Bioelectrocatalysis of sulfite dehydrogenase from Sinorhizobium meliloti with its physiological cytochrome electron partner

Kalimuthu, Palraj, Hsiao, Ju-Chun, Nair, Remya Purushothaman, Kappler, Ulrike and Bernhardt, Paul V. (2017) Bioelectrocatalysis of sulfite dehydrogenase from Sinorhizobium meliloti with its physiological cytochrome electron partner. ChemElectroChem, . doi:10.1002/celc.201700838

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Author Kalimuthu, Palraj
Hsiao, Ju-Chun
Nair, Remya Purushothaman
Kappler, Ulrike
Bernhardt, Paul V.
Title Bioelectrocatalysis of sulfite dehydrogenase from Sinorhizobium meliloti with its physiological cytochrome electron partner
Formatted title
Bioelectrocatalysis of sulfite dehydrogenase from Sinorhizobium meliloti with its physiological cytochrome electron partner
Journal name ChemElectroChem   Check publisher's open access policy
ISSN 2196-0216
Publication date 2017-09-19
Year available 2017
Sub-type Article (original research)
DOI 10.1002/celc.201700838
Open Access Status Not yet assessed
Place of publication Weinheim, Germany
Publisher Wiley
Language eng
Formatted abstract
We demonstrate electrochemically driven catalytic voltammetry of the Mo-dependent sulfite dehydrogenase (SorT) from the α-Proteobacterium Sinorhizobium meliloti with its physiological electron acceptor, the c-type cytochrome (SorU), with both proteins co-adsorbed on a chemically modified Au working electrode. Both SorT and SorU were constrained under a perm-selective dialysis membrane with the biopolymer chitosan as a co-adsorbate, while the electrode was modified with a 3-mercaptopropionate self-assembled monolayer cast on the Au electrode. Cyclic voltammetry of the SorU protein reveals a well-defined quasireversible FeIII/II redox couple at +130 mV versus NHE in 100 mM phosphate buffer solution (pH 7.0). Introduction of wild-type sulfite dehydrogenase (SorTWT) and sulfite transforms this transient SorU voltammetric response into a sigmoidal catalytic wave, which increases with sulfite concentration before eventually saturating. In addition to the wild-type enzyme, the variants SorTR78K, SorTR78M, and SorTR78Q were also examined electrochemically in an effort to better understand the role of amino acid residue Arg78, which is in the vicinity of the Mo active site of SorT.
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID DP150103345
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
School of Chemistry and Molecular Biosciences
 
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Created: Wed, 13 Sep 2017, 12:33:16 EST by Dr Ulrike Kappler on behalf of School of Chemistry & Molecular Biosciences