{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T16:22:44Z","timestamp":1778689364517,"version":"3.51.4"},"reference-count":50,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100012310","name":"Alzahra University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100012310","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic &amp; Medicinal Chemistry"],"published-print":{"date-parts":[[2021,8]]},"DOI":"10.1016\/j.bmc.2021.116276","type":"journal-article","created":{"date-parts":[[2021,6,27]],"date-time":"2021-06-27T05:01:54Z","timestamp":1624770114000},"page":"116276","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":10,"special_numbering":"C","title":["Quantum mechanical study on the activation mechanism of human carbonic anhydrase VII cluster model with bis-histamine schiff bases and bis-spinaceamine derivatives"],"prefix":"10.1016","volume":"44","author":[{"given":"Mina","family":"Ghiasi","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Parisa","family":"Shahabi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4262-0323","authenticated-orcid":false,"given":"Claudiu T.","family":"Supuran","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"2","key":"10.1016\/j.bmc.2021.116276_b0005","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1038\/nrd2467","article-title":"Carbonic anhydrases: novel therapeutic applications for inhibitors and activators","volume":"7","author":"Supuran","year":"2008","journal-title":"Nat Rev Drug Discov"},{"issue":"10","key":"10.1016\/j.bmc.2021.116276_b0010","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1042\/CS20210040","article-title":"Emerging role of carbonic anhydrase inhibitors","volume":"135","author":"Supuran","year":"2021","journal-title":"Clin Sci (Lond)"},{"key":"10.1016\/j.bmc.2021.116276_b0015","doi-asserted-by":"crossref","first-page":"1305","DOI":"10.1080\/14756366.2017.1386660","article-title":"Synthesis and biological evaluation of histamine Schiff bases as carbonic anhydrase I, II, IV, VII, and IX activators","volume":"32","author":"Akocak","year":"2017","journal-title":"J Enzyme Inhib Med Chem"},{"key":"10.1016\/j.bmc.2021.116276_b0020","doi-asserted-by":"crossref","first-page":"4389","DOI":"10.1016\/j.bmcl.2014.08.015","article-title":"Discovery of a new family of carbonic anhydrases in the malaria pathogen Plasmodium falciparum\u2014The \u03b7-carbonic anhydrases","volume":"24","author":"Del Prete","year":"2014","journal-title":"Bioorg Med Chem Lett"},{"key":"10.1016\/j.bmc.2021.116276_b0025","doi-asserted-by":"crossref","first-page":"2094","DOI":"10.1038\/s41396-019-0426-8","article-title":"A new widespread subclass of carbonic anhydrase in marine phytoplankton","volume":"13","author":"Jensen","year":"2019","journal-title":"ISME J"},{"key":"10.1016\/j.bmc.2021.116276_b0030","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1038\/144442b0","article-title":"Carbonic anhydrase","volume":"144","author":"Keilin","year":"1939","journal-title":"Nature"},{"key":"10.1016\/j.bmc.2021.116276_b0035","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1038\/nature06636","article-title":"Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms","volume":"452","author":"Xu","year":"2008","journal-title":"Nature"},{"issue":"225","key":"10.1016\/j.bmc.2021.116276_b0040","article-title":"Deciphering the key heterocyclic scaffolds in targeting microtubules, kinases and carbonic anhydrases for cancer drug development","volume":"22","author":"Peerzada","year":"2021","journal-title":"Pharmacol Ther"},{"issue":"5","key":"10.1016\/j.bmc.2021.116276_b0045","doi-asserted-by":"crossref","first-page":"561","DOI":"10.4155\/fmc-2017-0223","article-title":"Carbonic anhydrase activators","volume":"10","author":"Supuran","year":"2018","journal-title":"Future Med Chem"},{"key":"10.1016\/j.bmc.2021.116276_b0050","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1002\/jps.2600830603","article-title":"Carbonic anhydrase activators. 