The reactivation of nitrate reductase from spinach (Spinacia oleracea L.) inactivated by NADH and cyanide, using trivalent manganese either generated by illuminated chloroplasts or as manganipyrophosphate

Planta ◽  
1980 ◽  
Vol 150 (3) ◽  
pp. 242-248 ◽  
Author(s):  
J. M. Maldonado ◽  
B. A. Notton ◽  
E. J. Hewitt
Keyword(s):  
Nitrate Reductase ◽  
Spinacia Oleracea ◽  
Spinacia Oleracea L

scholarly journals Oxidation–reduction midpoint potentials of the flavin, haem and Mo-pterin centres in spinach (Spinacia oleracea L.) nitrate reductase

1989 ◽  
Vol 263 (1) ◽  
pp. 285-287 ◽  
Author(s):  
C J Kay ◽  
M J Barber ◽  
B A Notton ◽  
L P Solomonson
Keyword(s):  
Nitrate Reductase ◽  
Room Temperature ◽  
Spinacia Oleracea ◽  
Midpoint Potential ◽  
Redox Couples ◽  
Oxidation Reduction ◽  
Spinacia Oleracea L ◽  
Unicellular Green Alga ◽  
Green Alga Chlorella ◽  
Prosthetic Groups

Oxidation-reduction midpoint potentials have been determined for the flavin, cytochrome b557 and Mo-pterin prosthetic groups of spinach (Spinacia oleracea L.) assimilatory nitrate reductase using visible, c.d. and room-temperature e.p.r. potentiometric titrations. At pH 7 and 25 degrees C, the midpoint potential for the FAD/FADH2 couple was determined by c.d. potentiometry to be -280 +/- 10 mV (n = 2). The redox potential for reduction of the haem was determined by visible potentiometry to be -123 +/- 10 mV (n = 1), significantly lower than the previously published value of -60 mV [Fido, Hewitt, Notton, Jones & Nasrulhaq-Boyce (1979) FEBS Lett. 99, 180-182]. Potentials for the Mo(VI)/Mo(V) and Mo(V)/Mo(IV) redox couples, determined by room-temperature e.p.r. potentiometry, were found to be +2 +/- 20 and -6 +/- 20 mV respectively. These values are very similar to the values previously determined for the FAD, haem and Mo-pterin centres in assimilatory nitrate reductase isolated from the unicellular green alga Chlorella vulgaris and indicate a close thermodynamic similarity between the two enzymes.

scholarly journals Red-Light Effects Sensitized by Methylene Blue on Nitrate Reductase from Spinach (Spinacia oleracea L.) Leaves

1984 ◽  
Vol 39 (11-12) ◽  
pp. 1079-1084 ◽  
Author(s):  
S. G. Mauriño ◽  
M. A. Vargas ◽  
P. J. Aparicio ◽  
J. M. Maldonado
Keyword(s):  
Methylene Blue ◽  
Nitrate Reductase ◽  
Spinacia Oleracea ◽  
Red Light ◽  
Deuterated Water ◽  
Anaerobic Conditions ◽  
Molybdenum Complex ◽  
Spinacia Oleracea L ◽  
Light Effects

Abstract Nitrate reductase from spinach (Spinacia oleracea L.) leaves, which had been inactivated in vitro by incubation with NADH and cyanide, was fully reactivated in minutes when irradiated in anaerobic conditions with red light in the presence of methylene blue. Both the rate and the extent of reactivation increased with light intensity (6 to 100 W·m-2) and dye concentration (1 to 10 μM). On the contrary, photoreactivation was completely abolished when NADH or ethylenediaminetetra-acetic acid were present during irradiation. We propose that methylene blue, when photo excited, exhibits a redox potential positive enough to reoxidise the CN--re-duced molybdenum complex settled in the inactive enzyme, thus causing its reactivation. On the other hand, prolonged irradiation of nitrate reductase, under air and in the presence of methylene blue, promoted an oxygen-dependent irreversible inactivation of the two partial activities of the enzyme. This inactivation was markedly enhanced in 77% deuterated water and greatly prevented by azide, which indicates that singlet oxygen is the species primarily involved in the photooxidative inactivation of the enzyme.

Cloning of a nitrate reductase inactivator (NRI) cDNA from Spinacia oleracea L. and expression of mRNA and protein of NRI in cultured spinach cells

Planta ◽  
2003 ◽  
Vol 216 (6) ◽  
pp. 961-968 ◽  
Author(s):  
Masatoshi Sonoda ◽  
Hiroaki Ide ◽  
Shinya Nakayama ◽  
Asako Sasaki ◽  
Shinei Kitazaki ◽  
...  
Keyword(s):  
Nitrate Reductase ◽  
Spinacia Oleracea ◽  
Spinacia Oleracea L ◽  
Nitrate Reductase Inactivator

Sequence Analysis of Cloned cDNA and Proteolytic Fragments for Nitrate Reductase from Spinacia oleracea L.

1991 ◽  
Vol 32 (7) ◽  
pp. 1031-1038 ◽  
Author(s):  
Naomasa Shiraishi ◽  
Yoshihiro Kubo ◽  
Go Takeba ◽  
Seiichiro Kiyota ◽  
Katsuhiro Sakano ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Nitrate Reductase ◽  
Spinacia Oleracea ◽  
Spinacia Oleracea L ◽  
Cloned Cdna

Versuche zur präparativen Isolierung pflanzlicher Zellorganellen mittels der trägerfreien, kontinuierlichen Ablenkungselektrophorese

1964 ◽  
Vol 19 (11) ◽  
pp. 1072-1075 ◽  
Author(s):  
K. Hannig ◽  
W. Klofat ◽  
H. Endres
Keyword(s):  
Spinacia Oleracea ◽  
Taraxacum Officinale ◽  
Wird Eine ◽  
Spinacia Oleracea L ◽  
Helianthus Annus

Es wird eine präparative Methode zur Isolierung pflanzlicher Zellbestandteile mittels der trägerfreien, kontinuierlichen Ablenkungselektrophorese nach HANNIG 1, 2 kurz skizziert. Als Versuchsmaterial dienen Blätter von Spinat (Spinacia oleracea L.), Sonnenblumen (Helianthus annus L.) und Löwenzahn (Taraxacum officinale Web.).Die Verteilungskurven werden durch Extinktionsmessung der einzelnen Fraktionen in den Auffanggläschen erhalten. Die Definition der Teilchen erfolgt vorläufig morphologisch durch Anfärben und lichtmikroskopische Prüfung als auch durch elektronenmikroskopische Kontrolle nach vorheriger Präparation nach dem „negativ staining“ Verfahren 3,4 oder Kontrastierung mit Phosphorwolframsäure.Bei der Trennung werden Zellkerne und Zellkernfragmente, ganze Chloroplasten, „Mitochondrien“ und plasmatische Strukturen erhalten.

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