Control of metallation and active cofactor assembly in the class Ia and Ib ribonucleotide reductases: Diiron or dimanganese?

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Abstract

Ribonucleotide reductases (RNRs) convert nucleotides to deoxynucleotides in all organisms. Activity of the class Ia and Ib RNRs requires a stable tyrosyl radical (Y), which can be generated by the reaction of O2 with a diferrous cluster on the β subunit to form active diferric-Y cofactor. Recent experiments have demonstrated, however, that in vivo the class Ib RNR contains an active dimanganese(III)-Y cofactor. The similar metal binding sites of the class Ia and Ib RNRs, their ability to bind both MnII and FeII, and the activity of the class Ib RNR with both diferric-Y and dimanganese(III)-Y cofactors raise the intriguing question of how the cell prevents mismetallation of these essential enzymes. The presence of the class Ib RNR in numerous pathogenic bacteria also highlights the importance of manganese for these organisms' growth and virulence.

Original languageEnglish (US)
Pages (from-to)284-290
Number of pages7
JournalCurrent Opinion in Chemical Biology
Volume15
Issue number2
DOIs
StatePublished - Apr 1 2011

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Ribonucleotide Reductases
Manganese
Virulence
Bacteria
Nucleotides
Metals
Binding Sites
Enzymes
Growth

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Analytical Chemistry

Cite this

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title = "Control of metallation and active cofactor assembly in the class Ia and Ib ribonucleotide reductases: Diiron or dimanganese?",
abstract = "Ribonucleotide reductases (RNRs) convert nucleotides to deoxynucleotides in all organisms. Activity of the class Ia and Ib RNRs requires a stable tyrosyl radical (Y), which can be generated by the reaction of O2 with a diferrous cluster on the β subunit to form active diferric-Y cofactor. Recent experiments have demonstrated, however, that in vivo the class Ib RNR contains an active dimanganese(III)-Y cofactor. The similar metal binding sites of the class Ia and Ib RNRs, their ability to bind both MnII and FeII, and the activity of the class Ib RNR with both diferric-Y and dimanganese(III)-Y cofactors raise the intriguing question of how the cell prevents mismetallation of these essential enzymes. The presence of the class Ib RNR in numerous pathogenic bacteria also highlights the importance of manganese for these organisms' growth and virulence.",
author = "JoAnne Stubbe and {Cotruvo, Jr.}, {Joseph Alfred}",
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TY - JOUR

T1 - Control of metallation and active cofactor assembly in the class Ia and Ib ribonucleotide reductases

T2 - Diiron or dimanganese?

AU - Stubbe, JoAnne

AU - Cotruvo, Jr., Joseph Alfred

PY - 2011/4/1

Y1 - 2011/4/1

N2 - Ribonucleotide reductases (RNRs) convert nucleotides to deoxynucleotides in all organisms. Activity of the class Ia and Ib RNRs requires a stable tyrosyl radical (Y), which can be generated by the reaction of O2 with a diferrous cluster on the β subunit to form active diferric-Y cofactor. Recent experiments have demonstrated, however, that in vivo the class Ib RNR contains an active dimanganese(III)-Y cofactor. The similar metal binding sites of the class Ia and Ib RNRs, their ability to bind both MnII and FeII, and the activity of the class Ib RNR with both diferric-Y and dimanganese(III)-Y cofactors raise the intriguing question of how the cell prevents mismetallation of these essential enzymes. The presence of the class Ib RNR in numerous pathogenic bacteria also highlights the importance of manganese for these organisms' growth and virulence.

AB - Ribonucleotide reductases (RNRs) convert nucleotides to deoxynucleotides in all organisms. Activity of the class Ia and Ib RNRs requires a stable tyrosyl radical (Y), which can be generated by the reaction of O2 with a diferrous cluster on the β subunit to form active diferric-Y cofactor. Recent experiments have demonstrated, however, that in vivo the class Ib RNR contains an active dimanganese(III)-Y cofactor. The similar metal binding sites of the class Ia and Ib RNRs, their ability to bind both MnII and FeII, and the activity of the class Ib RNR with both diferric-Y and dimanganese(III)-Y cofactors raise the intriguing question of how the cell prevents mismetallation of these essential enzymes. The presence of the class Ib RNR in numerous pathogenic bacteria also highlights the importance of manganese for these organisms' growth and virulence.

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