanol to formaldehyde. The refined structure of MEDH at 2.4-A resolution, based on recently obtained amino acid sequence data, reveals that the PQQ, located in a central channel of the disk-shaped protein, is sandwiched between a Trp side chain and a very unusual vicinal disulfide. A Ca2+ ion forms a bridge between PQQ and the protein molecule, very close to a putative substrate binding pocket. The vicinal disulfide may form during PQQ incorporation and possibly act to hold the latter in place.

    PMID: 8241148 [PubMed - indexed for MEDLINE]

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