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

Crack, Jason C. and Le Brun, Nick E. ORCID: https://orcid.org/0000-0001-9780-4061 (2025) Synergy of native mass spectrometry and other biophysical techniques in studies of iron sulfur cluster proteins and their assembly. Biochimica Et Biophysica Acta-Molecular Cell Research, 1872 (1). ISSN 0167-4889

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Abstract

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. Such metalloproteins include those that contain an iron‑sulfur (Fesingle bondS) cluster and, despite their fragility and O2 sensitivity, they have been a particular focus for applications of native MS because of its capacity to accurately monitor mass changes that reveal chemical changes at the cluster. Here we review recent advances in these applications of native MS, which, together with data from more traditionally applied biophysical methods, have yielded a remarkable breadth of information about the Fesingle bondS species present, and provided key mechanistic insight not only for Fesingle bondS cluster proteins themselves, but also their assembly.

Item Type: Article
Additional Information: Data Availability Statement: Data will be made available on request. Funding information: The authors acknowledge support from: the UK's Biotechnology and Biological Sciences Research Council (BBSRC) for their work on Fesingle bondS cluster regulators over many years, and UEA for the purchase of an ESI-Q-TOF instrument, and UEA and the British Mass Spectrometry Society for assistance in maintenance of the instrument. This article is based upon work from COST Action FeSImmChemNet, CA21115, supported by COST (European Cooperation in Science and Technology).
Uncontrolled Keywords: dna regulation,iron sensing,mass spectrometry,nitric oxide sensing,o sensing,iron‑sulfur cluster,iron‑sulfur cluster biogenesis,molecular biology,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1312
Faculty \ School: Faculty of Science > School of Chemistry, Pharmacy and Pharmacology
UEA Research Groups: Faculty of Science > Research Groups > Chemistry of Life Processes
Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
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Depositing User: LivePure Connector
Date Deposited: 23 Oct 2024 15:30
Last Modified: 06 Nov 2024 13:30
URI: https://ueaeprints.uea.ac.uk/id/eprint/97162
DOI: 10.1016/j.bbamcr.2024.119865

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