Journal article

Allyl sulfides are privileged substrates in aqueous cross-metathesis: application to site-selective protein modification.

Abstract:: Allyl sulfides undergo efficient cross-metathesis in aqueous media with Hoveyda-Grubbs second generation catalyst 1. The high reactivity of allyl sulfides in cross-metathesis was exploited in the first examples of cross-metathesis on a protein surface. S-Allylcysteine was incorporated chemically into the protein, providing the requisite allyl sulfide handle. Preliminary efforts to genetically incorporate S-allylcysteine into proteins are also reported.

Publication status:: Published

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APA Style

Lin, Y., Chalker, J., Floyd, N., Bernardes, G., & Davis, B. (2008). Allyl sulfides are privileged substrates in aqueous cross-metathesis: application to site-selective protein modification. Journal of the American Chemical Society, 130(30), 9642–9643.

MLA Style

Lin, Y, et al. “Allyl Sulfides Are Privileged Substrates in Aqueous Cross-Metathesis: Application to Site-Selective Protein Modification.” Journal of the American Chemical Society, vol. 130, no. 30, 2008, pp. 9642–43.

Chicago Style

Lin, Y, J Chalker, N Floyd, G Bernardes, and B Davis. 2008. “Allyl Sulfides Are Privileged Substrates in Aqueous Cross-Metathesis: Application to Site-Selective Protein Modification.” Journal of the American Chemical Society 130 (30): 9642–43.
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Publisher copy:: 10.1021/ja8026168

Authors

+ Lin, Y More by this author

Role:: Author

+ Chalker, J More by this author

Role:: Author

+ Floyd, N More by this author

Role:: Author

+ Bernardes, G More by this author

Role:: Author

+ Davis, B More by this author

Institution:: University of Oxford
Division:: MPLS
Department:: Chemistry
Sub department:: Organic Chemistry
Role:: Author

Journal:: Journal of the American Chemical Society More from this journal
Volume:: 130
Issue:: 30
Pages:: 9642-9643
Publication date:: 2008-07-01
DOI:: 10.1021/ja8026168
EISSN:: 1520-5126
ISSN:: 0002-7863

Language:: English
Keywords:: Methionine

Sulfides

Allyl Compounds

Escherichia coli

Bacillus

Models, Molecular

Bacterial Proteins

Subtilisin

Cysteine

Water

Glucosidases
Pubs id:: pubs:34292
UUID:: uuid:1b6eb320-c78c-400d-b5df-235389590684
Local pid:: pubs:34292
Source identifiers:: 34292
Deposit date:: 2012-12-19
ARK identifier:: ark:/29072/ora_1b6eb320c78c400db5df235389590684

Terms of use

Copyright date:: 2008

Licence:: Terms and Conditions of Use for Oxford University Research Archive

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