Microperoxidase-11, MP-11, is made by proteolytic digestion of cytochrome c, cyt. c. It consists of a polypeptide of 11 amino residues attached covalently to the heme. Given that MP-11 has a more exposed heme than the complete protein, it would seem that electron transfer, ET, between immobilized MP-11 and electrodes would be at least as fast as for intact cyt. c. However, while the maximal heterogeneous ET rate for immobilized cyt. c is around 1000 s(-1), that reported previously for immobilized MP-11 does not exceed 20 s(-1). This work attempts to understand this difference in measured ET rates. The MP-11 was immobilized on gold electrodes using several protocols: (electrode A) the immobilization was done following a previously published carbodiimide based recipe yielding ET rates of the order of 20 s(-1); (B) MP-11 was bound to gold electrodes by Lomant's reagent and gave an ET rate close to 4000 s(-1); (C) physisorbed MP-11 on gold electrodes with a self assembled monolayer, SAM, of alkane thiols gave an ET rate approaching 2000 s(-1) for the shortest length alkane thiol. Inspection of the immobilization chemistries suggests that the procedure employed in producing electrodes B and C are likely to lead to a monolayer or less of immobilized MP-11 while the procedure employed for electrode A may lead to a film comprised of a multilayer of MP-11. The presence of such a film on electrode A complicates the ET process since the MP-11 in the layer adjacent to the electrode could have fast ET rates while the MP-11 in the outer layers may have significantly slower ET rates. The net result would be an apparent ET rate constant which is much smaller than the value for the first layer. The measurements and calculations are presented in support of such an interpretation.