NDLI: Effects of Amino and Thiol Group Reagents on the Ferredoxin:NADP$^{+}$ Oxidoreductase Catalysed Reduction of Dibromothymoquinone

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Effects of Amino and Thiol Group Reagents on the Ferredoxin:NADP$^{+}$ Oxidoreductase Catalysed Reduction of Dibromothymoquinone

Content Provider	Springer Nature Link
Author	Grzyb, J. Bojko, M. Więckowski, S.
Copyright Year	2003
Abstract	Effects of selective reagents of amino groups (fluorescamine, Fc) and thiol [5,5′-dithio-bis(2-nitrobenzoic) acid, DTNB] groups on the diaphorase activity of spinach ferredoxin:NADP$^{+}$ oxidoreductase (FNR, E.C 1.18.1.2) in the presence of dibromothymoquinone (DBMIB) as an electron acceptor were studied. The incubation of FNR with 250 μM Fc in the time range from 0 to 120 min led to the gradual decrease of FNR activity according to biphasic kinetics. At the initial phase the activity (defined as the rate of NADPH oxidation) decreased about 4-time faster than at the subsequent second slower phase. Incubation of FNR simultaneously with Fc and DBMIB for more than 20 min caused restoration of the activity to about 80 % of the control. The inhibitory effect of Fc on the FNR-catalysed DBMIB reduction had non-competitive character. Incubation of FNR with DTNB led also to a gradual decrease of the enzyme activity, which reached about 45 % of the control after 2 h of incubation. Thus neither amino nor thiol groups in the FNR molecule are involved directly in the DBMIB reduction. However, the presence of DBMIB in the incubation medium influenced the inhibitory pattern of Fc and DTNB, and this suggests that DBMIB modified the conformational state of the FNR molecule.
Starting Page	627
Ending Page	630
Page Count	4
File Format	PDF
ISSN	03003604
Journal	Photosynthetica
Volume Number	41
Issue Number	4
e-ISSN	15739058
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2003-01-01
Publisher Place	Dordrecht
Access Restriction	Subscribed
Subject Keyword	Plant Physiology
Content Type	Text
Resource Type	Article
Subject	Physiology Plant Science

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