Article ID Journal Published Year Pages File Type
181763 Electrochemistry Communications 2007 5 Pages PDF
Abstract

The state of the heme of myoglobin molecules incorporated in a didodecyldimethylammonium bromide (DDAB) film on a pyrolytic graphite electrode was described using the results of electroreflectance measurements. It was found that the hemes are released from the myoglobin molecules. The ER spectrum of PG electrode|Mb–DDAB film was indistinguishable from the spectrum of PG electrode|hemin–DDAB film, even in the presence of NaBr, but clearly different from PG electrode|imidazole-coordinated hemin–DDAB. These results support the claim of de Groot and coworker [M.T. de Groot, M. Merksx, M.T.M. Koper, J. Am. Chem. Soc. 127 (2005) 16224; M.T. de Groot, M. Merkx, M.T.M. Koper, Electrochem. Commun. 8 (2006) 999]. It is likely that DDAB is not a strong inhibitor of imidazole coordination but acts on the protein, resulting in conformational change and the heme release.

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Physical Sciences and Engineering Chemical Engineering Chemical Engineering (General)
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