Electron transfer of peroxidase assemblies at tailored nanocarbon electrodes

Jennifer L. Lyon, Keith J. Stevenson

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)


In bioelectrochemistry, the catalytic function of redox enzymes depends largely upon the nature of the working electrode material. One major example of this phenomenon is the improvement of biogenic analyte detection at graphitic carbon with increased edge plane character in the graphene lattice. In our laboratories, we have found that the edge plane character of carbon nanotubes (CNTs) prepared using chemical vapor deposition (CVD) can be tuned via selective doping with nitrogen, termed N-CNTs. In this report, we extend these studies to investigate the influence of N-doping of nanocarbons on the electron transfer of horseradish peroxidase (HRP) using spectrophotometric enzyme activity assays and electrochemical measurements. Our findings demonstrate that HRP adsorption at N-CNTs increases by a factor of two relative to that of nondoped CNTs, with surface coverages, Γm, of 75 ± 4 and 33 ± 5 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) U/mg, respectively. Surprisingly, however, only ∼40% of the HRP adsorbed at N-CNTs is electroactive, as assessed by voltammetry of the HRP Fe2+/3+ redox response. By contrast, HRP adsorbed at nondoped CNTs is nearly 100% electroactive, suggesting that the nature of the HRP adsorption (e.g., electrostatic, van der Waals) and geometric factors of heme orientation affect the biocatalytic performance. We also describe studies that utilize the properties of both nondoped CNTs and N-CNTs with adsorbed HRP for unmediated, quantitative H2O2 sensing.

Original languageEnglish
Pages (from-to)6714-6721
Number of pages8
JournalElectrochimica Acta
Issue number23
Publication statusPublished - 1 Oct 2008
Externally publishedYes


  • Bioelectrocatalysis
  • Horseradish peroxidase
  • Unmediated enzyme electrochemistry


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