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Johansson, M.W., Holmblad, T., Thornqvist, P.-O., Cammarata, M., Parrinello, N. and Soderhall, K. (1999) A Cell-Surface Superoxide Dismutase Is a Binding Protein for Peroxinectin, a Cell-Adhesive Peroxidase in Crayfish. Journal of Cell Science, 112, 917-925.

has been cited by the following article:

• TITLE: Differential Regulation of Proteins and a Possible Role for Manganese Superoxide Dismutase in Bioluminescence of Panellus stipticus Revealed by Suppression Subtractive Hybridization

  AUTHORS: Galina A. Vydryakova, John Bissett

  KEYWORDS: Panellus stipticus, Mushroom Bioluminescence, Suppression Subtractive Hybridization, Manganese Superoxide Dismutase

  JOURNAL NAME: Advances in Microbiology, Vol.6 No.9, August 2, 2016

  ABSTRACT: Suppression subtractive hybridization (SSH) was employed to investigate bioluminescence in Panellus stipticus (Bull.) P. Karst. by detecting proteins differentially expressed in bioluminescent and luminescent strains. Comparisons of luminescent and non-luminescent monokaryon cultures of North American strains revealed differences in transcript levels of proteins responsible for post-translational modification (PTM) of enzymes. A similar comparison of a luminescent strain of P. stipticus from North America with a non-luminescent European strain revealed the presence of extracellular manganese superoxide dismutase (MnSOD) in the luminescent form, in addition to proteins involved in PTM. The application of MnSOD-specific inhibitors to luminescent mycelium resulted in the rapid loss of luminescence. The relevance to luminescence of proteins involved in PTM is discussed, together with a possible role for MnSOD that considers the potential for SODs to form stable complexes with catechols revealed in previously published research. In light of the recent discovery that hispidine may be the precursor of fungal luciferin, we consider a hypothetical mechanism for fungal luminescence in which the ο-hydroquinone moiety of a hispidine derivative ligates with the extracellular form of MnSOD producing a semiquinone-radical complex, with the resultant semiquinonato complex potentially reacting with molecular oxygen or other reactive oxygen species to produce sufficiently excited intermediates to emit light on relaxation.