Premium
Mechanism of o ‐aminophenol metabolism in human erythrocytes
Author(s) -
Tomoda Akio,
Yamaguchi Jundo,
Kojima Hisanori,
Amemiya Hidemitsu,
Yoneyama Yoshimasa
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80211-3
Subject(s) - methemoglobin , chemistry , metabolism , intracellular , hemoglobin , ferrous , azide , sodium azide , cyanide , biochemistry , ferric , spectrophotometry , heme , chromatography , enzyme , inorganic chemistry , organic chemistry
o ‐Aminophenol was found to be rapidly metabolized to a brown compound in the presence of purified human oxy‐ and methemoglobin, coupled with the oxidation and reduction of these hemoglobins by o ‐amino‐phenol. The final product of o ‐aminophenol was identified as 2‐aminophenoxazine‐3‐one, by using spectrophotometry and HPLC. The metabolism of o ‐aminophenol was also observed in human erythrocytes. The production rates of 2‐aminophenoxazine‐3‐one in the cells were very fast, but these were strongly decreased by bubbling carbon monoxide into the cell suspension when intracellular hemoglobin was in the ferrous state. The production of 2‐aminophenoxazine‐3‐one from o ‐aminophenol in the cells was completely suppressed by cyanide and azide when intracellular hemoglobin was in the ferric state. These results suggest that oxy‐ and methemoglobin are involved in metabolism of o ‐aminophenol to 2‐aminophenoxazine‐3‐one in human erythrocytes.