3: Structure-activity correlations for a series of isozyme II activators","volume":"83","author":"Clare","year":"1994","journal-title":"J Pharm Sci"},{"key":"10.1016\/j.bmc.2021.116276_b0055","doi-asserted-by":"crossref","unstructured":"Temperini C, Scozzafava A, Vullo D, Supuran CT. Carbonic Anhydrase Activators. Activation of Isozymes I, II, IV, VA, VII, and XIV with L\u2010and D\u2010Histidine and Crystallographic Analysis of Their Adducts with Isoform II: Engineering Proton\u2010Transfer Processes within the Active Site of an Enzyme. Chem Eur J. 2006; 12: 7057-7066. https:\/\/doi: 10.1002\/chem.200600159.","DOI":"10.1002\/chem.200600159"},{"issue":"4","key":"10.1016\/j.bmc.2021.116276_b0060","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1016\/j.bmcl.2004.12.052","article-title":"Carbonic anhydrase inhibitors. Inhibition of the human cytosolic isozyme VII with aromatic and heterocyclic sulfonamides","volume":"15","author":"Vullo","year":"2005","journal-title":"Bioorg Med Chem Lett"},{"key":"10.1016\/j.bmc.2021.116276_b0065","doi-asserted-by":"crossref","first-page":"4187","DOI":"10.1016\/j.bmc.2018.07.011","article-title":"Activation studies with amines and amino acids of the \u03b1-carbonic anhydrase from the pathogenic protozoan Trypanosoma cruzi","volume":"26","author":"Angeli","year":"2018","journal-title":"Bioorganic Med Chem"},{"key":"10.1016\/j.bmc.2021.116276_b0070","first-page":"26","article-title":"X-Ray Charge Densities and Chemical Bonding","volume":"120","author":"Coppens","year":"1997","journal-title":"Int Union Crystallography"},{"key":"10.1016\/j.bmc.2021.116276_b0075","doi-asserted-by":"crossref","first-page":"28460","DOI":"10.1039\/C9RA04603H","article-title":"Novel bovine carbonic anhydrase encapsulated in a metal\u2013organic framework: a new platform for biomimetic sequestration of CO2","volume":"9","author":"Asadi","year":"2019","journal-title":"RSC Adv"},{"key":"10.1016\/j.bmc.2021.116276_b0080","doi-asserted-by":"crossref","unstructured":"Abdo, M. R. et al. Carbonic anhydrase activators: Activation of human isozymes I, II and IX with phenylsulfonylhydrazido l-histidine derivatives. Bioorganic Med. Chem. Lett. 2009; 19: 2440\u20132443. (https:\/\/doi.org\/10.1016\/j.bmcl.2009.03.050.","DOI":"10.1016\/j.bmcl.2009.03.050"},{"issue":"1","key":"10.1016\/j.bmc.2021.116276_b0085","doi-asserted-by":"crossref","first-page":"1206","DOI":"10.1080\/14756366.2020.1766455","article-title":"Carbonic anhydrase modulation of emotional memory. Implications for the treatment of cognitive disorders","volume":"35","author":"Blandina","year":"2020","journal-title":"J Enzyme Inhib Med Chem"},{"key":"10.1016\/j.bmc.2021.116276_b0090","doi-asserted-by":"crossref","first-page":"800","DOI":"10.1016\/j.bmc.2019.01.017","article-title":"\u03b1-Carbonic anhydrases are strongly activated by spinaceamine derivatives","volume":"27","author":"Akocak","year":"2019","journal-title":"Bioorganic Med Chem"},{"key":"10.1016\/j.bmc.2021.116276_b0095","doi-asserted-by":"crossref","first-page":"2561","DOI":"10.1016\/S0021-9258(18)62326-9","article-title":"The carbon dioxide hydration activity of carbonic anhydrase I. Stop-flow kinetic studies on the native human isoenzymes B and C","volume":"246","author":"Khalifah","year":"1971","journal-title":"J Biol