Deciphering Radical Transport in the Large Subunit of Class I Ribonucleotide Reductase
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Stubbe_Deciphering radical.pdf
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Author(s)
Stubbe, JoAnne
Nocera, Daniel G.
Holder, Patrick
Pizano, Arturo Alejandro
Anderson, Bryce Lane
Date Issued
November 2011
Journal
Journal of the American Chemical Society
Publisher
American Chemical Society (ACS)
Citation
Holder, Patrick G., Arturo A. Pizano, Bryce L. Anderson, JoAnne Stubbe, and Daniel G. Nocera. “Deciphering Radical Transport in the Large Subunit of Class I Ribonucleotide Reductase.” Journal of the American Chemical Society 134, no. 2 (January 18, 2012): 1172-1180.
Version
Author's final manuscript
Abstract
Incorporation of 2,3,6-trifluorotyrosine (F[subscript 3]Y) and a rhenium bipyridine ([Re]) photooxidant into a peptide corresponding to the C-terminus of the β protein (βC19) of Escherichia coli ribonucleotide reductase (RNR) allows for the temporal monitoring of radical transport into the α2 subunit of RNR. Injection of the photogenerated F[subscript 3]Y radical from the [Re]–F[subscript 3]Y−βC19 peptide into the surface accessible Y731 of the α2 subunit is only possible when the second Y730 is present. With the Y–Y established, radical transport occurs with a rate constant of 3 × 10[superscript 5] s[superscript –1]. Point mutations that disrupt the Y–Y dyad shut down radical transport. The ability to obviate radical transport by disrupting the hydrogen bonding network of the amino acids composing the colinear proton-coupled electron transfer pathway in α2 suggests a finely tuned evolutionary adaptation of RNR to control the transport of radicals in this enzyme.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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DOI of Published Version
https://doi.org/10.1021/ja209016j
