Polymyxin-Coated Au and Carbon Nanotube Electrodes for Stable [NiFe]-Hydrogenase Film Voltammetry

• Published in: Langmuir 2008-06, Vol.24 (11), p.5925-5931
• Main Authors: Hoeben, Freek J. M, Heller, Iddo, Albracht, Simon P. J, Dekker, Cees, Lemay, Serge G, Heering, Hendrik A
• Format: Article
• Language: English
• Subjects: Allochromatium vinosum; Bacterial Proteins - chemistry; Catalysis; Chemistry; Chlorides - chemistry; Colloidal state and disperse state; Electrochemistry; Electrochemistry: Charge Transfer, Electrocatalysis, Kinetics, Bioelectrochemistry; Electrodes; Enzymes, Immobilized - chemistry; Exact sciences and technology; Gammaproteobacteria - enzymology; General and physical chemistry; Gold - chemistry; Hydrogenase - chemistry; Kinetics and mechanism of reactions; Nanotubes, Carbon - chemistry; Polymyxins - chemistry; Surface physical chemistry; Theory of reactions, general kinetics. Catalysis. Nomenclature, chemical documentation, computer chemistry
• ISSN: 0743-7463; 1520-5827
• DOI: 10.1021/la703984z

We report on the use of polymyxin (PM), a cyclic cationic lipodecapeptide, as an electrode modifier for studying protein film voltammetry (PFV) on Au and single-walled carbon nanotube (SWNT) electrodes. Pretreating the electrodes with PM allows for the subsequent immobilization of an active submonolayer of [NiFe]-hydrogenase from Allochromatium vinosum (Av H2ase). Probed by cyclic voltammetry (CV), the adsorbed enzyme exhibits characteristic electrocatalytic behavior that is stable for several hours under continuous potential cycling. An unexpected feature of the immobilization procedure is that the presence of chloride ions is a prerequisite for obtaining electrocatalytic activity. Atomic force microscopy (AFM) relates the observed catalytic activity to enzymatic adsorption at the PM/Au(111) surface, and a combination of concentration-dependent CV and AFM is used to investigate the interaction between the enzyme and the PM layer.