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Literature summary for 1.17.4.1 extracted from

  • Pierce, B.S.; Hendrich, M.P.
    Local and global effects of metal binding within the small subunit of ribonucleotide reductase (2005), J. Am. Chem. Soc., 127, 3613-3623.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Iron construction of heterobinuclear Mn(II)Fe(II) and Mn(III)Fe(III) clusters within a single beta-protomer of the small subunit of Escherichia coli ribonucleotide reductase due to differential binding affinity of the A- and B-sites. The binding of the first metal is under kinetic control. The binding of the first Fe(II) atom to the active site in a beta-protomer induces a global protein conformational change that inhibits access of metal to the active site in the other protomer and also induces a local effect at the active site in the first protomer, which lowers the affinity for metal in the A-site Escherichia coli
Manganese construction of heterobinuclear Mn(II)Fe(II) and Mn(III)Fe(III) clusters within a single beta-protomer of the small subunit of Escherichia coli ribonucleotide reductase due to differential binding affinity of the A- and B-sites Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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