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    Covalent labelling of the protochlorophyllide oxidoreductase from etioplast membranes with (3H)N-phenylmaleimide

    Access Status
    Fulltext not available
    Authors
    Oliver, Richard
    Griffiths, W.
    Date
    1981
    Type
    Journal Article
    
    Metadata
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    Citation
    OLIVER RP & GRIFFITHS WT (1981) Covalent labelling of the protochlorophyllide oxidoreductase from etioplast membranes with (3H)N-phenylmaleimide. Biochemical Journal 195 93-101
    Additional URLs
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1162858/?tool=pubmed
    Faculty
    Department of Environmental & Agriculture
    School of Agriculture and Environment
    Faculty of Science and Engineering
    Remarks

    A copy of this item may be available from Professor Richard Oliver

    Email: Richard.oliver@curtin.edu.au

    URI
    http://hdl.handle.net/20.500.11937/21703
    Collection
    • Curtin Research Publications
    Abstract

    [3H]N-Phenylmaleimide has been used to covalently label in a specific manner the substrate-protected thiol groups of the enzyme protochlorophyllide reductase. In membrane preparations from oat (Avena sativa) and runner-bean (Phaseolus vulgaris) seedlings, two related peptides of mol.wts. 35000/37000 and 34000/35000 respectively and showing properties expected of the reductase have been identified, whereas the same technique with barley (Hordeum vulgare) extracts resulted in labelling a single peptide of mol.wt. 38000. Evidence is presented that both NADPH and protochlorophyllide are required for protection of the essential thiol groups on the reductase in oat extracts, a situation favouring a ternary complex as the structure for the photoactive enzyme--substrates intermediate.

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