Abstract
Electron transfer rates in Zn/Ru modified myoglobins are calculated using a molecular orbital method to obtain the electronic factor and empirical values of the reorganization energy and driving force. The protein is partitioned into three subsystems, A, B, and C, where A and C consist of the metal ions and their ligands and B is the protein bridge between A and C. Molecular orbitals are calculated in each subsystem. Interaction matrix elements between the subsystems are calculated and the total eigenvalue problem solved using a partitioning technique. The distance dependence of the rate is only roughly exponential as a function of intermetal distance. In particular, the rate of the His-12 derivative is larger than the average exponential decrease, in agreement with the experiments. If the indole group in the pathway between the metal ions is replaced by an equally large (CH{sub 2})n-chain, the calculated rate is close to the average exponential decrease. The electronic spectra of zinc porphin (ZnP) and Zn-substituted myoglobin (ZnMb) are calculated using a CNDO/S approach, and the results compare favorably with the corresponding experimental spectra.
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