{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,4]],"date-time":"2026-05-04T07:58:31Z","timestamp":1777881511478,"version":"3.51.4"},"publisher-location":"Cham","reference-count":43,"publisher":"Springer Nature Switzerland","isbn-type":[{"value":"9783032231710","type":"print"},{"value":"9783032231727","type":"electronic"}],"license":[{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026]]},"DOI":"10.1007\/978-3-032-23172-7_2","type":"book-chapter","created":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:45:02Z","timestamp":1777596302000},"page":"17-28","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Mechanisms of Carbonic Anhydrase Catalysis and Inhibition"],"prefix":"10.1007","author":[{"given":"Neera","family":"Raghav","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Claudiu T.","family":"Supuran","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alessio","family":"Nocentini","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2026,5,1]]},"reference":[{"key":"2_CR1","doi-asserted-by":"publisher","first-page":"4421","DOI":"10.1021\/cr200176r","volume":"112","author":"V Alterio","year":"2012","unstructured":"Alterio V, Di Fiore A, D\u2019Ambrosio K, Supuran CT, De Simone G (2012) Multiple binding modes of inhibitors to carbonic anhydrases: how to design specific drugs targeting 15 different isoforms? Chem Rev 112:4421\u20134468","journal-title":"Chem Rev"},{"issue":"80","key":"2_CR2","doi-asserted-by":"publisher","first-page":"11983","DOI":"10.1039\/C6CC06399C","volume":"52","author":"V Alterio","year":"2016","unstructured":"Alterio V, Cadoni R, Esposito D, Vullo D, Fiore AD, Monti SM, Caporale A, Ruvo M, Sechi M, Dumy P, Supuran CT, De Simone G, Winum JY (2016) Benzoxaborole as a new chemotype for carbonic anhydrase inhibition. Chem Commun (Camb) 52(80):11983\u201311986","journal-title":"Chem Commun (Camb)"},{"key":"2_CR3","doi-asserted-by":"publisher","first-page":"10384","DOI":"10.1021\/bi970760v","volume":"36","author":"F Briganti","year":"1997","unstructured":"Briganti F, Mangani S, Orioli P, Scozzafava A, Vernaglione G, Supuran CT (1997) Carbonic anhydrase activators: X-ray crystallographic and spectroscopic investigations for the interaction of isozymes I and II with histamine. Biochemistry 36:10384\u201310392","journal-title":"Biochemistry"},{"issue":"4","key":"2_CR4","doi-asserted-by":"publisher","first-page":"1721","DOI":"10.1021\/jm300031j","volume":"55","author":"F Carta","year":"2012","unstructured":"Carta F, Aggarwal M, Maresca A, Scozzafava A, McKenna R, Masini E, Supuran CT (2012) Dithiocarbamates strongly inhibit carbonic anhydrases and show antiglaucoma action in vivo. J Med Chem 55(4):1721\u20131730","journal-title":"J Med Chem"},{"key":"2_CR5","doi-asserted-by":"publisher","first-page":"114","DOI":"10.4155\/fmc.14.68","volume":"6","author":"F Carta","year":"2014","unstructured":"Carta F, Supuran CT, Scozzafava A (2014) Sulfonamides and their isosters as carbonic anhydrase inhibitors. Future Med Chem 6:114\u20131165","journal-title":"Future Med Chem"},{"key":"2_CR6","doi-asserted-by":"publisher","first-page":"5511","DOI":"10.1021\/jm1003667","volume":"53","author":"F Carta","year":"2010","unstructured":"Carta F, Temperini C, Innocenti A, Scozzafava A, Kaila K, Supuran CT (2010) Polyamines inhibit carbonic anhydrases by anchoring to the zinc-coordinated water molecule. J Med Chem 53:5511\u20135522","journal-title":"J Med Chem"},{"key":"2_CR7","doi-asserted-by":"publisher","first-page":"302","DOI":"10.1039\/C4CC07320G","volume":"51","author":"K D\u2019Ambrosio","year":"2015","unstructured":"D\u2019Ambrosio K, Carradori