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

Dipankar Chaudhuri; Joseph Martin Bollinger

doi:10.1007/s10751-008-9811-9

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

Dipankar Chaudhuri, Joseph Martin Bollinger

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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 language	English (US)
Pages (from-to)	57-62
Number of pages	6
Journal	Hyperfine Interactions
Volume	185
Issue number	1-3
DOIs	https://doi.org/10.1007/s10751-008-9811-9
State	Published - 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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10.1007/s10751-008-9811-9

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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.",

author = "Dipankar Chaudhuri and Bollinger, {Joseph Martin}",

note = "Funding Information: Acknowledgements Financial support from the National Institutes of Health NIH (GM-55365 to J.M.B., Jr.), Department of Biochemistry and Molecular Biology, Pennsylvania State University, Shuxian Chen and Vincent Huynh, Emory University, Atlanta.",

year = "2008",

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doi = "10.1007/s10751-008-9811-9",

language = "English (US)",

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T1 - Characterization of the kinetics of Fe (II) binding by the R2 protein subunit of E. coli ribonucleotide reductase

AU - Chaudhuri, Dipankar

AU - Bollinger, Joseph Martin

N1 - Funding Information: Acknowledgements Financial support from the National Institutes of Health NIH (GM-55365 to J.M.B., Jr.), Department of Biochemistry and Molecular Biology, Pennsylvania State University, Shuxian Chen and Vincent Huynh, Emory University, Atlanta.

PY - 2008/7

Y1 - 2008/7

N2 - 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.

AB - 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.

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

Abstract

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