Inactivation of Lactobacillus leichmannii ribonucleotide reductase by F2CTP: adenosylcobalamin destruction and formation of a nucleotide based radical
Ribonucleotide reductase (RNR, 76 kDa) from Lactobacillus leichmannii is a class II RNR that requires adenosylcobalamin (AdoCbl) as a cofactor. It catalyzes the conversion of nucleoside triphosphates to deoxynucleotides and is 100% inactivated by 1 equiv of 2′,2′-difluoro-2′-deoxycytidine 5′-triphos...
Main Authors: | Lohman, Gregory J. S., Gerfen, Gary J., Stubbe, JoAnne |
---|---|
Other Authors: | Massachusetts Institute of Technology. Department of Biology |
Format: | Article |
Language: | en_US |
Published: |
American Chemical Society (ACS)
2012
|
Online Access: | http://hdl.handle.net/1721.1/72366 https://orcid.org/0000-0001-8076-4489 |
Similar Items
-
Inactivation of Lactobacillus leichmannii ribonucleotide reductase by F2CTP: covalent modification
by: Lohman, Gregory J. S., et al.
Published: (2012) -
Cloning, sequencing, expression, and characterization of the adenosylcobalamin-dependent ribonucleotide reductase from Lactobacillus leichmannii
by: Booker, Squire J
Published: (2006) -
Insight into the Mechanism of Inactivation of Ribonucleotide Reductase by Gemcitabine 5′-Diphosphate in the Presence or Absence of Reductant
by: Artin, Erin, et al.
Published: (2013) -
Bacillus subtilis Class Ib Ribonucleotide Reductase Is a Dimanganese(III)-Tyrosyl Radical Enzyme
by: Zhang, Yan, et al.
Published: (2012) -
Deciphering Radical Transport in the Large Subunit of Class I Ribonucleotide Reductase
by: Stubbe, JoAnne, et al.
Published: (2013)