S, Monti SM, Buonanno M, Secci D, Vullo D, Supuran CT, De Simone G (2015) Out of the active site binding pocket for carbonic anhydrase inhibitors. Chem Commun 51:302\u2013305","journal-title":"Chem Commun"},{"key":"2_CR8","doi-asserted-by":"publisher","first-page":"150","DOI":"10.1021\/acs.chemrev.4c00278","volume":"125","author":"K D\u2019Ambrosio","year":"2025","unstructured":"D\u2019Ambrosio K, Di Fiore A, Alterio V, Langella E, Monti SM, Supuran CT, De Simone G (2025) Multiple binding modes of inhibitors to human carbonic anhydrases: an update on the design of isoform-specific modulators of activity. Chem Rev 125:150\u2013222","journal-title":"Chem Rev"},{"key":"2_CR9","doi-asserted-by":"publisher","first-page":"117","DOI":"10.1016\/j.jinorgbio.2011.11.017","volume":"111","author":"G De Simone","year":"2012","unstructured":"De Simone G, Supuran CT (2012) (In)organic anions as carbonic anhydrase inhibitors. J Inorg Biochem 111:117\u2013129","journal-title":"J Inorg Biochem"},{"key":"2_CR10","doi-asserted-by":"publisher","first-page":"30766","DOI":"10.1074\/jbc.M805353200","volume":"283","author":"JF Domsic","year":"2008","unstructured":"Domsic JF, Avvaru BS, Kim CU, Gruner SM, Agbandje-McKenna M, Silverman DN, McKenna R (2008) Entrapment of carbon dioxide in the active site of carbonic anhydrase II. J Biol Chem 283:30766\u201330771","journal-title":"J Biol Chem"},{"issue":"9","key":"2_CR11","doi-asserted-by":"publisher","first-page":"836","DOI":"10.1016\/j.tips.2025.07.002","volume":"46","author":"S Giovannuzzi","year":"2025","unstructured":"Giovannuzzi S, Supuran CT (2025) Human carbonic anhydrase modulators: the past, present, and future. Trends Pharmacol Sci 46(9):836\u2013847","journal-title":"Trends Pharmacol Sci"},{"issue":"1","key":"2_CR12","doi-asserted-by":"publisher","DOI":"10.1002\/ardp.202400705","volume":"358","author":"S Giovannuzzi","year":"2025","unstructured":"Giovannuzzi S, Supuran CT (2025) Lactonase activity of \u03b1-carbonic anhydrases allows identification of novel inhibitors. Arch Pharm (Weinheim). 358(1):e2400705","journal-title":"Arch Pharm (Weinheim)."},{"key":"2_CR13","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/S0163-7258(96)00198-2","volume":"74","author":"S Lindskog","year":"1997","unstructured":"Lindskog S (1997) Structure and mechanism of carbonic anhydrase. Pharmacol Ther 74:1\u201320","journal-title":"Pharmacol Ther"},{"key":"2_CR14","doi-asserted-by":"publisher","first-page":"2505","DOI":"10.1073\/pnas.70.9.2505","volume":"70","author":"S Lindskog","year":"1973","unstructured":"Lindskog S, Coleman JE (1973) The catalytic mechanism of carbonic anhydrase. Proc Natl Acad Sci USA 70:2505\u20132508","journal-title":"Proc Natl Acad Sci USA"},{"key":"2_CR15","doi-asserted-by":"publisher","first-page":"3057","DOI":"10.1021\/ja809683v","volume":"131","author":"A Maresca","year":"2009","unstructured":"Maresca A, Temperini C, Vu H, Pham NB, Poulsen SA, Scozzafava A, Quinn RJ, Supuran CT (2009) Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors. J Am Chem Soc 131:3057\u20133062","journal-title":"J Am Chem Soc"},{"key":"2_CR16","doi-asserted-by":"publisher","first-page":"335","DOI":"10.1021\/jm901287j","volume":"53","author":"A Maresca","year":"2010","unstructured":"Maresca A, Temperini C, Pochet L, Masereel B, Scozzafava A, Supuran CT (2010) Deciphering the mechanism of carbonic anhydrase inhibition with coumarins and thiocoumarins. J Med Chem 53:335\u2013344","journal-title":"J Med Chem"},{"key":"2_CR17","doi-asserted-by":"publisher","first-page":"3659","DOI":"10.1021\/ja00087a086","volume":"116","author":"SK