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Kinetic, structural and electrostatic aspects of the reduction of pentacyanoferrate(III) complexes by myoglobin
Authors:Elwira Ilkowska  Krzysztof Lewiński  Rudi van Eldik  Grażyna Stochel
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
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
Keywords:  Pentacyanoferrate(III) complexes  Oxymyoglobin  Electron transfer  Kinetics  Electrostatic potential
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