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The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant
Author(s) -
Yifeng Wei,
Michael A. Funk,
Leonardo Astolfi Rosado,
Jiyeon Baek,
Catherine L. Drennan,
JoAnne Stubbe
Publication year - 2014
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.1414396111
Subject(s) - ribonucleotide reductase , ribonucleotide , formate , nucleotide , biochemistry , archaea , thioredoxin , biology , deoxyribonucleotides , chemistry , enzyme , protein subunit , gene , catalysis
The class III anaerobic ribonucleotide reductases (RNRs) studied to date couple the reduction of ribonucleotides to deoxynucleotides with the oxidation of formate to CO2. Here we report the cloning and heterologous expression of the Neisseria bacilliformis class III RNR and show that it can catalyze nucleotide reduction using the ubiquitous thioredoxin/thioredoxin reductase/NADPH system. We present a structural model based on a crystal structure of the homologous Thermotoga maritima class III RNR, showing its architecture and the position of conserved residues in the active site. Phylogenetic studies suggest that this form of class III RNR is present in bacteria and archaea that carry out diverse types of anaerobic metabolism.

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