Orientation and Function of a Membrane-Bound Enzyme Monitored by Electrochemical Surface-Enhanced Infrared Absorption Spectroscopy

Ines Antunes Pereira

doi:10.1021/jz4013678

Orientation and Function of a Membrane-Bound Enzyme Monitored by Electrochemical Surface-Enhanced Infrared Absorption Spectroscopy

Ines Antunes Pereira

Instituto de Tecnologia Química e Biológica António Xavier (ITQB)

Research output: Contribution to journal › Article › peer-review

21 Citations (Scopus)

Abstract

Electrochemical SEIRA is the method of choice for characterizing a lipid-bilayer-anchored, membrane bound hydrogenase Immobilized on a gold electrode. This setup allows the study of the enzyme under conditions mimicking its natural environment. A single experiment provides all of the crucial spectroscopic information relating to she protein orientation; active Site of the protein, and the lipid bilayer and also direct electrochemical determination of the catalytic H-2 oxidation by the enzyme

Original language	Unknown
Pages (from-to)	2794-2798
Journal	JOURNAL OF PHYSICAL CHEMISTRY LETTERS
Volume	4
Issue number	17
DOIs	https://doi.org/10.1021/jz4013678
Publication status	Published - 1 Jan 2013

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10.1021/jz4013678

Cite this

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abstract = "Electrochemical SEIRA is the method of choice for characterizing a lipid-bilayer-anchored, membrane bound hydrogenase Immobilized on a gold electrode. This setup allows the study of the enzyme under conditions mimicking its natural environment. A single experiment provides all of the crucial spectroscopic information relating to she protein orientation; active Site of the protein, and the lipid bilayer and also direct electrochemical determination of the catalytic H-2 oxidation by the enzyme",

keywords = "HYDROGENASE, LACCASE, DESULFOVIBRIO-VULGARIS HILDENBOROUGH, IMMOBILIZATION, NIFE, ELECTRODE",

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AB - Electrochemical SEIRA is the method of choice for characterizing a lipid-bilayer-anchored, membrane bound hydrogenase Immobilized on a gold electrode. This setup allows the study of the enzyme under conditions mimicking its natural environment. A single experiment provides all of the crucial spectroscopic information relating to she protein orientation; active Site of the protein, and the lipid bilayer and also direct electrochemical determination of the catalytic H-2 oxidation by the enzyme

KW - HYDROGENASE

KW - LACCASE

KW - DESULFOVIBRIO-VULGARIS HILDENBOROUGH

KW - IMMOBILIZATION

KW - NIFE

KW - ELECTRODE

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DO - 10.1021/jz4013678

M3 - Article

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