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• W2013886122 abstract "The anaerobic ribonucleotide reductase (ARR) from E. coli is the prototype for enzymes that use the combination of S-adenosylmethionine (AdoMet) and an iron-sulfur center for generating catalytically essential free radicals. ARR is a homodimeric alpha2 protein which acquires a glycyl radical during anaerobic incubation with a [4Fe-4S]-containing activating enzyme (beta) and AdoMet under reducing conditions. Here we show that the EPR-active S = 1/2 reduced [4Fe-4S]+ cluster is competent for AdoMet reductive cleavage, yielding 1 equiv of methionine and almost 1 equiv of glycyl radical. These data support the proposal that the glycyl radical results from a one-electron oxidation of the reduced cluster by AdoMet. Reduced protein beta alone is also able to reduce AdoMet but only in the presence of DTT. However, in that case, 2 equiv of methionine per reduced cluster was formed. This unusual stoichiometry and combined EPR and Mössbauer spectroscopic analysis are used to tentatively propose that AdoMet reductive cleavage proceeds by an alternative mechanism involving catalytically active [3Fe-4S] intermediate clusters." @default.
• W2013886122 created "2016-06-24" @default.
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• W2013886122 date "2001-05-17" @default.
• W2013886122 modified "2023-09-26" @default.
• W2013886122 title "Activation of Class III Ribonucleotide Reductase from <i>E. coli</i>. The Electron Transfer from the Iron−Sulfur Center to <i>S</i>-Adenosylmethionine" @default.
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• W2013886122 doi "https://doi.org/10.1021/bi002936q" @default.
• W2013886122 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11389585" @default.
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