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

Dipankar Chaudhuri, Joseph M. Bollinger, Jr.

Research output: Contribution to journalArticle

1 Citation (Scopus)

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 1 2008

Fingerprint

Ribonucleotide Reductases
Protein Subunits
Escherichia coli
proteins
Kinetics
kinetics
Spectroscopy
Escherichia
spectroscopy
Antiviral Agents
drugs
Iron
assembly
iron

All Science Journal Classification (ASJC) codes

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

Cite this

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title = "Characterization of the kinetics of Fe (II) binding by the R2 protein subunit of E. coli ribonucleotide reductase",
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) M{\"o}ssbauer spectroscopy. Based on the stopped flow absorption (SF-Abs) and CQF M{\"o}ssbauer 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.",
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Characterization of the kinetics of Fe (II) binding by the R2 protein subunit of E. coli ribonucleotide reductase. / Chaudhuri, Dipankar; Bollinger, Jr., Joseph M.

In: Hyperfine Interactions, Vol. 185, No. 1-3, 01.07.2008, p. 57-62.

Research output: Contribution to journalArticle

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