Change search
ReferencesLink to record
Permanent link

Direct link
The class Ib ribonucleotide reductase from Mycobacterium tuberculosis has two active R2F subunits
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. University of Oslo, Norway.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Show others and affiliations
2014 (English)In: Journal of Biological Inorganic Chemistry, ISSN 0949-8257, E-ISSN 1432-1327, Vol. 19, no 6, 893-902 p.Article in journal (Refereed) Published
Abstract [en]

Ribonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides to their corresponding deoxyribonucleotides, playing a crucial role in DNA repair and replication in all living organisms. Class Ib RNRs require either a diiron-tyrosyl radical (Y center dot) or a dimanganese-Y center dot cofactor in their R2F subunit to initiate ribonucleotide reduction in the R1 subunit. Mycobacterium tuberculosis, the causative agent of tuberculosis, contains two genes, nrdF1 and nrdF2, encoding the small subunits R2F-1 and R2F-2, respectively, where the latter has been thought to serve as the only active small subunit in the M. tuberculosis class Ib RNR. Here, we present evidence for the presence of an active Fe (2) (III) -Y center dot cofactor in the M. tuberculosis RNR R2F-1 small subunit, supported and characterized by UV-vis, X-band electron paramagnetic resonance, and resonance Raman spectroscopy, showing features similar to those for the M. tuberculosis R2F-2-Fe (2) (III) -Y center dot cofactor. We also report enzymatic activity of Fe (2) (III) -R2F-1 when assayed with R1, and suggest that the active M. tuberculosis class Ib RNR can use two different small subunits, R2F-1 and R2F-2, with similar activity.

Place, publisher, year, edition, pages
2014. Vol. 19, no 6, 893-902 p.
Keyword [en]
Ribonucleotide reductase, R2, Tyrosyl radical, Mycobacterium tuberculosis, Iron
National Category
Biological Sciences Chemical Sciences
URN: urn:nbn:se:su:diva-107026DOI: 10.1007/s00775-014-1121-xISI: 000339975100015OAI: diva2:743621


Available from: 2014-09-04 Created: 2014-09-02 Last updated: 2014-09-04Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text

Search in DiVA

By author/editor
Gräslund, AstridHögbom, Martin
By organisation
Department of Biochemistry and Biophysics
In the same journal
Journal of Biological Inorganic Chemistry
Biological SciencesChemical Sciences

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 19 hits
ReferencesLink to record
Permanent link

Direct link