The electrocatalytic properties of two related proteins, myoglobin (Mb) and hemoglobin (Hb), immobilized in a surfactant film (didodecyldimethylammonium bromide, DDAB) on an electrode were investigated. The direct electrochemistry of the myoglobin/ DDAB and hemoglobin/DDAB films was compared and showed one redox couple, two redox couples. and three redox couples, when transferred to strong acidic, weak acidic and basic, and pH 13 aqueous solutions, respectively. The redox couples and their formal potentials are pH dependent. An electrochemical quartz crystal microbalance (EQCM) and cyclic voltammetry were used to study the in situ growth of both DDAB deposition on gold disk electrodes and myoglobin deposition on DDAB film-modified electrodes. The electrocatalytic properties were investigated and showed that the myoglobin/DDAB and hemoglobin/DDAB film modified electrodes are both electrocatalytically active for oxygen reduction, and more H2O2 was produced during electrocatalytic reduction using a myoglobin/DDAB film than when using a hemoglobin/DDAB film. The electrocatalysis that was active for L-cystine, N2O, and 2,2'-dithiosalicylic acid reductions showed an electrocatalytic current developed from the cathodic peak of the redox couple at about -0.9 V (Fe(II)/Fe(I) redox couple) in neutral and weak basic aqueous solutions. The electrocatalysis that was active for L-cysteine oxidation, showed an elect rocatalytic current developed from the cathodic peak of the redox couple at about +0.2 V (Fe(III)/Fe(IV) redox couple). Mb/DDAB and Hb/DDAB film modified electrodes are electrocatalytically active for trichloroacetic acid reduction in weak acidic and basic buffered aqueous solutions through the Fe(II)/Fe(I) redox couple. However. the electrocatalytic current developed from the cathodic peak of the redox couple at a potential of about -0.1 V (from the Fe(III)/Fe(II) redox couple) in strong acidic aqueous solutions occurs only with higher concentrations of reactant. (C) 2004 Elsevier B.V. All rights reserved.