{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T18:12:47Z","timestamp":1788372767525,"version":"build-2803163510"},"reference-count":56,"publisher":"American Chemical Society (ACS)","issue":"44","license":[{"start":{"date-parts":[[2015,10,21]],"date-time":"2015-10-21T00:00:00Z","timestamp":1445385600000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/100000774","name":"Defense Threat Reduction Agency","doi-asserted-by":"publisher","award":["CBM.THERB.02.11.RD.012"],"award-info":[{"award-number":["CBM.THERB.02.11.RD.012"]}],"id":[{"id":"10.13039\/100000774","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,11,11]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The CapD enzyme of Bacillus anthracis is a \u03b3-glutamyl transpeptidase from the N-terminal nucleophile hydrolase superfamily that covalently anchors the poly-\u03b3-d-glutamic acid (pDGA) capsule to the peptidoglycan. The capsule hinders phagocytosis of B. anthracis by host cells and is essential for virulence. The role CapD plays in capsule anchoring and remodeling makes the enzyme a promising target for anthrax medical countermeasures. Although the structure of CapD is known, and a covalent inhibitor, capsidin, has been identified, the mechanisms of CapD catalysis and inhibition are poorly understood. Here, we used a computational approach to map out the reaction steps involved in CapD catalysis and inhibition. We found that the rate-limiting step of either CapD catalysis or inhibition was a concerted asynchronous formation of the tetrahedral intermediate with a barrier of 22\u201323 kcal\/mol. However, the mechanisms of these reactions differed for the two amides. The formation of the tetrahedral intermediate with pDGA was substrate-assisted with two proton transfers. In contrast, capsidin formed the tetrahedral intermediate in a conventional way with one proton transfer. Interestingly, capsidin coupled a conformational change in the catalytic residue of the tetrahedral intermediate to stretching of the scissile amide bond. Furthermore, capsidin took advantage of iminol\u2013amide tautomerism of its diacetamide moiety to convert the tetrahedral intermediate to the acetylated CapD. As evidence of the promiscuous nature of CapD, the enzyme cleaved the amide bond of capsidin by attacking it on the opposite side compared to pDGA.<\/jats:p>","DOI":"10.1021\/bi500623c","type":"journal-article","created":{"date-parts":[[2014,10,21]],"date-time":"2014-10-21T11:52:01Z","timestamp":1413892321000},"page":"6954-6967","source":"Crossref","is-referenced-by-count":8,"title":["A Reaction Path Study of the Catalysis and Inhibition\nof the\n                    <i>Bacillus anthracis<\/i>\n                    CapD \u03b3-Glutamyl\nTranspeptidase"],"prefix":"10.1021","volume":"53","author":[{"given":"Ilja V.","family":"Khavrutskii","sequence":"first","affiliation":[{"name":"United States Army Medical Research and Materiel Command , , , ,","place":["Fort Detrick, Maryland, United States, 21702"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patricia M.","family":"Legler","sequence":"additional","affiliation":[{"name":"Naval Research Laboratories , , ,","place":["Washington, D.C., United States, 20375"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arthur M.","family":"Friedlander","sequence":"additional","affiliation":[{"name":"United States Army Medical Research Institute of Infectious Diseases , , ,","place":["Fort Detrick, Maryland, United States, 21702"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anders","family":"Wallqvist","sequence":"additional","affiliation":[{"name":"United States Army Medical Research and Materiel Command , , , ,","place":["Fort Detrick, Maryland, United States, 21702"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2014,10,21]]},"reference":[{"issue":"3","key":"2026090213164367900_cit1","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1136\/jcp.56.3.182","article-title":"Bacillus anthracis","volume":"56","author":"Spencer","year":"2003","journal-title":"J. Clin. Pathol."