Probing redox proteins on a gold surface by single molecule fluorescence spectroscopy

The interaction between the fluorescently labeled redox protein, azurin, and a thin gold film is characterized using single-molecule fluorescence intensity and lifetime measurements. Fluorescence quenching starts at distances below 2.3 nm from the gold surface. At shorter distances the quantum yield...

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Bibliographic Details
Published in:The Journal of chemical physics 2012-06, Vol.136 (23), p.235101-235101
Main Authors: Elmalk, Abdalmohsen T, Salverda, Jante M, Tabares, Leandro C, Canters, Gerard W, Aartsma, Thijs J
Format: Article
Language:English
Subjects:
Azurin - chemistry
Bacterial Proteins - chemistry
Gold - chemistry
Immobilized Proteins - chemistry
Models, Molecular
Oxidation-Reduction
Pseudomonas aeruginosa - chemistry
Spectrometry, Fluorescence - methods
Surface Properties
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Summary:The interaction between the fluorescently labeled redox protein, azurin, and a thin gold film is characterized using single-molecule fluorescence intensity and lifetime measurements. Fluorescence quenching starts at distances below 2.3 nm from the gold surface. At shorter distances the quantum yield may decrease down to fourfold for direct attachment of the protein to bare gold. Outside of the quenching range, up to fivefold enhancement of the fluorescence is observed on average with increasing roughness of the gold layer. Fluorescence-detected redox activity of individual azurin molecules, with a lifetime switching ratio of 0.4, is demonstrated for the first time close to a gold surface.
ISSN:0021-9606
1089-7690
DOI:10.1063/1.4728107