| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 9582547 | Chemical Physics Letters | 2005 | 5 Pages |
Abstract
Phosphorescence of single protein molecules has been directly observed by laser confocal microscopy. The native horseradish peroxidase (HRP) has been converted into a phosphorescent analog (Pt-HRP) by replacing the heme prosthetic group with platinum mesoporphyrin IX (Pt-MP). Oxygen quenching of the triplet state emission of single Pt-HRP molecules has been directly detected and the oxygen quenching constant could be estimated at the single molecule level. The method lays a foundation for experimental studies of the pathways of oxygen diffusion in proteins.
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Authors
Erwen Mei, Feng Gao, Sergei Vinogradov, Jane M. Vanderkooi, Robin M. Hochstrasser,