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    Demonstration that CobG, the monooxygenase associated with the ring contraction process of the aerobic cobalamin (vitamin B12) biosynthetic pathway, contains an Fe-S center and a mononuclear non-heme iron center

    Access Status
    Open access via publisher
    Authors
    Schroeder, S.
    Lawrence, A.
    Biedendieck, R.
    Rose, R.
    Deery, E.
    Graham, Ross
    McLean, K.
    Munro, A.
    Rigby, S.
    Warren, M.
    Date
    2009
    Type
    Journal Article
    
    Metadata
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    Citation
    Schroeder, S. and Lawrence, A. and Biedendieck, R. and Rose, R. and Deery, E. and Graham, R. and McLean, K. et al. 2009. Demonstration that CobG, the monooxygenase associated with the ring contraction process of the aerobic cobalamin (vitamin B12) biosynthetic pathway, contains an Fe-S center and a mononuclear non-heme iron center. Journal of Biological Chemistry. 284 (8): pp. 4796-4805.
    Source Title
    Journal of Biological Chemistry
    DOI
    10.1074/jbc.M807184200
    ISSN
    0021-9258
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/31299
    Collection
    • Curtin Research Publications
    Abstract

    The ring contraction process that occurs during cobalamin (vitamin B12) biosynthesis is mediated via the action of two enzymes, CobG and CobJ. The first of these generates a tertiary alcohol at the C-20 position of precorrin-3A by functioning as a monooxygenase, a reaction that also forms a gamma lactone with the acetic acid side chain on ring A. The product, precorrin-3B, is then acted upon by CobJ, which methylates at the C-17 position and promotes ring contraction of the macrocycle by catalyzing a masked pinacol rearrangement. Here, we report the characterization of CobG enzymes from Pseudomonas denitrificans and Brucella melitensis. We show that both contain a [4Fe-4S] center as well as a mononuclear non-heme iron. Although both enzymes are active in vivo, the P. denitrificans enzyme was found to be inactive in vitro. Further analysis of this enzyme revealed that the mononuclear non-heme iron was not reducible, and it was concluded that it is rapidly inactivated once it is released from the bacterial cell. In contrast, the B. melitensis enzyme was found to be fully active in vitro and the mononuclear non-heme iron was reducible by dithionite. The reduced mononuclear non-heme was able to react with the oxygen analogue NO, but only in the presence of the substrate precorrin-3A. The cysteine residues responsible for binding the Fe-S center were identified by site-directed mutagenesis. A mechanism for CobG is presented. © 2009 by The American Society for Biochemistry and Molecular Biology, Inc.

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