C. S. Yee

发表

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 reductase.

J. Stubbe, M. Seyedsayamdost, C. S. Yee, 2011, Biochemistry.

Radical initiation in the class I ribonucleotide reductase: long-range proton-coupled electron transfer?

Michelle C. Y. Chang, D. Nocera, J. Stubbe, 2003, Chemical reviews.

Site-specific incorporation of fluorotyrosines into the R2 subunit of E. coli ribonucleotide reductase by expressed protein ligation

J. Stubbe, M. Seyedsayamdost, C. S. Yee, 2007, Nature Protocols.

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 pathway.

D. Nocera, Steven Y. Reece, J. Stubbe, 2006, Journal of the American Chemical Society.

2,3-difluorotyrosine at position 356 of ribonucleotide reductase R2: a probe of long-range proton-coupled electron transfer.

D. Nocera, J. Stubbe, J. Ge, 2003, Journal of the American Chemical Society.

The evolution of ribonucleotide reduction revisited.

J. Stubbe, J. Ge, C. S. Yee, 2001, Trends in biochemical sciences.

Turning on ribonucleotide reductase by light-initiated amino acid radical generation.

D. Nocera, J. Stubbe, C. S. Yee, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Use of 2,3,5-F 3 Y- β 2 and 3-NH 2 Y- α 2 to study PCET in E. coli Ribonucleotide Reductase

J. Stubbe, M. Seyedsayamdost, C. S. Yee, 2011 .

Use of 2,3,5-F[subscript 3]Y-beta 2 and 3-NH[subscript 2]Y-alpha 2 To Study Proton-Coupled Electron Transfer in Escherichia coli Ribonucleotide Reductase

J. Stubbe, M. Seyedsayamdost, C. S. Yee, 2010 .

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 process.

D. Nocera, J. Stubbe, M. Seyedsayamdost, 2003, Biochemistry.

Site-specific replacement of a conserved tyrosine in ribonucleotide reductase with an aniline amino acid: a mechanistic probe for a redox-active tyrosine.

D. Nocera, J. Stubbe, C. S. Yee, 2004, Journal of the American Chemical Society.