The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state

Wei Jiang; J. Martin Bollinger; Carsten Krebs

doi:10.1021/ja072528a

The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state

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Abstract

The class I ribonucleotide reductase from Chlamydia trachomatis uses a stable Mn^IV/Fe^III cofactor to initiate nucleotide reduction by a free-radical mechanism. The enzyme provides the first example both of a Mn-dependent ribonucleotide reductase and of a Mn/Fe redox cofactor. In this work, we have used variable-field Mössbauer spectroscopy to demonstrate that the active cofactor has an S = 1 ground state due to antiferromagnetic coupling between the Mn^IV (S^Mn = 3/2) and high-spin Fe^III (S_Fe = 5/2) sites.

Original language	English (US)
Pages (from-to)	7504-7505
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	129
Issue number	24
DOIs	https://doi.org/10.1021/ja072528a
State	Published - Jun 20 2007

All Science Journal Classification (ASJC) codes

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja072528a

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title = "The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state",

abstract = "The class I ribonucleotide reductase from Chlamydia trachomatis uses a stable MnIV/FeIII cofactor to initiate nucleotide reduction by a free-radical mechanism. The enzyme provides the first example both of a Mn-dependent ribonucleotide reductase and of a Mn/Fe redox cofactor. In this work, we have used variable-field M{\"o}ssbauer spectroscopy to demonstrate that the active cofactor has an S = 1 ground state due to antiferromagnetic coupling between the MnIV (SMn = 3/2) and high-spin FeIII (SFe = 5/2) sites.",

author = "Wei Jiang and Bollinger, \{J. Martin\} and Carsten Krebs",

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T1 - The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state

AU - Jiang, Wei

AU - Bollinger, J. Martin

AU - Krebs, Carsten

PY - 2007/6/20

Y1 - 2007/6/20

N2 - The class I ribonucleotide reductase from Chlamydia trachomatis uses a stable MnIV/FeIII cofactor to initiate nucleotide reduction by a free-radical mechanism. The enzyme provides the first example both of a Mn-dependent ribonucleotide reductase and of a Mn/Fe redox cofactor. In this work, we have used variable-field Mössbauer spectroscopy to demonstrate that the active cofactor has an S = 1 ground state due to antiferromagnetic coupling between the MnIV (SMn = 3/2) and high-spin FeIII (SFe = 5/2) sites.

AB - The class I ribonucleotide reductase from Chlamydia trachomatis uses a stable MnIV/FeIII cofactor to initiate nucleotide reduction by a free-radical mechanism. The enzyme provides the first example both of a Mn-dependent ribonucleotide reductase and of a Mn/Fe redox cofactor. In this work, we have used variable-field Mössbauer spectroscopy to demonstrate that the active cofactor has an S = 1 ground state due to antiferromagnetic coupling between the MnIV (SMn = 3/2) and high-spin FeIII (SFe = 5/2) sites.

UR - https://www.scopus.com/pages/publications/34250811950

UR - https://www.scopus.com/pages/publications/34250811950#tab=citedBy

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JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 24

ER -

The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state

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