An assessment of the role of intracellular reductive capacity in the biological clearance of triarylmethane dyes

Tacal O., Oezer I.

JOURNAL OF HAZARDOUS MATERIALS, cilt.149, sa.2, ss.518-522, 2007 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 149 Sayı: 2
  • Basım Tarihi: 2007
  • Doi Numarası: 10.1016/j.jhazmat.2007.08.022
  • Dergi Adı: JOURNAL OF HAZARDOUS MATERIALS
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.518-522
  • Anahtar Kelimeler: malachite green, methyl green, pararosaniline, triarylmethane reductase, thiol adduct, MALACHITE GREEN, GENTIAN-VIOLET, TRIPHENYLMETHANE, INHIBITION, PROTEIN, METABOLISM, MECHANISM, RATS, DNA
  • Hacettepe Üniversitesi Adresli: Evet

Özet

The second-order rate constants (at pH 7, 25 degrees C for the reduction of three cationic triarylmethane dyes [pararosaniline (PR+), malachite green (MG(+)), methyl green (MeG(+))] by NADH were 1.4 x 10(-2) to 6.7 x 10(-2) mM(-1) min(-1). Based on these values the intracellular nonenzymatic reduction of TAM(+) to TAM-H by endogenous NADH was estimated to proceed with an average half-life of 30 min. Rapid and significant adduct formation was observed with the thiol, 3-mercaptopropionic acid (MPA), suggesting that the primary intracellular form of the dyes must be a thiol adduct and that the conversion to adduct form takes place within ms-s. These time frames, when compared to the min-h time frame for microbial clearance of triarylmethanes from culture media, suggest that transport must be the rate-limiting step in nonadsorptive (chemical) clearance of the dyes and that the presence of enzymes to complement the nonenzymatic reductive and adduct-forming activities cited serves a kinetically limited purpose. It appears that a superior catalytic scavenger will be one with a superior transport capacity. (c) 2007 Elsevier B.V. All rights reserved.