},{"key":"2026090213164367900_cit2","first-page":"2715","article-title":"Bacillus anthracis (Anthrax)","volume-title":"Principles and Practices of\nInfectious Diseases","author":"Martin","year":"2010"},{"issue":"5","key":"2026090213164367900_cit3","first-page":"477","article-title":"The Chemical Basis of the Virulence\nof Bacillus anthracis. I: Properties of Bacteria\nGrown in vivo and Preparation of Extracts","volume":"34","author":"Smith","year":"1953","journal-title":"Br.\nJ. Exp. Pathol."},{"issue":"4","key":"2026090213164367900_cit4","first-page":"446","article-title":"The Chemical Basis of the Virulence\nof Bacillus anthracis IX. Its Aggressins and Their\nMode of Action","volume":"44","author":"Keppie","year":"1963","journal-title":"Br. J. Exp. Pathol."},{"issue":"2","key":"2026090213164367900_cit5","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1128\/jb.171.2.722-730.1989","article-title":"Molecular\nCharacterization and Protein Analysis of the Cap Region, Which Is\nEssential for Encapsulation in Bacillus anthracis","volume":"171","author":"Makino","year":"1989","journal-title":"J. Bacteriol."},{"issue":"1","key":"2026090213164367900_cit6","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1128\/AAC.00706-06","article-title":"Poly-\u03b3-glutamate Capsule-Degrading Enzyme Treatment\nEnhances Phagocytosis and Killing of Encapsulated Bacillus anthracis","volume":"51","author":"Scorpio","year":"2007","journal-title":"Antimicrob. Agents Chemother."},{"issue":"2","key":"2026090213164367900_cit7","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1128\/IAI.00764-08","article-title":"Association of Bacillus anthracis Capsule\nwith Lethal Toxin during Experimental Infection","volume":"77","author":"Ezzell","year":"2009","journal-title":"Infect. Immun."},{"issue":"6","key":"2026090213164367900_cit8","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1016\/j.mam.2009.07.001","article-title":"The Surface\nof Bacillus anthracis","volume":"30","author":"Fouet","year":"2009","journal-title":"Mol.\nAspects Med."},{"issue":"5","key":"2026090213164367900_cit9","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1111\/j.1365-2958.2006.05179.x","article-title":"Poly-\u03b3-glutamate in Bacteria","volume":"60","author":"Candela","year":"2006","journal-title":"Mol. Microbiol."},{"issue":"2","key":"2026090213164367900_cit10","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1111\/j.1365-2958.2008.06533.x","article-title":"Capsule Anchoring in Bacillus anthracis Occurs by a Transpeptidation Reaction that is Inhibited by Capsidin","volume":"71","author":"Richter","year":"2009","journal-title":"Mol. Microbiol."},{"issue":"12","key":"2026090213164367900_cit11","doi-asserted-by":"crossref","first-page":"2329","DOI":"10.1110\/ps.9.12.2329","article-title":"Structural Comparison of Ntn-Hydrolases","volume":"9","author":"Oinonen","year":"2000","journal-title":"Protein Sci."},{"issue":"3","key":"2026090213164367900_cit12","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1111\/j.1365-2958.1993.tb01710.x","article-title":"Identification of a novel gene, dep, associated with depolymerization of the capsular polymer\nin Bacillus anthracis","volume":"9","author":"Uchida","year":"1993","journal-title":"Mol.\nMicrobiol."},{"issue":"2","key":"2026090213164367900_cit13","doi-asserted-by":"crossref","first-page":"686","DOI":"10.1073\/pnas.0911839107","article-title":"The Quorum-Quenching\nN-Acyl Homoserine Lactone Acylase PvdQ Is an Ntn-Hydrolase With an\nUnusual Substrate-Binding Pocket","volume":"107","author":"Bokhove","year":"2010","journal-title":"Proc. Natl.\nAcad. Sci. U.S.A."},{"issue":"9","key":"2026090213164367900_cit14","doi-asserted-by":"crossref","first-page":"2589","DOI":"10.1111\/j.1742-4658.2009.06987.x","article-title":"Do N-Terminal Nucleophile Hydrolases Indeed Have a\nSingle Amino Acid Catalytic Center? Supporting Amino Acid Residues\nat the Active Site of Penicilin G Acylase","volume":"276","author":"Zhiryakova","year":"2009","journal-title":"FEBS\nJ."},{"issue":"5","key":"2026090213164367900_cit15","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1134\/S0006297907050057","article-title":"Quantum Chemical Studies of the Catalytic\nMechanism of N-Terminal Nucleophile Hydrolase","volume":"72","author":"Chilov","year":"2007","journal-title":"Biochemistry (Moscow)"},{"issue":"6","key":"2026090213164367900_cit16","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1021\/ja9628967","article-title":"A Simulation of the Catalytic Mechanism of Aspartylglucosaminidase\nUsing ab Initio Quantum Mechanics and Molecular Dynamics","volume":"119","author":"Perakyla","year":"1997","journal-title":"J. Am. Chem. Soc."