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The following steps are for SP2E (enrichment) and SP3 (full proteome). 1). SP2E: The samples were clicked to biotin azide using click master mix, cleaned up by using TCEP for reduction and IAA for alkylation, followed by DTT for quench of excessive IAA. All the samples were treated with carboxylate beads, and proteome were precipitated with EtOH, eluted with SDS. The clicked proteome was enriched with streptavidin beads, washed with NP-40, urea and water. 2). SP3: The samples were cleaned up by using TCEP, IAA for and DTT. all the samples were treated with carboxylate beads, washed with EtOH and acetonitrile. All the enriched or cleaned up proteome was digested with trypsin. The digested peptides were desalted with handmade STAGE tips using wash buffer (TFA in isopropanol, TFA in water) and elution buffer (ammonia in acetonitrile). The eluted peptides were dried using a concentrator and reconstituted in formic acid for MS/MS measurements"],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["1. Preparative Labeling and Full Proteome LC-MS/MS Data Analysis MS data was analyzed using DIA-NN (version 1.8.1) in library-free mode.  The DIA-NN was operated with the default settings. The following procedures were used to proceed with data: 1). Rename columns, 2). Add annotations, 3). Log2 Transform of LFQ intensities, 4). Categorical annotations of rows, 5). Remove contaminants, 6). Remove reverse, 7). Filter rows based on valid values (2 for three replicates, 3 for four replicates) with at least in one group, 8). Impute the missing values from normal distribution over the total matrix, 9). Two-sample Student's t-test with 5% FDR.  2. MS/MS Data Analysis The MS/MS data was analyzed with Fragpipe (version 20.0, for E. coli K-12 data analysis) and Maxquant (version 2.6.4, for RuvB binding site identification). Open search analysis with FragPipe The negative controls were set as \"Control\" and the PQQ-treated experiments were set \"Experiment.\" The \"MS/MS type\" was selected IM-MS. The \"Run MS Fragger\" was enabled with the default settings except that a custom reduced mass-list file was used as the \"Custom annotation file\" under \"Annotation\" of \"PTM-Shepherd.\" For downstream data analysis, the unannotated mass shift of 309.9860 was retrieved from 'global.modsummary.tsv' file.  Offset search with Fragpipe The \"MS/MS type\" was selected IM-MS. Here, PQQ-treated experiments only were uploaded for data analysis. The default settings were used for this search except that under \"Advanced Options,\" the \"Mass offsets\" was set to 0/309.9860 and the \"Restrict delta mass\" was set to all under \"Run MS Fragger\"; the \"Run PTM-Shepherd\" option was enabled with the following parameters: under \"Annotation,\" the \"Annotation tolerance\" was set to 0.01 Da; a custom reduced mass-list file was used as the \"Custom annotation file.\" For downstream analysis, the \"tsv\" files were individually processed. Only entries were retained that contains one lower-case letter. Next, the entries were filtered for a delta score > 1. All peptide sequences that did not occur exactly once in the identified protein were excluded and the residue number of the modified residue was determined based on the UniProt Code. For each entry, an identifier was generated in the format \"UniProtCode\"_X_\"residue number,\" where X is the one letter code of the modified amino acid. Duplicates of entries with the same identifier were retained only once. The fraction of all sites that were modified at each amino acid and the terminal was reported.  Closed Search Analysis with Fragpipe To identify the binding proteins of PQQ against E. coli K-12 proteome, a closed search was performed. The \"MS/MS type\" was selected IM-MS. Here, the PQQ-treated experiments only were uploaded for data analysis. The defaulting setting were used for this search except that the \"Variable modifications\" was set to 309.9860 from Open Search, the \"Site\" was set to K with \"Max occurrences\" of 2, no \"fixed modifications\" under \"Modification\" was enabled under \"Run MS Fragge.\"  For downstream data analysis, the \"ion.tsv\" files and the ''combined modified peptides'' file were analyzed. Merge the ''ion.tsv'' files and ''combined modified peptides'' into one file based on the PQQ modified peptides, charges and spectral count. First, the \"Modified Peptide\" and \"Peptide Sequence\" with the shortest sequence were kept. Then this \"identifier\" was deleted if the total number of MS/MS and MBR as the match type from all replicates were less than 2, and the total PSMs was less than 2. In addition, the \"identifier\" was kept and considered to be as true positive only if the Peptideprophet Probability > 0.75. Last, the \"identifier\" was kept if the standard deviation of Log10 Intensity of all replicates was less than 0.5 for all ions of the same \"Identifier.\" Finally, the filtered modified peptides were linked to the related proteins.   