Redox Properties of Cytochromes and Bioelectronics

  • Geoffrey R. Moore
Part of the Electronics and Biotechnology Advanced (EL.B.A.) Forum Series book series (ELBA, volume 2)


The structural basis of metalloprotein action has been under investigation for many years by numerous researchers. The relationships they have uncovered should inform the discussion concerning the use of metalloproteins in synthetic electronic devices. The present paper is a contribution to this discussion. It concentrates on properties of cytochromes: these are haem-containing proteins in which the haem iron undergoes a reversible redox state change during their normal biological function (Belka et al., 1979). The paper will summarise some of the work currently going on in the author’s laboratory and review certain topics relevant to the use of cytochromes in electronic devices. These include factors influencing rates of interprotein electron transfer and redox potentials of cytochromes c,and redox properties of non-haem-iron-containing cytochromes b which act as iron-storage proteins, bacterioferritins, in bacteria.


Redox Property Haem Iron Axial Ligand Haem Group Work Term 
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Copyright information

© Springer Science+Business Media New York 1996

Authors and Affiliations

  • Geoffrey R. Moore
    • 1
  1. 1.Centre for Metalloprotein Spectroscopy and Biology School of Chemical SciencesUniversity of East AngliaNorwichNorway

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