A manganese(IV)/iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase

Wei Jiang, Danny Yun, Lana Saleh, Eric W. Barr, Gang Xing, Lee M. Hoffart, Monique Anne Maslak, Carsten Krebs, J. Martin Bollinger

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In a conventional class I ribonucleotide reductase (RNR), a diiron(II/II) cofactor in the R2 subunit reacts with oxygen to produce a diiron(III/IV) intermediate, which generates a stable tyrosyl radical (Y*). The Y* reversibly oxidizes a cysteine residue in the R1 subunit to a cysteinyl radical (C*), which abstracts the 3′-hydrogen of the substrate to initiate its reduction. The RNR from Chlamydia trachomatis lacks the Y*, and it had been proposed that the diiron(III/IV) complex in R2 directly generates the C* in R1. By enzyme activity measurements and spectroscopic methods, we show that this RNR actually uses a previously unknown stable manganese(IV)/iron(III) cofactor for radical initiation.

Original languageEnglish (US)
Pages (from-to)1188-1191
Number of pages4
Issue number5828
StatePublished - May 25 2007


All Science Journal Classification (ASJC) codes

  • General

Cite this

Jiang, W., Yun, D., Saleh, L., Barr, E. W., Xing, G., Hoffart, L. M., Maslak, M. A., Krebs, C., & Bollinger, J. M. (2007). A manganese(IV)/iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase. Science, 316(5828), 1188-1191. https://doi.org/10.1126/science.1141179