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• W1983015946 abstract "The cytochrome “a1” or P-428, previously proposed to be a high affinity terminal oxidase in nitrogen-fixing bacteroids of Bradyrhizobium japonicum has been purified. The water-soluble native hemoprotein has an Mr of 136 000, lacks heme a and is a high-spin ferric protohemoprotein: It is slowly reduced with dithionite to give a species with an optical spectrum like that of hemoprotein b-590 (Escherichia coli; peak at 555 nm, shoulder at 590 nm), and which reacts slowly with CO. It has catalase and peroxidase activities, again resembling the E. colib-590. Neither hemoprotein forms a stable oxy complex under conditions in which dithionite-reduced horseradish per-oxidase reacts with oxygen to form such a complex. The hemoprotein, which we name hemoprotein, b-590 (Bradyrhizobium japonicum, may play a role in removal of peroxides generated during respiration in the bacteroids of several Rhizobium and Bradyrhizobium species. The high-affinity terminal oxidase under nitrogen-fixing conditions remains to be identified." @default.
• W1983015946 created "2016-06-24" @default.
• W1983015946 creator A5008614222 @default.
• W1983015946 creator A5064853377 @default.
• W1983015946 date "1991-03-01" @default.
• W1983015946 modified "2023-10-11" @default.
• W1983015946 title "Characterization of a soluble catalase-peroxidase hemoprotein<i>b</i>-590, previously identified as ‘cytochrome<i>a</i>₁’ from<i>Bradyrhizobium japonicum</i>bacteroids" @default.
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• W1983015946 doi "https://doi.org/10.1111/j.1574-6968.1991.tb04464.x" @default.
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