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Oxyleghemoglobin-mediated Hydrogen Oxidation by Rhizobium japonicum USDA 122 DES Bacteroids
Author(s) -
David W. Emerich,
Steve L. Albrecht,
Sterling A. Russell,
Temay Ching,
Harold J. Evans
Publication year - 1980
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.65.4.605
Subject(s) - oxidizing agent , chemistry , substrate (aquarium) , redox , rhizobium , endogeny , biochemistry , respiration , nitrogen fixation , biology , inorganic chemistry , botany , nitrogen , organic chemistry , ecology , gene
Oxyleghemoglobin was used to supply low concentrations of O(2) to H(2)-oxidizing bacteroids from Rhizobium japonicum USDA 122 DES. The H(2) oxidation system of these bacteroids was capable of effectively utilizing O(2) at the low concentrations of O(2) expected to be found in soybean nodules. Apparent K(m) values of approximately 10 nanomolar O(2) have been calculated for the oxyhydrogen reaction. These values include the K(m) values for both H(2) oxidation and endogenous substrate oxidation. Even in the presence of oxyleghemoglobin, H(2) additions stimulated C(2)H(2) reduction, reduced the rate of endogenous respiration and maintained the ATP contents of bacteroids. In our reconstituted oxyleghemoglobin and bacteriod system, we estimate that the H(2) oxidation system is capable of recycling all of the H(2) evolved during the N(2) fixation process.

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