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Inactivation of bacterial respiratory chain enzymes by singlet oxygen
Author(s) -
Tatsuzawa Hidetaka,
Maruyama Tadashi,
Misawa Norihiko,
Fujimori Ken,
Hori Kazutoshi,
Sano Yosiaki,
Kambayashi Yasuhiro,
Nakano Minoru
Publication year - 1998
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/s0014-5793(98)01397-0
Subject(s) - enzyme , escherichia coli , biochemistry , oxidase test , chemistry , microbiology and biotechnology , singlet oxygen , biology , oxygen , organic chemistry , gene
To distinguish the bactericidal action of singlet oxygen ( 1 O 2 ) from hypohalous acids, wild‐type and lycopene transformant E. coli strains were exposed to each of the oxidants and then bacterial viability was investigated. 1 O 2 was generated by chemical and enzymatic systems at pH 4.5. Exposure of wild‐type E. coli to 1 O 2 caused a significant loss of E. coli viability due to inactivation of membrane respiratory chain enzymes by 1 O 2 . This action of 1 O 2 could be attenuated by lycopene in the bacterial cell membrane. In the lycopene transformant strain of E. coli , inactivation of NADH oxidase and succinate oxidase by hypohalous acids were significantly suppressed, but E. coli viability was unaffected. Based on these findings, we suggest that phagocytic leukocytes produce 1 O 2 as a major bactericidal oxidant in the phagosome.