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• W1972814606 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 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." @default.
• W1972814606 created "2016-06-24" @default.
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• W1972814606 creator A5064569232 @default.
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• W1972814606 date "2007-05-27" @default.
• W1972814606 modified "2023-10-16" @default.
• W1972814606 title "The Active Form of <i>Chlamydia trachomatis</i> Ribonucleotide Reductase R2 Protein Contains a Heterodinuclear Mn(IV)/Fe(III) Cluster with <i>S</i> = 1 Ground State" @default.
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• W1972814606 doi "https://doi.org/10.1021/ja072528a" @default.
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