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Formation of methemoglobin and metmyoglobin using 8‐aminoquinoline derivatives or sodium nitrite and subsequent reaction with cyanide
Author(s) -
Steinhaus Ralph K.,
Baskin Steven I.,
Clark James H.,
Kirby Stephen D.
Publication year - 1990
Publication title -
journal of applied toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.784
H-Index - 87
eISSN - 1099-1263
pISSN - 0260-437X
DOI - 10.1002/jat.2550100507
Subject(s) - chemistry , metmyoglobin , methemoglobin , sodium nitrite , medicinal chemistry , myoglobin , reaction rate constant , sodium dithionite , autocatalysis , nitrite , potassium cyanide , hemoglobin , quinoline , inorganic chemistry , cyanide , catalysis , kinetics , organic chemistry , physics , quantum mechanics , nitrate
The kinetics of the oxidation of hemoglobin (Hb) and myoglobin (Mb) by sodium nitrite, 8‐[(4‐amino‐1‐methylbutyl)amino]‐6‐methoxy‐quinoline diphosphate (primaquine), 6‐methoxy‐8‐(6‐diethvlaminohexylamino)‐4‐meihyl‐quinoline dihydrochloride (WR6026) and 8‐[(4‐amino‐1‐methylbutyl)amino]‐2,6‐diniethoxy‐4‐methyl‐5‐[(3‐trifluoromethyl)phenoxy]quinoline succinate (WR238,605) were studied at pH values ranging from 7.4 to 7.6 and at 37 ± 1°C. The reaction between Hb and primaquine, WR6026 and WR238,605 resulted in precipitation, as did the reaction between Mb and WR238,605. The reaction between nitrite ion (NO 2 − ) and Hb showed a lag period followed by an autocatalytic phase. The data in this study are consistent with and substantiate the proposed mechanism for the Hb–NO 2 − oxidation reaction. The reaction between Mb and NO 2 − at higher NO 2 − concentrations also showed a lag period followed by an autocatalytic period, while at lower NO 2 − concentrations no lag period was seen. The data suggest a shift in rate constant at these lower NO 2 − concentrations. The reaction between Mb and both WR6026 and primaquine followed a two‐term rate law with oxidant‐dependent and ‐independent terms. Concentration–effect curve data, along with these results, suggest the presence of a catalytic pathway. The rates of formation of cyanomethemoglobin and cyanometinyoglobin complexes from cyanide ion and methemoglobin (MHb) and metmyoglobin (MMb), respectively, were followed in the presence of the heme oxidants. The rate constants were all within a narrow range and suggest that complexation of cyanide by MHb and MMb is not affected by the presence of oxidants.