Characterization of the kinetics of Fe (II) binding by the R2 protein subunit of E. coli ribonucleotide reductase

Dipankar Chaudhuri, Joseph Martin Bollinger

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

The kinetics of Fe(II) binding to Escherichia coli Ribonucleotide reductase (R2) has been studied using rapid kinetics techniques including chemical quenched flow (CQF) Mössbauer spectroscopy. Based on the stopped flow absorption (SF-Abs) and CQF Mössbauer spectroscopy results, the pre-steady kinetics of binding of Fe(II) to the two sites A and B on R2 have been established with attendant conformational changes. Fe (II) binds to Site B tighter and faster and these and other results provide important information towards the di-iron cofactor assembly mechanism in R2 and could have possible implications for the development of modified and new anticancer and antiviral drugs.

Original languageEnglish (US)
Pages (from-to)57-62
Number of pages6
JournalHyperfine Interactions
Volume185
Issue number1-3
DOIs
StatePublished - Jul 2008

All Science Journal Classification (ASJC) codes

  • Atomic and Molecular Physics, and Optics
  • Nuclear and High Energy Physics
  • Condensed Matter Physics
  • Physical and Theoretical Chemistry

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