Abstract：
:To reduce ribonucleotides to deoxyribonucleotides, the manganese-bound form of class Ib ribonucleotide reductase (RNR) must be activated via a pathway that involves redox protein(s). The reduced flavoprotein NrdI is an important protein in this pathway, as it reduces dioxygen to superoxide. Superoxide then reacts with the RNR Mn(II)2 site to generate a tyrosyl radical that is required for catalysis. A native NrdI reductase has not yet been identified. We herein demonstrate through kinetic and spectroscopic studies that an endogenous flavodoxin reductase can function as the NrdI reductase in Bacillus cereus. When the flavodoxin reductase reduces NrdI, tyrosyl radical formation in RNR is promoted under aerobic conditions, significantly increasing the radical yield. Thus, a missing piece of the class Ib RNR NrdI redox pathway has finally been identified.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Lofstad M,Gudim I,Hammerstad M,Røhr ÅK,Hersleth HPdoi
10.1021/acs.biochem.6b00699subject
Has Abstractpub_date
2016-09-13 00:00:00pages
4998-5001issue
36eissn
0006-2960issn
1520-4995journal_volume
55pub_type
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