Nair","year":"1994","unstructured":"Nair SK, Ludwig PA, Christianson DW (1994) Two-site binding of phenol in the active site of human carbonic anhydrase II: structural implications for substrate association. J Am Chem Soc 116:3659\u20133660","journal-title":"J Am Chem Soc"},{"issue":"7990","key":"2_CR18","doi-asserted-by":"publisher","first-page":"182","DOI":"10.1038\/s41586-023-06716-y","volume":"624","author":"RS Nett","year":"2023","unstructured":"Nett RS, Dho Y, Tsai C, Passow D, Martinez Grundman J, Low YY, Sattely ES (2023) Plant carbonic anhydrase-like enzymes in neuroactive alkaloid biosynthesis. Nature 624(7990):182\u2013191","journal-title":"Nature"},{"issue":"31","key":"2_CR19","doi-asserted-by":"publisher","first-page":"7840","DOI":"10.1002\/chem.201800941","volume":"24","author":"A Nocentini","year":"2018","unstructured":"Nocentini A, Carta F, Tanc M, Selleri S, Supuran CT, Bazzicalupi C, Gratteri P (2018) Deciphering the mechanism of human carbonic anhydrases inhibition with sulfocoumarins: computational and experimental studies. Chemistry 24(31):7840\u20137844","journal-title":"Chemistry"},{"issue":"5","key":"2_CR20","doi-asserted-by":"publisher","first-page":"1188","DOI":"10.1002\/chem.201805039","volume":"25","author":"A Nocentini","year":"2019","unstructured":"Nocentini A, Gratteri P, Supuran CT (2019) Phosphorus versus sulfur: discovery of benzenephosphonamidates as versatile sulfonamide-mimic chemotypes acting as carbonic anhydrase inhibitors. Chemistry 25(5):1188\u20131192","journal-title":"Chemistry"},{"key":"2_CR21","doi-asserted-by":"publisher","first-page":"8371","DOI":"10.1039\/c0cc02707c","volume":"46","author":"F Pacchiano","year":"2010","unstructured":"Pacchiano F, Aggarwal M, Avvaru BS, Robbins AH, Scozzafava A, McKenna R, Supuran CT (2010) Selective hydrophobic pocket binding observed within the carbonic anhydrase II active site accommodate different 4-substituted-ureido-benzenesulfonamides and correlate to inhibitor potency. Chem Commun (Camb) 46:8371\u20138373","journal-title":"Chem Commun (Camb)"},{"key":"2_CR22","doi-asserted-by":"publisher","first-page":"1896","DOI":"10.1021\/jm101541x","volume":"54","author":"F Pacchiano","year":"2011","unstructured":"Pacchiano F, Carta F, McDonald PC, Lou Y, Vullo D, Scozzafava A, Dedhar S, Supuran CT (2011) Ureido-substituted benzenesulfonamides potently inhibit carbonic anhydrase IX and show antimetastatic activity in a model of breast cancer metastasis. J Med Chem 54:1896\u20131902","journal-title":"J Med Chem"},{"issue":"1","key":"2_CR23","doi-asserted-by":"publisher","DOI":"10.1002\/ardp.202400776","volume":"358","author":"R Paciotti","year":"2025","unstructured":"Paciotti R, Carradori S, Angeli A, D\u2019Agostino I, Ferraroni M, Coletti C, Supuran CT (2025) Unprecedented carbonic anhydrase inhibition mechanism: targeting histidine 64 side chain through a halogen bond. Arch Pharm (Weinheim) 358(1):e2400776","journal-title":"Arch Pharm (Weinheim)"},{"key":"2_CR24","doi-asserted-by":"publisher","DOI":"10.1016\/j.ejmech.2025.118043","volume":"298","author":"N Pala","year":"2025","unstructured":"Pala N, Ladu F, Szlasa W, Cadoni R, Lomelino C, Mahon BP, Gulkis M, McKenna R, Dess\u00ec A, Dallocchio R, Demelas A, Carcelli M, Rogolino D, Crosio C, Iaccarino C, Kulbacka J, Vullo D, Carta F, Supuran CT, Sechi M (2025) Design, anticancer activity, and mechanistic evaluation of a novel class of selective human carbonic anhydrase IX inhibitors featuring a trifluorodihydroxypropanone pharmacophore. Eur J Med Chem 298:118043","journal-title":"Eur J Med Chem"},{"key":"2_CR25","doi-asserted-by":"publisher","first-page":"2641","DOI":"10.1021\/jm9900523","volume":"42","author":"A