Probing biocatalytic transformations with CdSe-ZnS QDs

Ron Gill; Ronit Freeman; Jian Ping Xu; Itamar Willner; Shira Winograd; Itzik Shweky; Uri Banin

doi:10.1021/ja066636t

Probing biocatalytic transformations with CdSe-ZnS QDs

Ron Gill
, Ronit Freeman
, Jian Ping Xu
, Itamar Willner^*
, Shira Winograd
, Itzik Shweky
, Uri Banin

^*Corresponding author for this work

Institute of Chemistry

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

177 Scopus citations

Abstract

CdSe/ZnS QDs enable the optical probing of the biocatalytic oxidation of tyrosine derivatives and of the scission of peptides by thrombin. CdSe/ZnS QDs were modified with tyrosine methyl ester or with a tyrosine-containing peptide. The tyrosine units were reacted with tyrosinase/O₂ to yield the respective l-DOPA and quinone derivatives. The luminescence of QDs modified by the enzyme-generated quinone units is quenched. The quinone-functionalized peptide associated with the QDs was cleaved by thrombin, a process that restored the luminescence of the QDs.

Original language	English
Pages (from-to)	15376-15377
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	128
Issue number	48
DOIs	https://doi.org/10.1021/ja066636t
State	Published - 6 Dec 2006

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abstract = "CdSe/ZnS QDs enable the optical probing of the biocatalytic oxidation of tyrosine derivatives and of the scission of peptides by thrombin. CdSe/ZnS QDs were modified with tyrosine methyl ester or with a tyrosine-containing peptide. The tyrosine units were reacted with tyrosinase/O2 to yield the respective l-DOPA and quinone derivatives. The luminescence of QDs modified by the enzyme-generated quinone units is quenched. The quinone-functionalized peptide associated with the QDs was cleaved by thrombin, a process that restored the luminescence of the QDs.",

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AU - Gill, Ron

AU - Freeman, Ronit

AU - Xu, Jian Ping

AU - Willner, Itamar

AU - Winograd, Shira

AU - Shweky, Itzik

AU - Banin, Uri

PY - 2006/12/6

Y1 - 2006/12/6

N2 - CdSe/ZnS QDs enable the optical probing of the biocatalytic oxidation of tyrosine derivatives and of the scission of peptides by thrombin. CdSe/ZnS QDs were modified with tyrosine methyl ester or with a tyrosine-containing peptide. The tyrosine units were reacted with tyrosinase/O2 to yield the respective l-DOPA and quinone derivatives. The luminescence of QDs modified by the enzyme-generated quinone units is quenched. The quinone-functionalized peptide associated with the QDs was cleaved by thrombin, a process that restored the luminescence of the QDs.

AB - CdSe/ZnS QDs enable the optical probing of the biocatalytic oxidation of tyrosine derivatives and of the scission of peptides by thrombin. CdSe/ZnS QDs were modified with tyrosine methyl ester or with a tyrosine-containing peptide. The tyrosine units were reacted with tyrosinase/O2 to yield the respective l-DOPA and quinone derivatives. The luminescence of QDs modified by the enzyme-generated quinone units is quenched. The quinone-functionalized peptide associated with the QDs was cleaved by thrombin, a process that restored the luminescence of the QDs.

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JF - Journal of the American Chemical Society

IS - 48

ER -

Probing biocatalytic transformations with CdSe-ZnS QDs

Abstract

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