},{"issue":"12","key":"2026090213164367900_cit17","first-page":"1548","article-title":"Ab Initio Quantum Mechanical Model\nCalculations on\nthe Catalytic Mechanism of Aspartylglucosaminidase (AGA): A Serine\nProtease-Like Mechanism with an N-Terminal Threonine and Substrate-Assisted\nCatalysis","volume":"2","author":"Perakyla","year":"1996","journal-title":"Chem.\u2500Eur. J."},{"issue":"1","key":"2026090213164367900_cit18","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1046\/j.1365-2958.1999.01137.x","article-title":"Germination of Bacillus anthracis Spores within Alveolar Macrophages","volume":"31","author":"Guidi-Rontani","year":"1999","journal-title":"Mol. Microbiol."},{"issue":"12","key":"2026090213164367900_cit19","doi-asserted-by":"crossref","first-page":"4374","DOI":"10.1128\/IAI.01011-12","article-title":"Bacillus anthracis Lethal Toxin Reduces Human Alveolar Epithelial\nBarrier Function","volume":"80","author":"Langer","year":"2012","journal-title":"Infect. Immun."},{"issue":"3","key":"2026090213164367900_cit20","doi-asserted-by":"crossref","first-page":"1014","DOI":"10.1128\/AAC.00741-07","article-title":"Treatment\nof Experimental Anthrax with Recombinant Capsule Depolymerase","volume":"52","author":"Scorpio","year":"2008","journal-title":"Antimicrob. Agents Chemother."},{"issue":"5","key":"2026090213164367900_cit21","doi-asserted-by":"crossref","first-page":"1459","DOI":"10.1099\/mic.0.035857-0","article-title":"Capsule\nDepolymerase Overexpression Reduces Bacillus anthracis Virulence","volume":"156","author":"Scorpio","year":"2010","journal-title":"Microbiology"},{"issue":"37","key":"2026090213164367900_cit22","doi-asserted-by":"crossref","first-page":"32586","DOI":"10.1074\/jbc.M111.251041","article-title":"Improvement of a\nPotential Anthrax Therapeutic by Computational Protein Design","volume":"286","author":"Wu","year":"2011","journal-title":"J. Biol. Chem."},{"issue":"2","key":"2026090213164367900_cit23","doi-asserted-by":"crossref","first-page":"e32397","DOI":"10.1371\/journal.pone.0032397","article-title":"A Catalytic Mechanism for Cysteine\nN-Terminal Nucleophile Hydrolases, as Revealed by Free Energy Simulations","volume":"7","author":"Lodola","year":"2012","journal-title":"PLoS One"},{"issue":"46","key":"2026090213164367900_cit24","doi-asserted-by":"crossref","first-page":"13407","DOI":"10.1021\/bi701599e","article-title":"Characterization\nof Helicobacter pylori \u03b3-Glutamyltranspeptidase\nReveals the Molecular Basis for Substrate Specificity and a Critical\nRole for the Tyrosine 433-Containing Loop in Catalysis","volume":"46","author":"Morrow","year":"2007","journal-title":"Biochemistry"},{"issue":"44","key":"2026090213164367900_cit25","doi-asserted-by":"crossref","first-page":"31902","DOI":"10.1074\/jbc.M113.498139","article-title":"Novel Insights into Eukaryotic \u03b3-Glutamyltranspeptidase\n1 from the Crystal Structure of the Glutamate-bound Human Enzyme","volume":"288","author":"West","year":"2013","journal-title":"J. Biol. Chem."},{"issue":"4","key":"2026090213164367900_cit26","doi-asserted-by":"crossref","first-page":"1000","DOI":"10.1111\/j.1742-4658.2009.07543.x","article-title":"Crystal Structure\nof\nthe Halotolerant \u03b3-Glutamyltranspeptidase from Bacillus subtilis in Complex with Glutamate Reveals a Unique Architecture\nof the Solvent-Exposed Catalytic Pocket","volume":"277","author":"Wada","year":"2010","journal-title":"FEBS\nJ."},{"issue":"2","key":"2026090213164367900_cit27","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/j.jmb.2008.05.007","article-title":"Crystal Structures\nof Escherichia coli \u03b3-Glutamyltranspeptidase\nin Complex with Azaserine and Acivicin: Novel Mechanistic Implication\nfor Inhibition by Glutamine Antagonists","volume":"380","author":"Wada","year":"2008","journal-title":"J.\nMol. Biol."},{"issue":"1","key":"2026090213164367900_cit28","doi-asserted-by":"crossref","first-page":"534","DOI":"10.1074\/jbc.M607694200","article-title":"Autoprocessing of Helicobacter pylori \u03b3-Glutamyltranspeptidase Leads to the Formation\nof a Threonine-Threonine Catalytic Dyad","volume":"282","author":"Boanca","year":"2007","journal-title":"J.