Plant Physiol.
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Plant Physiology 61:748-752 (1978)
© 1978 American Society of Plant Biologists

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Nitrate Reductase and Soluble Cytochrome c Reductase(s) in Higher Plants 1

William Wallace2 and Christopher B. Johnson

Department of Physiology and Environmental Studies, School of Agriculture, University of Nottingham, Sutton Bonington, Loughborough, LE12 5RD England

The 4S cytochrome c (Cyt c) reductase activity of several plant species was markedly stimulated by cyanide and ferrocyanide but those of the 8S nitrate reductase component and other particulate components of the maize (Zea mays L.) scutellum by comparison, were increased only slightly. The effect of cyanide and ferrocyanide was not due to elimination of cytochrome oxidase interference but resulted from the stimulation of NADH-dependent reduction of Cyt c. A 4S Cyt c reductase component which could be isolated by ammonium sulfate fractionation and diethyl-aminoethyl-cellulose chromatography was found to be stimulated markedly by cyanide and ferrocyanide. The remaining 4S Cyt c reductase, which was insensitive to cyanide and ferrocyanide, was also fractionated with ammonium sulfate into two components. One of these, like the 8S Cyt c reductase, was sensitive to a protease from the maize roots which is relatively specific for nitrate reductase. This 4S Cyt c reductase species could be a subunit of nitrate reductase.


2 On sabbatical leave from the Department of Agricultural Biochemistry, Waite Agricultural Research Institute, University of Adelaide, Glen Osmond, S.A. 5064, Australia.

1 This work was supported by SRC Grant B-RG-8983.3 to C. B. J. and an SRC Senior Visiting Fellowship to W. W.







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