Chem"},{"key":"10.1016\/j.bmc.2021.116276_b0100","doi-asserted-by":"crossref","first-page":"1379","DOI":"10.1080\/14756366.2020.1781845","article-title":"Activation studies of the \u03b2-carbonic anhydrases from Escherichia coli with amino acids and amines","volume":"35","author":"Nocentini","year":"2020","journal-title":"J Enzyme Inhib Med Chem"},{"key":"10.1016\/j.bmc.2021.116276_b0105","doi-asserted-by":"crossref","first-page":"3601","DOI":"10.1021\/cr400388t","article-title":"Quantum chemical studies of mechanisms for metalloenzymes","volume":"114","author":"Blomberg","year":"2014","journal-title":"Chem Rev"},{"key":"10.1016\/j.bmc.2021.116276_b0110","doi-asserted-by":"crossref","unstructured":"Lonsdale, R. & J Mulholland, A. QM\/MM modelling of drug-metabolizing enzymes. Curr. Top. Med. Chem. 2014; 14: 1339\u20131347. https:\/\/doi.org\/ 10.2174\/1568026614666140506114859.","DOI":"10.2174\/1568026614666140506114859"},{"key":"10.1016\/j.bmc.2021.116276_b0115","doi-asserted-by":"crossref","DOI":"10.1002\/wcms.1281","article-title":"Application of quantum mechanics\/molecular mechanics methods in the study of enzymatic reaction mechanisms","volume":"7","author":"Sousa","year":"2017","journal-title":"Wiley Interdiscip Rev Comput Mol Sci"},{"key":"10.1016\/j.bmc.2021.116276_b0120","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.abb.2015.03.013","article-title":"Computational strategies for the design of new enzymatic functions","volume":"582","author":"\u015awiderek","year":"2015","journal-title":"Arch Biochem Biophys"},{"key":"10.1016\/j.bmc.2021.116276_b0125","doi-asserted-by":"crossref","first-page":"10020","DOI":"10.1002\/anie.201403689","article-title":"Multiscale modeling of biological functions: from enzymes to molecular machines (Nobel Lecture)","volume":"53","author":"Warshel","year":"2014","journal-title":"Angew Chemie Int Ed"},{"key":"10.1016\/j.bmc.2021.116276_b0130","doi-asserted-by":"crossref","first-page":"14804","DOI":"10.1021\/ja9037142","article-title":"Human insulin-degrading enzyme working mechanism","volume":"131","author":"Amata","year":"2009","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.bmc.2021.116276_b0135","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1021\/cr050262p","article-title":"Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein\u2212 ligand binding","volume":"108","author":"Krishnamurthy","year":"2008","journal-title":"Chem Rev"},{"key":"10.1016\/j.bmc.2021.116276_b0140","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1021\/acscatal.5b01928","article-title":"Unveiling the catalytic mechanism of NADP+-dependent isocitrate dehydrogenase with QM\/MM calculations","volume":"6","author":"Neves","year":"2016","journal-title":"ACS Catal"},{"key":"10.1016\/j.bmc.2021.116276_b0145","doi-asserted-by":"crossref","unstructured":"Alterio, V., Di Fiore, A., D\u2019Ambrosio, K., Supuran, C. T. & De Simone, G. Multiple binding modes of inhibitors to carbonic anhydrases: how to design specific drugs targeting 15 different isoforms? Chem. Rev. 2012; 112: 4421\u20134468. https:\/\/doi.org\/ 10.1021\/cr200176r.","DOI":"10.1021\/cr200176r"},{"key":"10.1016\/j.bmc.2021.116276_b0150","doi-asserted-by":"crossref","first-page":"17824","DOI":"10.1021\/ja207065v","article-title":"A proposal for mitochondrial processing peptidase catalytic mechanism","volume":"133","author":"Amata","year":"2011","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.bmc.2021.116276_b0155","doi-asserted-by":"crossref","first-page":"22523","DOI":"10.1073\/pnas.1014060108","article-title":"Mechanism of tungsten-dependent acetylene hydratase from quantum chemical