\nBiol. Chem."},{"issue":"36","key":"2026090213164367900_cit29","doi-asserted-by":"crossref","first-page":"24406","DOI":"10.1074\/jbc.M109.019034","article-title":"Crystal Structure of Bacillus anthracis Transpeptidase Enzyme CapD","volume":"284","author":"Wu","year":"2009","journal-title":"J. Biol. Chem."},{"issue":"17","key":"2026090213164367900_cit30","doi-asserted-by":"crossref","first-page":"6471","DOI":"10.1073\/pnas.0511020103","article-title":"Crystal Structures\nof \u03b3-Glutamyltranspeptidase from Escherichia coli, a Key Enzyme in Glutathione Metabolism, and Its Reaction Intermediate","volume":"103","author":"Okada","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"6","key":"2026090213164367900_cit31","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1021\/bi200987b","article-title":"Probing the\nDonor and Acceptor Substrate Specificity of the \u03b3-Glutamyl Transpeptidase","volume":"51","author":"Hu","year":"2012","journal-title":"Biochemistry"},{"issue":"2","key":"2026090213164367900_cit32","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1002\/jcc.21334","article-title":"AutoDock Vina: Improving the Speed and Accuracy of\nDocking with a New Scoring Function, Efficient Optimization, and Multithreading","volume":"31","author":"Trott","year":"2010","journal-title":"J. Comput. Chem."},{"issue":"16","key":"2026090213164367900_cit33","doi-asserted-by":"crossref","first-page":"165104","DOI":"10.1063\/1.4826470","article-title":"Exploring Chemical Reaction Mechanisms\nthrough Harmonic Fourier Beads Path Optimization","volume":"139","author":"Khavrutskii","year":"2013","journal-title":"J. Chem. Phys."},{"issue":"50","key":"2026090213164367900_cit34","doi-asserted-by":"crossref","first-page":"19357","DOI":"10.1021\/jp962071j","article-title":"ONIOM: A Multilayered Integrated\nMO+MM Method for Geometry Optimizations and Single Point Energy Predictions.\nA Test for Diels-Alder Reactions and Pt(P(t-Bu)3)2 + H2 Oxidative Addition","volume":"100","author":"Svensson","year":"1996","journal-title":"J. Phys.\nChem."},{"key":"2026090213164367900_cit35","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0166-1280(98)00475-8","article-title":"A New ONIOM\nImplementation in Gaussian98. Part I. The Calculation of Energies,\nGradients, Vibrational Frequencies and Electric Field Derivatives","volume":"461","author":"Dapprich","year":"1999","journal-title":"J. Mol. Struct.: THEOCHEM"},{"issue":"3","key":"2026090213164367900_cit36","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1021\/ct050289g","article-title":"Combining Quantum Mechanics Methods\nwith Molecular Mechanics Methods in ONIOM","volume":"2","author":"Vreven","year":"2006","journal-title":"J.\nChem. Theory Comput."},{"issue":"4813","key":"2026090213164367900_cit37","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1126\/science.3299704","article-title":"Engineering Enzyme Specificity by \u201cSubstrate-Assisted\nCatalysis\u201d","volume":"237","author":"Carter","year":"1987","journal-title":"Science"},{"key":"2026090213164367900_cit38","volume-title":"GaussView","author":"Dennington","year":"2009"},{"issue":"19","key":"2026090213164367900_cit39","doi-asserted-by":"crossref","first-page":"5179","DOI":"10.1021\/ja00124a002","article-title":"A Second Generation Force Field for\nthe Simulation\nof Proteins, Nucleic Acids, and Organic Molecules","volume":"117","author":"Cornell","year":"1995","journal-title":"J. Am. Chem. 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Graphics Modell."},{"key":"2026090213164367900_cit42","volume-title":"Gaussian 09","author":"Frisch","year":"2009"},{"issue":"5204","key":"2026090213164367900_cit43","doi-asserted-by":"crossref","first-page":"1619","DOI":"10.1126\/science.7886447","article-title":"Navigating\nthe Folding Routes","volume":"267","author":"Wolynes","year":"1995","journal-title":"Science"},{"issue":"1","key":"2026090213164367900_cit44","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1038\/nsb0197-10","article-title":"From Levinthal to\nPathways to Funnels","volume":"4","author":"Dill","year":"1997","journal-title":"Nat. Struct. Mol. Biol."