Mediated electrochemistry of nitrate reductase from Arabidopsis thaliana

Kalimuthu, Palraj, Fischer-Schrader, Katrin, Schwarz, Guenter and Bernhardt, Paul V. (2013) Mediated electrochemistry of nitrate reductase from Arabidopsis thaliana. Journal of Physical Chemistry B, 117 25: 7569-7577. doi:10.1021/jp404076w

Author Kalimuthu, Palraj
Fischer-Schrader, Katrin
Schwarz, Guenter
Bernhardt, Paul V.
Title Mediated electrochemistry of nitrate reductase from Arabidopsis thaliana
Formatted title
Mediated electrochemistry of nitrate reductase from Arabidopsis thaliana
Journal name Journal of Physical Chemistry B   Check publisher's open access policy
ISSN 1520-6106
Publication date 2013-06-27
Sub-type Article (original research)
DOI 10.1021/jp404076w
Volume 117
Issue 25
Start page 7569
End page 7577
Total pages 9
Place of publication Washington, DC, United States
Publisher American Chemical Society
Collection year 2014
Language eng
Formatted abstract
Herein we report the mediated electrocatalytic voltammetry of the plant molybdoenzyme nitrate reductase (NR) from Arabidopsis thaliana using the established truncated molybdenum-heme fragment at a glassy carbon (GC) electrode. Methyl viologen (MV), benzyl viologen (BV), and anthraquinone-2-sulfonic acid (AQ) are employed as effective artificial electron transfer partners for NR, differing in redox potential over a range of about 220 mV and delivering different reductive driving forces to the enzyme. Nitrate is reduced at the Mo active site of NR, yielding the oxidized form of the enzyme, which is reactivated by the electro-reduced form of the mediator. Digital simulation was performed using a single set of enzyme dependent parameters for all catalytic voltammetry obtained under different sweep rates and various substrate or mediator concentrations. The kinetic constants from digital simulation provide new insight into the kinetics of the NR catalytic mechanism.
Keyword Protein film voltammetry
Catalytic electrochemistry
Amperometric detection
Sulfite dehydrogenase
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
School of Chemistry and Molecular Biosciences
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