These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Luminescence from the carbon monoxide derivative of Agaricus bispora tyrosinase.
    Author: Kanagy C, Vanderkooi JM, Bonner WD.
    Journal: Arch Biochem Biophys; 1988 Dec; 267(2):668-75. PubMed ID: 2975158.
    Abstract:
    The luminescence of the CO adduct of two isozymic tyrosinases isolated from Agaricus bispora, an edible white mushroom, has been studied. At room temperature the emission appears as a single smooth peak centered at 530 nm with FWHM of 2700 cm-1 and a lifetime of 36 microseconds. The lifetime and wavelength of the emission are virtually unchanged on lowering the temperature from 298 to 77 degrees K. Solvent composition affects the wavelength of emission minimally. The emission is quenched by oxygen but not by a series of substrate analogs, inhibitors, or Lewis bases. The emission further appeared independent of aggregation state of the enzyme or isozyme type. A comparison of these data is made with those obtained by other researchers for the tyrosinase from Neurospora crassa and for several hemocyanins. The comparison supports the hypothesis that regulation of enzymatic activity does not take place within the coordination sphere of the copper atom observed. In addition, it suggests that the 550- to 560-nm emissions previously observed may not be considered characteristic of all CO derivatives of coupled binuclear copper proteins.
    [Abstract] [Full Text] [Related] [New Search]