Inactivation of lyophilized DPNH dehydrogenase from Escherichia coli by oxygen

M. Gutman; A. Schejter; Y. Avi-Dor

doi:10.1016/0005-2728(69)90142-X

Inactivation of lyophilized DPNH dehydrogenase from Escherichia coli by oxygen

M. Gutman^*, A. Schejter, Y. Avi-Dor

^*Corresponding author for this work

Biochemistry Molecular Biology

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2 Scopus citations

Abstract

Lyophilized Escherichia coli membranes lose 50% of their DPNH oxidase activity when exposed to O₂. The oxidation of succinate or lactate is not affected by this treatment. The enzyme damaged by O₂ is the membrane DPNH dehydrogenase (DPNH-ferricyanide oxidoreductase, EC 1.6.99.3). The K_m values for DPNH and the electron acceptor K₃Fe(CN)₆ are the same in the native and the inactivated enzyme. The v_max of the latter is decreased by 50% for both substrates. The accessibility of non-heme iron to o-phenanthroline is partly increased. It is suggested that the non-heme iron of DPNH dehydrogenase participates in intramolecular electron conductance between the oxidizing and the reducing sites of the enzyme.

Original language	English
Pages (from-to)	462-466
Number of pages	5
Journal	Biochimica et Biophysica Acta - Bioenergetics
Volume	172
Issue number	3
DOIs	https://doi.org/10.1016/0005-2728(69)90142-X
State	Published - 8 Apr 1969

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title = "Inactivation of lyophilized DPNH dehydrogenase from Escherichia coli by oxygen",

abstract = "Lyophilized Escherichia coli membranes lose 50% of their DPNH oxidase activity when exposed to O2. The oxidation of succinate or lactate is not affected by this treatment. The enzyme damaged by O2 is the membrane DPNH dehydrogenase (DPNH-ferricyanide oxidoreductase, EC 1.6.99.3). The Km values for DPNH and the electron acceptor K3Fe(CN)6 are the same in the native and the inactivated enzyme. The vmax of the latter is decreased by 50% for both substrates. The accessibility of non-heme iron to o-phenanthroline is partly increased. It is suggested that the non-heme iron of DPNH dehydrogenase participates in intramolecular electron conductance between the oxidizing and the reducing sites of the enzyme.",

author = "M. Gutman and A. Schejter and Y. Avi-Dor",

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doi = "10.1016/0005-2728(69)90142-X",

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T1 - Inactivation of lyophilized DPNH dehydrogenase from Escherichia coli by oxygen

AU - Gutman, M.

AU - Schejter, A.

AU - Avi-Dor, Y.

PY - 1969/4/8

Y1 - 1969/4/8

N2 - Lyophilized Escherichia coli membranes lose 50% of their DPNH oxidase activity when exposed to O2. The oxidation of succinate or lactate is not affected by this treatment. The enzyme damaged by O2 is the membrane DPNH dehydrogenase (DPNH-ferricyanide oxidoreductase, EC 1.6.99.3). The Km values for DPNH and the electron acceptor K3Fe(CN)6 are the same in the native and the inactivated enzyme. The vmax of the latter is decreased by 50% for both substrates. The accessibility of non-heme iron to o-phenanthroline is partly increased. It is suggested that the non-heme iron of DPNH dehydrogenase participates in intramolecular electron conductance between the oxidizing and the reducing sites of the enzyme.

AB - Lyophilized Escherichia coli membranes lose 50% of their DPNH oxidase activity when exposed to O2. The oxidation of succinate or lactate is not affected by this treatment. The enzyme damaged by O2 is the membrane DPNH dehydrogenase (DPNH-ferricyanide oxidoreductase, EC 1.6.99.3). The Km values for DPNH and the electron acceptor K3Fe(CN)6 are the same in the native and the inactivated enzyme. The vmax of the latter is decreased by 50% for both substrates. The accessibility of non-heme iron to o-phenanthroline is partly increased. It is suggested that the non-heme iron of DPNH dehydrogenase participates in intramolecular electron conductance between the oxidizing and the reducing sites of the enzyme.

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Inactivation of lyophilized DPNH dehydrogenase from Escherichia coli by oxygen

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