calculations","volume":"107","author":"Liao","year":"2010","journal-title":"Proc Natl Acad Sci"},{"key":"10.1016\/j.bmc.2021.116276_b0160","doi-asserted-by":"crossref","first-page":"2185","DOI":"10.1002\/chem.201201943","article-title":"Catalytic mechanism of the arylsulfatase promiscuous enzyme from Pseudomonas aeruginosa","volume":"19","author":"Marino","year":"2013","journal-title":"Chem Eur J"},{"key":"10.1016\/j.bmc.2021.116276_b0165","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1021\/ar7001045","article-title":"Computational enzymatic catalysis","volume":"41","author":"Ramos","year":"2008","journal-title":"Acc Chem Res"},{"key":"10.1016\/j.bmc.2021.116276_b0170","doi-asserted-by":"crossref","DOI":"10.1063\/1.3382344","article-title":"A consistent and accurate ab initio parametrization of density functional dispersion correction (DFT-D) for the 94 elements H-Pu","volume":"132","author":"Grimme","year":"2010","journal-title":"J Chem Phys"},{"key":"10.1016\/j.bmc.2021.116276_b0175","doi-asserted-by":"crossref","first-page":"1456","DOI":"10.1002\/jcc.21759","article-title":"Effect of the damping function in dispersion corrected density functional theory","volume":"32","author":"Grimme","year":"2011","journal-title":"J Comput Chem"},{"key":"10.1016\/j.bmc.2021.116276_b0180","doi-asserted-by":"crossref","unstructured":"Kumar, P. S. V., Raghavendra, V. & Subramanian, V. Bader\u2019s Theory of Atoms in Molecules (AIM) and its Applications to Chemical Bonding. J. Chem. Sci. 2016; 128: 1527\u20131536 .https:\/\/doi.org\/10.1007\/s12039-016-1172-3.","DOI":"10.1007\/s12039-016-1172-3"},{"key":"10.1016\/j.bmc.2021.116276_b0185","doi-asserted-by":"crossref","unstructured":"Foresman, J. B., Keith, T. A., Wiberg, K. B., Snoonian, J. & Frisch, M. J. Solvent effects. 5. Influence of cavity shape, truncation of electrostatics, and electron correlation on ab initio reaction field calculations. J. Phys. Chem. 1996; 100: 16098\u201316104. https:\/\/doi.org\/10.1021\/jp960488j.","DOI":"10.1021\/jp960488j"},{"key":"10.1016\/j.bmc.2021.116276_b0190","doi-asserted-by":"crossref","first-page":"2999","DOI":"10.1021\/cr9904009","article-title":"Quantum mechanical continuum solvation models","volume":"105","author":"Tomasi","year":"2005","journal-title":"Chem Rev"},{"key":"10.1016\/j.bmc.2021.116276_b0195","doi-asserted-by":"crossref","first-page":"2027","DOI":"10.1021\/cr00031a013","article-title":"Molecular interactions in solution: an overview of methods based on continuous distributions of the solvent","volume":"94","author":"Tomasi","year":"1994","journal-title":"Chem Rev"},{"key":"10.1016\/j.bmc.2021.116276_b0200","doi-asserted-by":"crossref","first-page":"9072","DOI":"10.1021\/j100022a019","article-title":"Solvent effects on 1, 2-dihaloethane gauche\/trans ratios","volume":"99","author":"Wiberg","year":"1995","journal-title":"J Phys Chem"},{"key":"10.1016\/j.bmc.2021.116276_b0205","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1007\/s13404-021-00292-7","article-title":"QM study of interaction between arginine amino acid and Au clusters and the effects on arginine acidity","volume":"54","author":"Ghiasi","year":"2021","journal-title":"Gold Bull"},{"key":"10.1016\/j.bmc.2021.116276_b0210","doi-asserted-by":"crossref","unstructured":"Malmberg, C. G. & Maryott, A. A. with a maximum deviation of 0.01 unit in dielectric constant. The experimental method and sources of error are considered in some detail. J. Res. Natl. Bur. Stand. 1956; 56: 1. https:\/\/ doi.org\/10.6028\/jres.056.001.","DOI":"10.6028\/jres.056.001"},{"key":"10.1016\/j.bmc.2021.116276_b0215","doi-asserted-by":"crossref","unstructured":"Reed, A. E., Carpenter, J. E., Weinhold, F. & Glendening, E. D. NBO, version 3.1. Univ. Wisconsin. 