Scozzafava","year":"1999","unstructured":"Scozzafava A, Menabuoni L, Mincione F, Briganti F, Mincione G, Supuran CT (1999) Carbonic anhydrase inhibitors. Synthesis of water-soluble, topically effective, intraocular pressure-lowering aromatic\/heterocyclic sulfonamides containing cationic or anionic moieties: is the tail more important than the ring? J Med Chem 42:2641\u20132650","journal-title":"J Med Chem"},{"key":"2_CR26","doi-asserted-by":"publisher","first-page":"10609","DOI":"10.1073\/pnas.0904184106","volume":"106","author":"B Sj\u00f6blom","year":"2009","unstructured":"Sj\u00f6blom B, Polentarutti M, Djinovic-Carugo K (2009) Structural study of X-ray induced activation of carbonic anhydrase. Proc Natl Acad Sci USA 106:10609\u201310613","journal-title":"Proc Natl Acad Sci USA"},{"key":"2_CR27","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1111\/j.1432-1033.1975.tb02449.x","volume":"59","author":"H Steiner","year":"1975","unstructured":"Steiner H, Jonsson BH, Lindskog S (1975) The catalytic mechanism of carbonic anhydrase. Eur J Biochem 59:253\u2013259","journal-title":"Eur J Biochem"},{"issue":"2","key":"2_CR28","doi-asserted-by":"publisher","first-page":"168","DOI":"10.1038\/nrd2467","volume":"7","author":"CT Supuran","year":"2008","unstructured":"Supuran CT (2008) Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat Rev Drug Discov 7(2):168\u2013181","journal-title":"Nat Rev Drug Discov"},{"key":"2_CR29","doi-asserted-by":"publisher","first-page":"2023","DOI":"10.1042\/BCJ20160115","volume":"473","author":"CT Supuran","year":"2016","unstructured":"Supuran CT (2016) Structure and function of carbonic anhydrases. Biochem J 473:2023\u20132032","journal-title":"Biochem J"},{"key":"2_CR30","doi-asserted-by":"publisher","first-page":"345","DOI":"10.3109\/14756366.2015.1122001","volume":"31","author":"CT Supuran","year":"2016","unstructured":"Supuran CT (2016) How many carbonic anhydrase inhibition mechanisms exist? J Enzyme Inhib Med Chem 31:345\u2013360","journal-title":"J Enzyme Inhib Med Chem"},{"key":"2_CR31","doi-asserted-by":"publisher","DOI":"10.1016\/j.bmcl.2023.129411","volume":"93","author":"CT Supuran","year":"2023","unstructured":"Supuran CT (2023) A simple yet multifaceted 90 years old, evergreen enzyme: carbonic anhydrase, its inhibition and activation. Bioorg Med Chem Lett 93:129411","journal-title":"Bioorg Med Chem Lett"},{"key":"2_CR32","doi-asserted-by":"publisher","first-page":"1326633","DOI":"10.3389\/fmolb.2023.1326633","volume":"10","author":"CT Supuran","year":"2023","unstructured":"Supuran CT (2023) Carbonic anhydrase versatility: from pH regulation to CO2 sensing and metabolism. Front Mol Biosci 10:1326633","journal-title":"Front Mol Biosci"},{"key":"2_CR33","doi-asserted-by":"publisher","first-page":"897","DOI":"10.1080\/14728222.2023.2263914","volume":"27","author":"CT Supuran","year":"2023","unstructured":"Supuran CT (2023) An overview of novel antimicrobial carbonic anhydrase inhibitors. Expert Opin Ther Targets 27:897\u2013910","journal-title":"Expert Opin Ther Targets"},{"key":"2_CR34","doi-asserted-by":"publisher","first-page":"701","DOI":"10.1080\/13543776.2023.2245971","volume":"33","author":"CT Supuran","year":"2023","unstructured":"Supuran CT (2023) Targeting carbonic anhydrases for the management of hypoxic metastatic tumors. Expert Opin Ther Pat 33:701\u2013720","journal-title":"Expert Opin Ther Pat"},{"key":"2_CR35","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1080\/13543776.2023.2201432","volume":"33","author":"CT Supuran","year":"2023","unstructured":"Supuran