PXD043873 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | A General Approach for Activity-based Protein Profiling of Oxidoreductases with Redox-differentiated Diarylhalonium Warheads |
Description | Activity-based protein profiling (ABPP) is a unique proteomic tool for measuring the activity of enzymes in their cellular context, which has been well established for enzyme classes exhibiting a characteristic nucleophilic residue (e.g. hydrolases). In contrast, the enzyme class of oxidoreductases has received less attention, as its members rely mainly on cofactors instead of nucleophilic amino acid residues for catalysis. ABPP probes have been designed for specific oxidoreductase subclasses, which rely on the oxidative conversion of the probes into strong electrophiles. Here we describe the development of ABPP probes for the simultaneous labeling of various subclasses of oxidoreductases. The probe warheads are based on hypervalent diarylhalonium salts, which show unique reactivity as their activation proceeds via a reductive mechanism resulting in aryl radicals leading to covalent labeling of liver proteins at several different amino acids in close proximity to the active sites. The redox potential of the probes can be tuned by isosteric replacement varyring the halonium central atom. ABPP experiments with liver using 16 probes differing in warhead, linker, and structure revealed distinct overlapping profiles and broad substrate specificities of several probes. With their capability of multi oxidoreductase subclass labeling – including rare examples for the class of reductases – and their unique design, the herein reported probes offer new opportunities for the investigation of the “oxidoreductome” of microorganisms, plants, animal and human tissues. |
HostingRepository | PRIDE |
AnnounceDate | 2025-05-06 |
AnnouncementXML | Submission_2025-05-06_12:54:37.225.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Laura Liesinger |
SpeciesList | scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; |
ModificationList | monohydroxylated residue |
Instrument | timsTOF Pro |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2023-07-18 12:56:23 | ID requested | |
⏵ 1 | 2025-05-06 12:54:39 | announced | |
Publication List
Krammer L, Darnhofer B, Kljajic M, Liesinger L, Schittmayer M, Neshchadin D, Gescheidt G, Kollau A, Mayer B, Fischer RC, Wallner S, Macheroux P, Birner-Gruenberger R, Breinbauer R, A general approach for activity-based protein profiling of oxidoreductases with redox-differentiated diarylhalonium warheads. Chem Sci, 16(15):6240-6256(2025) [pubmed] |
10.1039/d4sc08454c; |
Keyword List
submitter keyword: Oxidoreductase probe, mouse liver;,Activity-based Protein Profiling |
Contact List
Ruth Birner-Gruenberger |
contact affiliation | Institute of Chemical Technologies and Analytics, Technische Universität Wien, Getreidemarkt 9, 1060 Vienna, Austria; Research and Diagnostic Institute of Pathology, Medical University of Graz, Stiftingtalstraße 6, 8036, Graz, Austria |
contact email | ruth.birner-gruenberger@tuwien.ac.at |
lab head | |
Laura Liesinger |
contact affiliation | Faculty of Technical Chemistry, Institute of Chemical Technologies and Analytics, Technische Universität Wien (TU Wien), 1060 Vienna, Austria; |
contact email | laura.liesinger@tuwien.ac.at |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/05/PXD043873 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD043873
- Label: PRIDE project
- Name: A General Approach for Activity-based Protein Profiling of Oxidoreductases with Redox-differentiated Diarylhalonium Warheads