Opportunities for mesoporous nanocrystalline SnO2 electrodes in kinetic and catalytic analyses of redox proteins

Kemp, Gemma L., Marritt, Sophie J., Xiaoe, Li, Durrant, James R., Cheesman, Myles R. and Butt, Julea ORCID: https://orcid.org/0000-0002-9624-5226 (2009) Opportunities for mesoporous nanocrystalline SnO2 electrodes in kinetic and catalytic analyses of redox proteins. Biochemical Society Transactions, 37 (2). pp. 368-372. ISSN 0300-5127

Preview

PDF (Kemp_et_al._Biochem_Soc_Trans_2009.pdf) Download (265kB) | Preview

Abstract

PFV (protein film voltammetry) allows kinetic analysis of redox and coupled-chemical events. However, the voltammograms report on the electron transfer through a flow of electrical current such that simultaneous spectroscopy is required for chemical insights into the species involved. Mesoporous nanocrystalline SnO2 electrodes provide opportunities for such ‘spectroelectrochemical’ analyses through their high surface area and optical transparency at visible wavelengths. Here, we illustrate kinetic and mechanistic insights that may be afforded by working with such electrodes through studies of Escherichia coli NrfA, a pentahaem cytochrome with nitrite and nitric oxide reductase activities. In addition, we demonstrate that the ability to characterize electrocatalytically active protein films by MCD (magnetic circular dichroism) spectroscopy is an advance that should ultimately assist our efforts to resolve catalytic intermediates in many redox enzymes.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Chemistry of Light and Energy Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Energy Materials Laboratory
Depositing User:	Rachel Smith
Date Deposited:	17 Feb 2011 16:31
Last Modified:	23 Oct 2024 23:36
URI:	https://ueaeprints.uea.ac.uk/id/eprint/21395
DOI:	10.1042/BST0370368

Downloads

Actions (login required)

View Item