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Cyril S Yee

Showing results (1-10 of 7) with videos related to

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Nature Protocols|June 5, 2007
Site-specific incorporation of fluorotyrosines into the R2 subunit of E. coli ribonucleotide reductase by expressed protein ligationMohammad R Seyedsayamdost, Cyril S Yee, Joanne Stubbe
Biochemistry|December 25, 2010
Use of 2,3,5-F(3)Y-β2 and 3-NH(2)Y-α2 to study proton-coupled electron transfer in Escherichia coli ribonucleotide reductaseMohammad R Seyedsayamdost, Cyril S Yee, JoAnne Stubbe
Journal of the American Chemical Society|December 23, 2004
Site-specific replacement of a conserved tyrosine in ribonucleotide reductase with an aniline amino acid: a mechanistic probe for a redox-active tyrosineMichelle C Y Chang, Cyril S Yee, Daniel G Nocera, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 5, 2004
Turning on ribonucleotide reductase by light-initiated amino acid radical generationMichelle C Y Chang, Cyril S Yee, JoAnne Stubbe, et al.
Journal of the American Chemical Society|August 28, 2003
2,3-difluorotyrosine at position 356 of ribonucleotide reductase R2: a probe of long-range proton-coupled electron transferCyril S Yee, Michelle C Y Chang, Jie Ge, et al.
Journal of the American Chemical Society|February 2, 2006
pH Rate profiles of FnY356-R2s (n = 2, 3, 4) in Escherichia coli ribonucleotide reductase: evidence that Y356 is a redox-active amino acid along the radical propagation pathwayMohammad R Seyedsayamdost, Cyril S Yee, Steven Y Reece, et al.
Biochemistry|December 10, 2003
Generation of the R2 subunit of ribonucleotide reductase by intein chemistry: insertion of 3-nitrotyrosine at residue 356 as a probe of the radical initiation processCyril S Yee, Mohammad R Seyedsayamdost, Michelle C Y Chang, et al.
Pageof 1

Showing results (1-10 of 7) with videos related to

Sort By:
Pageof 1
Nature Protocols|June 5, 2007
Site-specific incorporation of fluorotyrosines into the R2 subunit of E. coli ribonucleotide reductase by expressed protein ligationMohammad R Seyedsayamdost, Cyril S Yee, Joanne Stubbe
Biochemistry|December 25, 2010
Use of 2,3,5-F(3)Y-β2 and 3-NH(2)Y-α2 to study proton-coupled electron transfer in Escherichia coli ribonucleotide reductaseMohammad R Seyedsayamdost, Cyril S Yee, JoAnne Stubbe
Journal of the American Chemical Society|December 23, 2004
Site-specific replacement of a conserved tyrosine in ribonucleotide reductase with an aniline amino acid: a mechanistic probe for a redox-active tyrosineMichelle C Y Chang, Cyril S Yee, Daniel G Nocera, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 5, 2004
Turning on ribonucleotide reductase by light-initiated amino acid radical generationMichelle C Y Chang, Cyril S Yee, JoAnne Stubbe, et al.
Journal of the American Chemical Society|August 28, 2003
2,3-difluorotyrosine at position 356 of ribonucleotide reductase R2: a probe of long-range proton-coupled electron transferCyril S Yee, Michelle C Y Chang, Jie Ge, et al.
Journal of the American Chemical Society|February 2, 2006
pH Rate profiles of FnY356-R2s (n = 2, 3, 4) in Escherichia coli ribonucleotide reductase: evidence that Y356 is a redox-active amino acid along the radical propagation pathwayMohammad R Seyedsayamdost, Cyril S Yee, Steven Y Reece, et al.
Biochemistry|December 10, 2003
Generation of the R2 subunit of ribonucleotide reductase by intein chemistry: insertion of 3-nitrotyrosine at residue 356 as a probe of the radical initiation processCyril S Yee, Mohammad R Seyedsayamdost, Michelle C Y Chang, et al.
Pageof 1