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Oxygen‐Induced Inactivation of NADH‐Oxidase in Lyophilized Cells of Escherichia Coli
Author(s) -
Lion M. B.,
AviDor Y.
Publication year - 1963
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.196300046
Subject(s) - chemistry , escherichia coli , flavin group , oxygen , oxidase test , enzyme , biochemistry , bacteria , liberation , in vitro , organic chemistry , genetics , biology , gene
NADH‐oxidase of Escherichia coli was inactivated when freeze‐dried cells were exposed to oxygen (air). A similar loss in the activity of the enzyme occurred also when a cell‐free extract was lyophilized and then exposed to oxygen. Inactivation of the enzyme was accompanied by liberation of a substance showing flavin‐like fluorescence. Addition of KNO 2 to the medium before lyophilization suppressed the adverse effect of oxygen both on the viability of the bacteria and on the NADH‐oxidase activity. The possible significance of these findings is discussed.

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