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Kinetic, structural and electrostatic aspects of the reduction of pentacyanoferrate(III) complexes by myoglobin

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Abstract

 The mechanism of the reduction of pentacyanoferrate(III) complexes by oxymyoglobin has been studied by conventional and high-pressure kinetic methods, and also by structural modelling. The results of this and an earlier study show that an outer-sphere mechanism is operating for electron transfer between oxymyoglobin and FeIII(CN)5Ln –, independent of the lability of the ligand L. The electron transfer process is preceded by precursor formation at a specific site on the protein close to the protein heme pocket.

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Authors and Affiliations

  1. Faculty of Chemistry, Jagiellonian University, Ingardena 3, PL-30-060 Kraków, Poland e-mail: stochel@trurl.ch.uj.edu.pl, Tel.: +48-12-6336377 ext 222, , , , , , PL

    Elwira Ilkowska, Krzysztof Lewiński & Grażyna Stochel

  2. Institute for Inorganic Chemistry, University of Erlangen-Nürnberg, Egerlandstrasse 1, D-91058 Erlangen, Germany, , , , , , DE

    Rudi van Eldik

Authors
  1. Elwira Ilkowska
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  2. Krzysztof Lewiński
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  3. Rudi van Eldik
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  4. Grażyna Stochel
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Received: 10 November 1998 / Accepted: 25 February 1999

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Ilkowska, E., Lewiński, K., van Eldik, R. et al. Kinetic, structural and electrostatic aspects of the reduction of pentacyanoferrate(III) complexes by myoglobin. JBIC 4, 302–310 (1999). https://doi.org/10.1007/s007750050316

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  • DOI: https://doi.org/10.1007/s007750050316

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