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Kinetics and mechanism of the reduction of hexacyanoferrate(III) by myoglobin in aqueous solution

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Abstract

 The kinetics of the reduction of hexacyanoferrate(III) by myoglobin was studied as a function of temperature and pressure. The results of the study show that both oxy- and deoxymyoglobin are redox active species. The rate and activation parameters underline the operation of an outer-sphere electron transfer mechanism for the studied system.

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Authors and Affiliations

  1. Institut für Anorganische Chemie, Universität Erlangen- Nürnberg, Egerlandstrasse 1, D-91058 Erlangen, Germany Tel.: +49-9131-857350; Fax: +49-9131-857387; e-mail: vaneldik@anorganik.chemie.uni-erlangen.de, , , , , , DE

    R. van Eldik

  2. Faculty of Chemistry Jagiellonian University, PL-30060 Kraków, Poland, , , , , , PL

    Elwira Ilkowska & Grazyna Stochel

Authors
  1. Elwira Ilkowska
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  2. R. van Eldik
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  3. Grazyna Stochel
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Received: 9 December 1996 / Accepted: 16 June 1997

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Ilkowska, E., van Eldik, R. & Stochel, G. Kinetics and mechanism of the reduction of hexacyanoferrate(III) by myoglobin in aqueous solution. JBIC 2, 603–610 (1997). https://doi.org/10.1007/s007750050175

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  • DOI: https://doi.org/10.1007/s007750050175

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