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Modelling the impact of geometric parameters on the redox potential of blue copper proteins

Taylor, M.K. and Stevenson, D.E. and Berlouis, L. and Kennedy, A.R. and Reglinski, J. (2005) Modelling the impact of geometric parameters on the redox potential of blue copper proteins. Journal of Inorganic Biochemistry, 100 (2). pp. 250-259. ISSN 0162-0134

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The synthesis and structure of a homologous series of cationic N2S2 copper(I) Schiff base complexes constructed using o-tert-butylthiobenzaldehyde and a series of terminal diamines (ethane, propane, butane) are reported. The complexes differ only in the length of the methylene chain between the imine groups. This simple modification forces the copper centre to shift geometry from a planar (1,2-diaminoethane) to a more distorted tetrahedral motif (1,4-diaminobutane). The redox potentials of the three cations were measured using cyclic voltammetry in donor (acetonitrile) and non-donor solvents (dichloromethane). The S-Cu-N angles for each complex are correlated against the respective redox potential allowing an analysis of the geometric impact on the redox potential in soft copper centres. The redox potential is observed to increase as the metal centre moves from a planar towards a tetrahedral motif. Comparing this data with the reported structures of the blue copper proteins (rusticyanin and plastocyanin) allows an assessment of the contribution of the geometry of the metal binding site to the operating potential of these proteins to be made.