Iron reductase activity in cowpea Rhizobium GN1 (peanut isolate)

Cell-free extracts of cowpea Rhizobium GN1 (peanut isolate) possessed reductase activity towards various ferric siderophores including its own. This activity was heat- and O2-sensitive and required NADH and flavins. Whereas NADPH could replace NADH with half-efficiency, succinate could not serve as...

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Bibliographic Details
Published in:World journal of microbiology & biotechnology 1997-05, Vol.13 (3), p.347-348
Main Authors: Jadhav, Rs, Desai, A
Format: Article
Language:English
Subjects:
Arachis hypogaea
Enzymes
Nitrates
Rhizobium
Rotenone
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Summary:Cell-free extracts of cowpea Rhizobium GN1 (peanut isolate) possessed reductase activity towards various ferric siderophores including its own. This activity was heat- and O2-sensitive and required NADH and flavins. Whereas NADPH could replace NADH with half-efficiency, succinate could not serve as reductant. Activity was insensitive to antimycin A and rotenone but was completely inhibited by HgCl2 (1 mM). Mg2+ (1 mM) enhanced reductase activity but Zn2+ and Cu2+ at the same concentration were inhibitory. The enzyme was located in the periplasmic fraction.[PUBLICATION ABSTRACT]
ISSN:0959-3993
1573-0972
DOI:10.1023/A:1018599411148