Molecular Assembly of Hemin on Single-Crystal Au(111)-electrode Surfaces

Ling Zhang, Jens Ulstrup, Jingdong Zhang

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Iron porphyrin, hemin, is the active core in cytochromes, haemoglobin and myoglobin, andenzymes such as the peroxidases. These metalloproteins are engaged in respiratory electron transfer, oxygen transport and storage, and enzyme catalysis in the biosynthesis of a range of metabolites. Hemin itself also acts as catalyst in electrochemical reduction of dioxygen and other small inert molecules such as nitrogen monoxide, and in electrochemiluminescent detection of dioxygen, peroxide, DNA, and proteins. л-л interactions of hemin with carbon materials have been broadly studied. Hemin onnoble metal surfaces has been prime targets in high-resolution STM but much less used in applied contexts such as biosensors and drug delivery. How hemin molecules interact with noble metal surfaces offers, however, other challenges in nanoscale and single-moleculescience. We have studied hemin adsorption on well-defined single-crystal Au(111)-electrodesurfaces using electrochemistry combined with scanning tunnelling microscopy under electrochemical control. Hemin gives two voltammetric peaks assigned to adsorbed monomers and dimmers (Fig. 1A). In situ STM shows that hemin self-assembles in ordered monolayers through non-covalent adsorption, as the reconstruction of the Au-(111) surface underneath the hemin layer is clearly visible (Fig. 1B).
Original languageEnglish
Publication date2016
Publication statusPublished - 2016
EventThe 6th Baltic Electrochemistry Conference: Electrochemistry of Functional Interfaces and Materials - Paasitorni Conference Centre, Helsinki, Finland
Duration: 15 Jun 201617 Jun 2016


ConferenceThe 6th Baltic Electrochemistry Conference
LocationPaasitorni Conference Centre
Internet address


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