Closed search with Maxquant MaxQuant search was performed against the Uniprot reference proteome: E. coli K-12. \"PQQ Modification\" of C14H4N2O7 (309.9862) was added to the configuration table. Under \"Raw data,\" the \"PTM\" of negative controls were set false and experiments set as true, the \"Fraction\" was set empty. The default settings were used except that the \"fixed modifications\" was set to carbamidomethylation (cysteine) and PQQ modification of 309.9860; under \"protein quantification,\" oxidation (methionine), acetylation (N-terminus) and PQQ modification were set for \"Modifications used in protein quantification\". For the downstream analysis, the \"PQQ Modification Sites\" text file was analyzed."],"omics_type":["Proteomics"],"labhead":["Stephan A Siber"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Center for Functional Protein Assemblies (CPA), Department of Bioscience, TUM School of Natural Sciences, Technical University of Munich (TUM), Ernst-Otto-Fischer-Stra?e 8, 85748 Garching, Germany"],"species":["Homo Sapiens (human)","Escherichia Coli","Pseudomonas Putida Kt2440"],"publication":["41925033 Wang T, Mühlhofer R, Lei E, Ding W, Klein AS, Zeymer C, Sieber SA. Chemical Proteomics Reveal the Inventory of Pyrroloquinoline Quinone Binding Proteins in Bacteria. J Am Chem Soc. 2026 148(14):15306-15319 10.1021/jacs.6c03427"],"submitter_mail":["tao.wang@tum.de"],"submitter_affiliation":["Technical University of Munich"],"submitter_country":["Germany"],"pubmed_abstract":["Pyrroloquinoline quinone (<b>PQQ</b>) is a bacterial redox cofactor enabling enzyme catalysis in various sugar and alcohol dehydrogenases. However, its proposed additional role as a \"longevity vitamin\" lacks a clear molecular basis and is thus highly debated. Here, we applied chemical proteomics to identify previously unknown classes of <b>PQQ</b>-binding proteins. We designed and synthesized a structurally diverse suite of five <b>PQQ</b> probes equipped with a diazirine photo-cross-linker and an alkyne handle for target identification. The fidelity of the probes was first evaluated for two well-characterized bacterial <b>PQQ</b>-dependent enzymes, demonstrating not only probe binding but also the reconstitution of catalytic activity. We then commenced with proteome profiling of <i>Escherichia coli</i> and <i>Pseudomonas putida</i> cells and unraveled a distinct set of putative <b>PQQ</b>-binding proteins. Recombinant expression of selected hits, including several chaperones, validated <b>PQQ</b> binding. Notably, in some cases, <b>PQQ</b> even formed covalent adducts with selected lysine residues, for instance, in the AAA+ ATPase RuvB involved in DNA remodeling. Overall, our work highlights the utility of <b>PQQ</b> probes to further unravel the complement of cofactor-binding proteins in whole cells. It also provides a basis for future mechanistic studies of <b>PQQ</b> functions beyond redox catalysis."],"pubmed_title":["Chemical Proteomics Reveal the Inventory of Pyrroloquinoline Quinone Binding Proteins in Bacteria."],"pubmed_authors":["Wang Tao T, Mühlhofer Rahel R, Lei E E, Ding Wei W, Klein Andreas S AS, Zeymer Cathleen C, Sieber Stephan A SA"],"additional_accession":[]},"is_claimable":false,"name":"Chemical proteomics reveal the inventory of pyrroloquinoline quinone binding proteins in bacteria","description":"Pyrroloquinoline quinone (PQQ) is a bacterial redox cofactor enabling enzyme catalysis in various sugar and alcohol dehydrogenases. However, its proposed additional role as a \"longevity vitamin\" lacks a clear molecular basis and is thus highly debated. Here, we applied chemical proteomics to identify so far unknown classes of PQQ-binding proteins. We designed and synthesized a structurally diverse suite of five PQQ probes equipped with a diazirine photocrosslinker and an alkyne handle for target identification. The fidelity of the probes was first evaluated for two well-characterized bacterial PQQ-dependent enzymes, demonstrating not only probe binding but also reconstitution of catalytic activity. We then commenced with proteome profiling of Escherichia coli and Pseudomonas putida cells and unraveled a distinct set of putative PQQ-binding proteins. Recombinant expression of selected hits including several chaperones validated PQQ binding. Notably, in some cases, PQQ even formed covalent adducts with selected lysine residues, for instance in the AAA+ ATPase RuvB involved in DNA remodeling. Overall, our work highlights the utility of PQQ probes to further unravel the complement of cofactor-binding proteins in whole cells. It also provides a basis for future mechanistic studies on PQQ functions beyond redox catalysis.","dates":{"publication":"2026-04-27","submission":"2025-10-10"},"accession":"PXD069310","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:7719","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:3715","NEWT:2065263","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:299467","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:10804","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601",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