A mixed valence form of the iron cluster in the B2 protein of ribonucleotide reductase from Escherichia coli

Michael P. Hendrich; Timothy E. Elgren; Lawrence Que

doi:10.1016/S0006-291X(05)80241-4

A mixed valence form of the iron cluster in the B2 protein of ribonucleotide reductase from Escherichia coli

Michael P. Hendrich, Timothy E. Elgren, Lawrence Que

Chemistry (Twin Cities)

Research output: Contribution to journal › Article › peer-review

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Abstract

A mixed valent form of the iron cluster (Fe(II)Fe(III)) in the B2 protein of ribonucleotide reductase has been isolated and characterized. The irons in this state of the protein are ferromagnetically coupled as indicated by the observation of a novel S = 9/2 EPR spectrum. This is the first ferromagnetically coupled Fe(II)Fe(III) cluster reported for a protein and the first observation of the mixed valence form of ribonucleotide reductase.

Original language	English (US)
Pages (from-to)	705-710
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	176
Issue number	2
DOIs	https://doi.org/10.1016/S0006-291X(05)80241-4
State	Published - Apr 30 1991

Bibliographical note

Funding Information:
This work was supported by grants from the National Institute of Health, GM-12996 (M. P. H.), and from the National Science Foundation, DMB-8314935, DMB-8804458 (L. Q.). We thank Professor Joanne Stubbe for providing E. coli strain N6405/pSPS2 used in these experiments.

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title = "A mixed valence form of the iron cluster in the B2 protein of ribonucleotide reductase from Escherichia coli",

abstract = "A mixed valent form of the iron cluster (Fe(II)Fe(III)) in the B2 protein of ribonucleotide reductase has been isolated and characterized. The irons in this state of the protein are ferromagnetically coupled as indicated by the observation of a novel S = 9/2 EPR spectrum. This is the first ferromagnetically coupled Fe(II)Fe(III) cluster reported for a protein and the first observation of the mixed valence form of ribonucleotide reductase.",

author = "Hendrich, {Michael P.} and Elgren, {Timothy E.} and Lawrence Que",

note = "Funding Information: This work was supported by grants from the National Institute of Health, GM-12996 (M. P. H.), and from the National Science Foundation, DMB-8314935, DMB-8804458 (L. Q.). We thank Professor Joanne Stubbe for providing E. coli strain N6405/pSPS2 used in these experiments.",

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T1 - A mixed valence form of the iron cluster in the B2 protein of ribonucleotide reductase from Escherichia coli

AU - Hendrich, Michael P.

AU - Elgren, Timothy E.

AU - Que, Lawrence

N1 - Funding Information: This work was supported by grants from the National Institute of Health, GM-12996 (M. P. H.), and from the National Science Foundation, DMB-8314935, DMB-8804458 (L. Q.). We thank Professor Joanne Stubbe for providing E. coli strain N6405/pSPS2 used in these experiments.

PY - 1991/4/30

Y1 - 1991/4/30

N2 - A mixed valent form of the iron cluster (Fe(II)Fe(III)) in the B2 protein of ribonucleotide reductase has been isolated and characterized. The irons in this state of the protein are ferromagnetically coupled as indicated by the observation of a novel S = 9/2 EPR spectrum. This is the first ferromagnetically coupled Fe(II)Fe(III) cluster reported for a protein and the first observation of the mixed valence form of ribonucleotide reductase.

AB - A mixed valent form of the iron cluster (Fe(II)Fe(III)) in the B2 protein of ribonucleotide reductase has been isolated and characterized. The irons in this state of the protein are ferromagnetically coupled as indicated by the observation of a novel S = 9/2 EPR spectrum. This is the first ferromagnetically coupled Fe(II)Fe(III) cluster reported for a protein and the first observation of the mixed valence form of ribonucleotide reductase.

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A mixed valence form of the iron cluster in the B2 protein of ribonucleotide reductase from Escherichia coli

Abstract

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