Nitrite causes reversible inactivation of nitrate reductase in the yeast Hansenula anornala

نویسندگان

  • Celedonio Gonzalez
  • Gregorio Gonzalez
  • Julio Avila
  • M. Dolores Perez
  • Nelida Brito
  • Jose M. Siverio
چکیده

Laguna, Tenerife, Canarias, Spain haemand Mo-dependent and Mo-dependent activities of nitrate reductase, determined with the non-physiological electron donors FMNH, and reduced methyl viologen respectively, were less affected. A similar inactivation was found with the proton ionophores 2,rddinitrophenol and carbonyl cyanide m-chlorophenylhydrazone. The inactive enzyme was found in the particulate fraction and cosedimented with the mitochondria1 fraction. When the NADPHdependent nitrate reductase activity was restored in vivo the enzyme was found in the soluble fraction. The inactivation of nitrate reductase by nitrite, 2,rddinitrophenol and carbonyl cyanide m-chlorophenylhydrazone was dependent on the external pH. The treatment of isolated mitochondria at alkaline pH with Triton X-100 solubilized about 30% of the inactive enzyme.

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تاریخ انتشار 2008