Presence of haem in the tungsten analogue of nitrate reductase and its relationship to dehydrogenase function

Autor:	Eric J. Hewitt, R.J. Fido, E. F. Watson, B.A. Notton
Rok vydání:	1979
Předmět:	biology Cytochrome fungi food and beverages Soil Science Dehydrogenase Molybdate Nitrate reductase biology.organism_classification chemistry.chemical_compound Tungstate chemistry Biochemistry Nitrate biology.protein Spinach Dichlorophenolindophenol Agronomy and Crop Science Nuclear chemistry
Zdroj:	Plant Science Letters. 14:85-90
ISSN:	0304-4211
DOI:	10.1016/0304-4211(79)90159-7
Popis:	Spinach plants were grown for 8 weeks in sand culture with either complete nutrient containing molybdate (0.05 p.p.m.) or molybdenum-free nutrient containing tungstate (1 p.p.m.). Nitrate reductase and its tungsten analogue were extracted and purified. Nitrate reductase activities (units/kg leaf) decreased during purification from 22.72 to 4.59 (molybdate plants) and from 2.19 to 0.86 (tungstate plants). Cytochrome c reductase activities decreased from 211 to 26 (molybdate plants) and from 539 to 22 (tungstate plants) reflecting the super-induction of the small molecular size enzyme and decreased stability of the analogue. Both nitrate reductase and its analogue contained similar amounts of cytochrome b557kg leaf, which was reduced by NADH and reoxidised by excess of the dehydrogenase electron acceptor dichlorophenolindophenol. Only the haem in the enzyme from molybdate plants was reoxidisable by nitrate.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::6282b0e3ad93659e4744fae0b0e1234c https://doi.org/10.1016/0304-4211(79)90159-7 Zobrazit plný text záznamu