Ribonucleotide reductase (RNR) is a key enzyme that mediates the synthesis of
deoxyribonucleotides, the DNA precursors, for DNA synthesis in every living cell. This …

Microorganisms play a dominant role in the biogeochemical cycling of nutrients. They are
rightly praised for their facility for fixing both carbon and nitrogen into organic matter, and …

Cell signaling relies extensively on dynamic pools of redox-inactive metal ions such as
sodium, potassium, calcium and zinc, but their redox-active transition metal counterparts …

Metal ions provide considerable functionality across biological systems, and their utilization
within biomolecules has adapted through changes in the chemical environment to maintain …

Incorporation of metallocofactors essential for the activity of many enyzmes is a major
mechanism of posttranslational modification. The cellular machinery required for these …

In most organisms, transition metal ions are necessary cofactors of ribonucleotide reductase
(RNR), the enzyme responsible for biosynthesis of the 2′-deoxynucleotide building blocks …

How cells ensure correct metallation of a given protein and whether a degree of promiscuity
in metal binding has evolved are largely unanswered questions. In a classic case, iron-and …

The genome of Escherichia coli encodes two class I ribonucleotide reductases. The first,
NrdAB, is a well‐studied iron‐dependent enzyme that is essential for aerobic growth. The …

The class Ib ribonucleotide reductase of Escherichia coli can initiate reduction of nucleotides
to deoxynucleotides with either a MnIII2-tyrosyl radical (Y•) or a FeIII2-Y• cofactor in the NrdF …

Escherichia coli class Ib ribonucleotide reductase (RNR) converts nucleoside 5′-
diphosphates to deoxynucleoside 5′-diphosphates and is expressed under iron-limited …