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• W2131077681 endingPage "4039" @default.
• W2131077681 startingPage "4027" @default.
• W2131077681 abstract "Ribonucleotide reductases (RNRs) utilize radical chemistry to reduce nucleotides to deoxynucleotides in all organisms. In the class Ia and Ib RNRs, this reaction requires a stable tyrosyl radical (Y(•)) generated by oxidation of a reduced dinuclear metal cluster. The Fe(III)2-Y(•) cofactor in the NrdB subunit of the class Ia RNRs can be generated by self-assembly from Fe(II)2-NrdB, O2, and a reducing equivalent. By contrast, the structurally homologous class Ib enzymes require a Mn(III)2-Y(•) cofactor in their NrdF subunit. Mn(II)2-NrdF does not react with O2, but it binds the reduced form of a conserved flavodoxin-like protein, NrdIhq, which, in the presence of O2, reacts to form the Mn(III)2-Y(•) cofactor. Here we investigate the mechanism of assembly of the Mn(III)2-Y(•) cofactor in Bacillus subtilis NrdF. Cluster assembly from Mn(II)2-NrdF, NrdI(hq), and O2 has been studied by stopped flow absorption and rapid freeze quench EPR spectroscopies. The results support a mechanism in which NrdI(hq) reduces O2 to O2(•-) (40-48 s(-1), 0.6 mM O2), the O2(•-) channels to and reacts with Mn(II)2-NrdF to form a Mn(III)Mn(IV) intermediate (2.2 ± 0.4 s(-1)), and the Mn(III)Mn(IV) species oxidizes tyrosine to Y(•) (0.08-0.15 s(-1)). Controlled production of O2(•-) by NrdIhq during class Ib RNR cofactor assembly both circumvents the unreactivity of the Mn(II)2 cluster with O2 and satisfies the requirement for an extra reducing equivalent in Y(•) generation." @default.
• W2131077681 created "2016-06-24" @default.
• W2131077681 creator A5024009979 @default.
• W2131077681 creator A5027572501 @default.
• W2131077681 creator A5065803066 @default.
• W2131077681 creator A5086254191 @default.
• W2131077681 date "2013-02-27" @default.
• W2131077681 modified "2023-10-14" @default.
• W2131077681 title "Mechanism of Assembly of the Dimanganese-Tyrosyl Radical Cofactor of Class Ib Ribonucleotide Reductase: Enzymatic Generation of Superoxide Is Required for Tyrosine Oxidation via a Mn(III)Mn(IV) Intermediate" @default.
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• W2131077681 doi "https://doi.org/10.1021/ja312457t" @default.
• W2131077681 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3739481" @default.
• W2131077681 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23402532" @default.
• W2131077681 hasPublicationYear "2013" @default.
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