ArticleDalton transactions (Cambridge, England : 2003)2021
Sensing mechanisms of iron-sulfur cluster regulatory proteins elucidated using native mass spectrometry.
Article in Dalton transactions (Cambridge, England : 2003), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.
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Who cites it
12 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Meta-analysis Driven Strain Design for Mitigating Oxidative Stresses Important in Biomanufacturing.ACS synthetic biology · 2024Pooled it
- An Aerobic in Vitro Cell Lysate-based Method for Fe-S Cluster Reconstitution in Recombinant Rv1460 Protein from Mycobacterium tuberculosis H37Rv.Applied biochemistry and biotechnology · 2026Article
- NRVS of FeS cluster proteins & models - A bestiary of nifty normal modes.Journal of inorganic biochemistry · 2025Review
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Proteomic strategies to interrogate the Fe-S proteome.Biochimica et biophysica acta. Molecular cell research · 2024Review
- The methylerythritol phosphate pathway as an oxidative stress sense and response system.Nature communications · 2024Review
- Iron-sulfur protein odyssey: exploring their cluster functional versatility and challenging identification.Metallomics : integrated biometal science · 2024Review
- The Cryptic Nature of Fe-S Clusters: A Case Study of the Hepatitis B HBx Oncoprotein.Inorganics · 2023Article
- Metalloprotein enabled redox signal transduction in microbes.Current opinion in chemical biology · 2023Review
- Native mass spectrometric studies of IscSU reveal a concerted, sulfur-initiated mechanism of iron-sulfur cluster assembly.Chemical science · 2022Article
- Radical SAM Enzymes and Metallocofactor Assembly: A Structural Point of View.ACS bio & med chem Au · 2022Review
- Native mass spectrometry identifies the HybG chaperone as carrier of the Fe(CN)Scientific reports · 2021Article
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3 authors.
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Abstract
The ability to sense and respond to various key environmental cues is important for the survival and adaptability of many bacteria, including pathogens. The particular sensitivity of iron-sulfur (Fe-S) clusters is exploited in nature, such that multiple sensor-regulator proteins, which coordinate the detection of analytes with a (in many cases) global transcriptional response, are Fe-S cluster proteins. The fragility and sensitivity of these Fe-S clusters make studying such proteins difficult, and gaining insight of what they sense, and how they sense it and transduce the signal to affect transcription, is a major challenge. While mass spectrometry is very widely used in biological research, it is normally employed under denaturing conditions where non-covalently attached cofactors are lost. However, mass spectrometry under conditions where the protein retains its native structure and, thus, cofactors, is now itself a flourishing field, and the application of such 'native' mass spectrometry to study metalloproteins is now relatively widespread. Here we describe recent advances in using native MS to study Fe-S cluster proteins. Through its ability to accurately measure mass changes that reflect chemistry occurring at the cluster, this approach has yielded a remarkable richness of information that is not accessible by other, more traditional techniques.
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