Voltammetry and in situ scanning tunneling microscopy of cytochrome c nitrite reductase on Au(111) electrodes

Gwyer, James D., Zhang, Jingdong, Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226 and Ulstrupy, Jens (2006) Voltammetry and in situ scanning tunneling microscopy of cytochrome c nitrite reductase on Au(111) electrodes. Biophysical Journal, 91 (10). pp. 3897-3906. ISSN 0006-3495

Full text not available from this repository. (Request a copy)

Abstract

Escherichia coli cytochrome c nitrite reductase (NrfA) catalyzes the six-electron reduction of nitrite to perform an important role in the biogeochemical cycling of nitrogen. Here we describe NrfA adsorption on single-crystal Au(111) electrodes as an electrocatalytically active film in which the enzyme undergoes direct electron exchange with the electrode. The adsorbed NrfA has been imaged to molecular resolution by in situ scanning tunneling microscopy (in situ STM) under full electrochemical potential control and under conditions where the enzyme is electrocatalytically active. Details of the density and orientational distribution of NrfA molecules are disclosed. The submonolayer coverage resolved by in situ STM is readily reconciled with the failure to detect nonturnover signals in cyclic voltammetry of the NrfA films. The molecular structures show a range of lateral dimensions. These are suggestive of a distribution of orientations that could account for the otherwise anomalously low turnover number calculated for the total population of adsorbed NrfA molecules when compared with that determined for solutions of NrfA. Thus, comparison of the voltammetric signals and in situ STM images offers a direct approach to correlate electrocatalytic and molecular properties of the protein layer, a long-standing issue in protein film voltammetry.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Biological Sciences Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) 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 15:02
Last Modified:	24 Sep 2024 09:48
URI:	https://ueaeprints.uea.ac.uk/id/eprint/21407
DOI:	10.1529/biophysj.106.089755

Actions (login required)

View Item