1992; https:\/\/doi.org\/10.1080\/0144235X.2016.1192262.","DOI":"10.1080\/0144235X.2016.1192262"},{"key":"10.1016\/j.bmc.2021.116276_b0220","doi-asserted-by":"crossref","unstructured":"Frisch, M. J. et al. Gaussian 09; Gaussian, Inc. Wallingford, CT .2009; 32: 5648\u20135652. https:\/\/doi.org\/10.1016\/j.comptc.2020.112911.","DOI":"10.1016\/j.comptc.2020.112911"},{"key":"10.1016\/j.bmc.2021.116276_b0225","doi-asserted-by":"crossref","first-page":"4777","DOI":"10.1021\/jp050717e","article-title":"Trapping of the OH radical by \u03b1-tocopherol: a theoretical study","volume":"109","author":"Navarrete","year":"2005","journal-title":"J Phys Chem A"},{"key":"10.1016\/j.bmc.2021.116276_b0230","doi-asserted-by":"crossref","DOI":"10.1016\/j.comptc.2020.112911","article-title":"Quantum mechanical study of human carbonic anhydrase II in complex with polyamines as novel inhibitors: Kinetic and thermodynamic investigation","volume":"1186","author":"Ghiasi","year":"2020","journal-title":"Comput Theor Chem"},{"key":"10.1016\/j.bmc.2021.116276_b0235","doi-asserted-by":"crossref","first-page":"1697","DOI":"10.1021\/jp4115699","article-title":"A Molecular Electrostatic Potential Analysis of Hydrogen, Halogen, and Dihydrogen Bonds","volume":"118","author":"Mohan","year":"2014","journal-title":"J Phys Chem A"},{"key":"10.1016\/j.bmc.2021.116276_b0240","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/ijms19061571","article-title":"The crystal structure of a hCA VII variant provides insights into the molecular determinants responsible for its catalytic behavior","volume":"19","author":"Buonanno","year":"2018","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.bmc.2021.116276_b0245","doi-asserted-by":"crossref","unstructured":"Akocak S, Lolak N, Bua S, Nocentini A, Supuran CT. Activation of human \u03b1-carbonic anhydrase isoforms I, II, IV and VII with bis-histamine schiff bases and bis-spinaceamine substituted derivatives. J Enzyme Inhib Med Chem. 2019; 34: 1193-1198.https:\/\/doi.org\/10.1080\/14756366.2019.1630616.","DOI":"10.1080\/14756366.2019.1630616"},{"key":"10.1016\/j.bmc.2021.116276_b0250","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1080\/07391102.2019.1585951","article-title":"Carbon and boron nanotubes as a template material for adsorption of 6-Thioguanine chemotherapeutic: a molecular dynamics and density functional approach","volume":"38","author":"Hasanzade","year":"2019","journal-title":"J Biomol Struct Dyn"}],"container-title":["Bioorganic &amp; Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968089621002844?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968089621002844?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,19]],"date-time":"2025-10-19T01:13:47Z","timestamp":1760836427000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0968089621002844"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,8]]},"references-count":50,"alternative-id":["S0968089621002844"],"URL":"https:\/\/doi.org\/10.1016\/j.bmc.2021.116276","relation":{},"ISSN":["0968-0896"],"issn-type":[{"value":"0968-0896","type":"print"}],"subject":[],"published":{"date-parts":[[2021,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Quantum mechanical study on the activation mechanism of human carbonic anhydrase VII cluster model with bis-histamine schiff bases and bis-spinaceamine derivatives","name":"articletitle","label":"Article Title"},{"value":"Bioorganic & Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bmc.2021.116276","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"116276"}}