Theoretical Chemistry Accounts

, Volume 119, Issue 1–3, pp 107–111 | Cite as

Protein voltammetry and spectroscopy: integrating approaches

  • Louise Male
  • Sophie J. Marritt
  • Ben C. Berks
  • Myles R. Cheesman
  • Jessica H. van Wonderen
  • Simon J. George
  • Julea N. Butt
Regular Article


Cyclic voltammetry readily visualizes the redox properties of many proteins. Net electron exchange between the protein and an electrode produces an electrical current that simultaneously quantitates and characterizes the underlying redox event(s). However, no direct information regarding the molecular origin, or consequences, of electron transfer is available. Integrating voltammetric and spectroscopic methods is one route to a more ‘holistic’ description of protein electron transfer. Here, we illustrate this approach with spectroelectrochemical studies of Rhodovulum sulfidophilum cytochrome c 2 and Escherichia coli cytochrome bd that employ electronic absorbance, infra-red and magnetic circular dichroism spectroscopies.


Cytochrome c2 Cytochrome bd Infrared spectroscopy Magnetic circular dichroism spectroscopy Spectroelectrochemistry 


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Copyright information

© Springer-Verlag 2007

Authors and Affiliations

  • Louise Male
    • 1
  • Sophie J. Marritt
    • 1
  • Ben C. Berks
    • 2
  • Myles R. Cheesman
    • 1
  • Jessica H. van Wonderen
    • 1
  • Simon J. George
    • 3
  • Julea N. Butt
    • 1
    • 4
  1. 1.Centre for Metalloprotein Spectroscopy and Biology, School of Chemical Sciences and PharmacyUniversity of East AngliaNorwichUK
  2. 2.Department of BiochemistryUniversity of OxfordOxfordUK
  3. 3.Physical Biosciences DivisionLawrence Berkeley National LaboratoryBerkeleyUSA
  4. 4.Centre for Metalloprotein Spectroscopy and Biology, School of Biological SciencesUniversity of East AngliaNorwichUK

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