CT (2023) Antiprotozoal drugs: challenges and opportunities. Expert Opin Ther Pat 33:133\u2013136","journal-title":"Expert Opin Ther Pat"},{"key":"2_CR36","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1080\/17425255.2024.2328152","volume":"20","author":"CT Supuran","year":"2024","unstructured":"Supuran CT (2024) Drug interactions of carbonic anhydrase inhibitors and activators. Expert Opin Drug Metab Toxicol 20:143\u2013155","journal-title":"Expert Opin Drug Metab Toxicol"},{"key":"2_CR37","doi-asserted-by":"publisher","unstructured":"Supuran CT (2024) Novel carbonic anhydrase inhibitors for the treatment of Helicobacter pylori infection. Expert Opin Investig Drugs (in press):1\u201310. https:\/\/doi.org\/10.1080\/13543784.2024.2334714","DOI":"10.1080\/13543784.2024.2334714"},{"key":"2_CR38","first-page":"383","volume":"55","author":"CT Supuran","year":"2024","unstructured":"Supuran CT (2024) Challenges for developing bacterial CA inhibitors as novel antibiotics. Enzyme 55:383\u2013411","journal-title":"Enzyme"},{"key":"2_CR39","doi-asserted-by":"publisher","DOI":"10.1124\/pharmrev.124.001125","volume":"77","author":"CT Supuran","year":"2025","unstructured":"Supuran CT (2025) Multi- and polypharmacology of carbonic anhydrase inhibitors. Pharmacol Rev 77:100004","journal-title":"Pharmacol Rev"},{"key":"2_CR40","doi-asserted-by":"publisher","first-page":"1889","DOI":"10.1021\/acsmedchemlett.5c00443","volume":"16","author":"CT Supuran","year":"2025","unstructured":"Supuran CT (2025) Human carbonic anhydrase inhibitors. ACS Med Chem Lett 16:1889\u20131895","journal-title":"ACS Med Chem Lett"},{"key":"2_CR41","doi-asserted-by":"publisher","first-page":"293","DOI":"10.1021\/jm301625s","volume":"56","author":"K Tars","year":"2013","unstructured":"Tars K, Vullo D, Kazaks A, Leitans J, Lends A, Grandane A, Zalubovskis R, Scozzafava A, Supuran CT (2013) Sulfocoumarins (1,2-benzoxathiine-2,2-dioxides): a class of potent and isoform-selective inhibitors of tumor-associated carbonic anhydrases. J Med Chem 56:293\u2013300","journal-title":"J Med Chem"},{"key":"2_CR42","doi-asserted-by":"publisher","first-page":"7913","DOI":"10.1021\/bi00445a054","volume":"28","author":"C Tu","year":"1989","unstructured":"Tu C, Silverman DN, Forsman C, Jonsson BH, Lindskog S (1989) Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant. Biochemistry 28:7913\u20137918","journal-title":"Biochemistry"},{"key":"2_CR43","doi-asserted-by":"publisher","first-page":"321","DOI":"10.3109\/14756366.2014.913587","volume":"30","author":"JY Winum","year":"2015","unstructured":"Winum JY, Supuran CT (2015) Recent advances in the discovery of zinc-binding motifs for the development of carbonic anhydrase inhibitors. J Enzyme Inhib Med Chem 30:321\u2013324","journal-title":"J Enzyme Inhib Med Chem"}],"container-title":["Subcellular Biochemistry","Carbonic Anhydrase Inhibitors"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/978-3-032-23172-7_2","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:45:02Z","timestamp":1777596302000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/978-3-032-23172-7_2"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026]]},"ISBN":["9783032231710","9783032231727"],"references-count":43,"URL":"https:\/\/doi.org\/10.1007\/978-3-032-23172-7_2","relation":{},"ISSN":["0306-0225","2542-8810"],"issn-type":[{"value":"0306-0225","type":"print"},{"value":"2542-8810","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026]]},"assertion":[{"value":"1 May 2026","order":1,"name":"first_online","label":"First Online","group":{"name":"ChapterHistory","label":"Chapter History"}}]}}