Electron transfer and adsorption of myoglobin on self-assembled surfactant films

An electrochemical tapping-mode AFM study

S. Boussaad, Nongjian Tao

Research output: Contribution to journalArticle

77 Citations (Scopus)

Abstract

We have studied myoglobin (Mb) on graphite basal plane and on self- assembled didodecyldimethylammonium bromide (DDAB) mono- and multilayers with in situ tapping-mode AFM, cyclic voltammetry, and differential capacitance measurements. On graphite, Mb molecules adsorb and aggregate into chainlike features. The aggregation indicates an attractive interaction between the adsorbed molecules. In contrast, the molecules are randomly distributed on the DDAB layers. The adsorption on DDAB changes drastically the domains and defects in the DDAB layers due to a strong Mb-DDAB interaction. On both the bare and the DDAB-coated electrodes, the protein undergoes a fast electron- transfer reaction involving Fe3+ + 1e- mutually implies Fe2+ in the heme group. The structure of the DDAB film is potential dependent. At low potentials, the film is in a solidlike phase. When the potential is raised to ~0 V, the film transforms into a liquidlike phase via a first-order phase transition. The liquidlike phase may be responsible for the fast diffusion of Mb through the DDAB layers.

Original languageEnglish (US)
Pages (from-to)4510-4515
Number of pages6
JournalJournal of the American Chemical Society
Volume121
Issue number18
DOIs
StatePublished - May 12 1999
Externally publishedYes

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Myoglobin
Surface-Active Agents
Adsorption
Surface active agents
Electrons
Molecules
Graphite
Capacitance measurement
Cyclic voltammetry
Monolayers
Multilayers
Agglomeration
Phase transitions
Proteins
Defects
Electrodes
didodecyldimethylammonium
Phase Transition
Heme

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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abstract = "We have studied myoglobin (Mb) on graphite basal plane and on self- assembled didodecyldimethylammonium bromide (DDAB) mono- and multilayers with in situ tapping-mode AFM, cyclic voltammetry, and differential capacitance measurements. On graphite, Mb molecules adsorb and aggregate into chainlike features. The aggregation indicates an attractive interaction between the adsorbed molecules. In contrast, the molecules are randomly distributed on the DDAB layers. The adsorption on DDAB changes drastically the domains and defects in the DDAB layers due to a strong Mb-DDAB interaction. On both the bare and the DDAB-coated electrodes, the protein undergoes a fast electron- transfer reaction involving Fe3+ + 1e- mutually implies Fe2+ in the heme group. The structure of the DDAB film is potential dependent. At low potentials, the film is in a solidlike phase. When the potential is raised to ~0 V, the film transforms into a liquidlike phase via a first-order phase transition. The liquidlike phase may be responsible for the fast diffusion of Mb through the DDAB layers.",
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T2 - An electrochemical tapping-mode AFM study

AU - Boussaad, S.

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N2 - We have studied myoglobin (Mb) on graphite basal plane and on self- assembled didodecyldimethylammonium bromide (DDAB) mono- and multilayers with in situ tapping-mode AFM, cyclic voltammetry, and differential capacitance measurements. On graphite, Mb molecules adsorb and aggregate into chainlike features. The aggregation indicates an attractive interaction between the adsorbed molecules. In contrast, the molecules are randomly distributed on the DDAB layers. The adsorption on DDAB changes drastically the domains and defects in the DDAB layers due to a strong Mb-DDAB interaction. On both the bare and the DDAB-coated electrodes, the protein undergoes a fast electron- transfer reaction involving Fe3+ + 1e- mutually implies Fe2+ in the heme group. The structure of the DDAB film is potential dependent. At low potentials, the film is in a solidlike phase. When the potential is raised to ~0 V, the film transforms into a liquidlike phase via a first-order phase transition. The liquidlike phase may be responsible for the fast diffusion of Mb through the DDAB layers.

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