Kinetic, structural and electrostatic aspects of the reduction of pentacyanoferrate(III) complexes by myoglobin |
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Authors: | Elwira Ilkowska Krzysztof Lewiński Rudi van Eldik Grażyna Stochel |
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Institution: | (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;(2) Institute for Inorganic Chemistry, University of Erlangen-Nürnberg, Egerlandstrasse 1, D-91058 Erlangen, Germany, DE |
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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)5L
n
–, 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.
Received: 10 November 1998 / Accepted: 25 February 1999 |
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Keywords: | Pentacyanoferrate(III) complexes Oxymyoglobin Electron transfer Kinetics Electrostatic potential |
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