Binding of a single nitric oxide molecule is sufficient to disrupt DNA binding of the nitrosative stress regulator NsrR.

The regulatory protein NsrR, a member of the Rrf2 protein superfamily, plays a major role in the cellular response to nitrosative stress in many benign and pathogenic bacteria. The homodimeric protein binds a [4Fe-4S] cluster in each subunit (termed holo NsrR), and represses transcription of genes primarily involved in NO detoxification. Holo NsrR reacts rapidly with multiple NO molecules per [4Fe-4S] cluster, a complex reaction, with loss of DNA binding and formation of NsrR-bound iron-nitrosyl species.

Synergy of native mass spectrometry and other biophysical techniques in studies of iron‑sulfur cluster proteins and their assembly.

The application of mass spectrometric methodologies has revolutionised biological chemistry, from identification through to structural and conformational studies of proteins and other macromolecules. Native mass spectrometry (MS), in which proteins retain their native structure, is a rapidly growing field. This is particularly the case for studies of metalloproteins, where non-covalently bound cofactors remain bound following ionisation.

CyaY and TusA regulate ISC- and SUF-mediated l-cysteine desulfurase activity.

CyaY, the frataxin homolog of , plays an important role in ISC iron-sulfur cluster assembly through interactions with the cysteine desulfurase IscS, which regulate the supply of sulfur. IscS is not exclusive for ISC Fe-S cluster assembly, as it functions as a hub for the supply of sulfur to a number of other sulfur-requiring pathways, such as for the biosynthesis of Moco and thiolated tRNAs. How the balance of sulfur supply to the various competing pathways is achieved is not fully understood, but a network of protein-protein interactions plays a key role.

Hydrothermal Carbonization of Biomass for Electrochemical Energy Storage: Parameters, Mechanisms, Electrochemical Performance, and the Incorporation of Transition Metal Dichalcogenide Nanoparticles.

Given the pressing climate and sustainability challenges, shifting industrial processes towards environmentally friendly practices is imperative. Among various strategies, the generation of green, flexible materials combined with efficient reutilization of biomass stands out. This review provides a comprehensive analysis of the hydrothermal carbonization (HTC) process as a sustainable approach for developing carbonaceous materials from biomass.

Binding of IscU and TusA to different but competing sites of IscS influences the activity of IscS and directs sulfur to the respective biomolecular synthesis pathway.

All sulfur transfer pathways generally have in common an l-cysteine desulfurase as the initial sulfur-mobilizing enzyme, which serves as a sulfur donor for the biosynthesis of numerous sulfur-containing biomolecules in the cell. In , the housekeeping l-cysteine desulfurase IscS functions as a hub for sulfur transfer through interactions with several partner proteins, which bind at different sites on IscS. So far, the interaction sites of IscU, Fdx, CyaY, and IscX involved in iron sulfur (Fe-S) cluster assembly, TusA, required for molybdenum cofactor biosynthesis and mnmsU34 transfer RNA (tRNA) modifications, and ThiI, involved in both the biosynthesis of thiamine and sU8 tRNA modifications, have been mapped.