The diferric-tyrosyl radical cluster of ribonucleotide reductase and cytosolic iron-sulfur clusters have distinct and similar biogenesis requirements.

The Journal of Biological Chemistry
Haoran LiMingxia Huang

Abstract

How each metalloprotein assembles the correct metal at the proper binding site presents challenges to the cell. The di-iron enzyme ribonucleotide reductase (RNR) uses a diferric-tyrosyl radical (FeIII2-Y•) cofactor to initiate nucleotide reduction. Assembly of this cofactor requires O2, FeII, and a reducing equivalent. Recent studies show that RNR cofactor biosynthesis shares the same source of iron, in the form of [2Fe-2S]-GSH2 from the monothiol glutaredoxin Grx3/4, and the same electron source, in the form of the Dre2-Tah18 electron transfer chain, with the cytosolic iron-sulfur protein assembly (CIA) machinery required for maturation of [4Fe-4S] clusters in cytosolic and nuclear proteins. Here, we further investigated the interplay between the formation of the FeIII2-Y• cofactor in RNR and the cellular iron-sulfur (Fe-S) protein biogenesis pathways by examining both the iron loading into the RNR β subunit and the RNR catalytic activity in yeast mutants depleted of individual components of the mitochondrial iron-sulfur cluster assembly (ISC) and the CIA machineries. We found that both iron loading and cofactor assembly in RNR are dependent on the ISC machinery. We also found that Dre2 is required for RNR cofactor formation b...Continue Reading

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Sep 19, 2019·Metallomics : Integrated Biometal Science·Paul A Lindahl
Aug 24, 2021·Journal of the American Chemical Society·JoAnne Stubbe, Daniel G Nocera
Sep 28, 2020·Biochimica Et Biophysica Acta. Bioenergetics·Carsten BerndtUlrich Mühlenhoff
Oct 13, 2020·Biochimica Et Biophysica Acta. Molecular Cell Research·Matthias MisslingerHubertus Haas

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