ErpA, an iron sulfur (Fe S) protein of the A-type essential for respiratory metabolism in Escherichia coli.

Understanding the biogenesis of iron-sulfur (Fe-S) proteins is relevant to many fields, including bioenergetics, gene regulation, and cancer research. Several multiprotein complexes assisting Fe-S assembly have been identified in both prokaryotes and eukaryotes. Here, we identify in Escherichia coli an A-type Fe-S protein that we named ErpA.

Layered inorganic materials as redox agents: ferrocenium-intercalated zirconium phosphate.

The direct intercalation reaction of ferrocene (bis(eta5-cyclopentadienyl)iron(II), Fc) with a highly hydrated layered zirconium phosphate (ZrP) resulted in the formation of the ferrocenium ion (Fc+) within the ZrP material. The Fc+-intercalated ZrP material has an interlayer distance of 10.7 A.

Dinucleotide spore photoproduct, a minimal substrate of the DNA repair spore photoproduct lyase enzyme from Bacillus subtilis.

The overwhelming majority of DNA photoproducts in UV-irradiated spores is a unique thymine dimer called spore photoproduct (SP, 5-thymine-5,6-dihydrothymine). This lesion is repaired by the spore photoproduct lyase (SP lyase) enzyme that directly reverts SP to two unmodified thymines. The SP lyase is an S-adenosylmethionine-dependent iron-sulfur protein that belongs to the radical S-adenosylmethionine superfamily.