},{"issue":"13","key":"2026090213164367900_cit45","doi-asserted-by":"crossref","first-page":"3902","DOI":"10.1021\/ja00299a024","article-title":"AM1: A New General\nPurpose Quantum Mechanical Molecular Model","volume":"107","author":"Dewar","year":"1985","journal-title":"J. Am. Chem. Soc."},{"key":"2026090213164367900_cit46","first-page":"35","volume-title":"Hybrid Methods: ONIOM(QM:MM) and QM\/MM","author":"Vreven","year":"2006"},{"issue":"6","key":"2026090213164367900_cit47","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1002\/jcc.10156","article-title":"Geometry\nOptimization with QM\/MM, ONIOM, and Other Combined Methods. I. Microiterations\nand Constraints","volume":"24","author":"Vreven","year":"2003","journal-title":"J. Comput. Chem."},{"issue":"4","key":"2026090213164367900_cit48","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1016\/j.bbrc.2013.06.109","article-title":"Structural\nModelling of Substrate Binding and Inhibition in Penicillin V Acylase\nfrom Pectobacterium atrosepticum","volume":"437","author":"Avinash","year":"2013","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"23","key":"2026090213164367900_cit49","doi-asserted-by":"crossref","first-page":"4186","DOI":"10.1016\/j.febslet.2012.10.019","article-title":"Crossover Inhibition as an Indicator\nof Convergent Evolution of Enzyme Mechanisms: A \u03b2-Lactamase\nand an N-Terminal Nucleophile Hydrolase","volume":"586","author":"Adediran","year":"2012","journal-title":"FEBS\nLett."},{"issue":"8","key":"2026090213164367900_cit50","doi-asserted-by":"crossref","first-page":"E653","DOI":"10.1073\/pnas.1221050110","article-title":"Intrinsic Evolutionary Constraints on Protease Structure,\nEnzyme Acylation, and the Identity of the Catalytic Triad","volume":"110","author":"Buller","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"2","key":"2026090213164367900_cit51","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1073\/pnas.70.2.430","article-title":"Temperature\nAdaptation of Enzymes:\nRoles of the Free Energy, the Enthalpy, and the Entropy of Activation","volume":"70","author":"Low","year":"1973","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"1","key":"2026090213164367900_cit52","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1006\/jmbi.2001.5043","article-title":"Crystal\nStructures of Penicillin Acylase Enzyme-Substrate Complexes: Structural\nInsights into the Catalytic Mechanism","volume":"313","author":"McVey","year":"2001","journal-title":"J. Mol.\nBiol."},{"issue":"6511","key":"2026090213164367900_cit53","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1038\/373264a0","article-title":"Penicillin Acylase Has a Single-Amino-Acid Catalytic\nCentre","volume":"373","author":"Duggleby","year":"1995","journal-title":"Nature"},{"issue":"12","key":"2026090213164367900_cit54","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1093\/protein\/13.12.857","article-title":"Characterization of \u03b2-Lactam\nBinding Site of Penicilin Acylase of Escherichia coli by Structural and Site-Directed Mutagenesis Studies","volume":"13","author":"Alkema","year":"2000","journal-title":"Protein Eng."},{"issue":"1","key":"2026090213164367900_cit55","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1111\/febs.12591","article-title":"pH-Dependent Hydrolase,\nGlutaminase, Transpeptidase and Autotranspeptidase Activities of Bacillus subtilis \u03b3-Glutamyltransferase","volume":"281","author":"Morelli","year":"2014","journal-title":"FEBS J."},{"key":"2026090213164367900_cit56","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1155\/2014\/216270","article-title":"Effect of pH on the Hydrolytic Kinetics of \u03b3-Glutamyl\nTransferase from Bacillus subtilis","volume":"2014","author":"Balakrishna","year":"2014","journal-title":"Sci. World J."}],"container-title":["Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/bi500623c","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/bichaw\/article-pdf\/53\/44\/6954\/15696419\/bi500623c.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/bichaw\/article-pdf\/53\/44\/6954\/15696419\/bi500623c.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T17:16:53Z","timestamp":1788369413000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/bichaw\/article\/53\/44\/6954\/1476946\/A-Reaction-Path-Study-of-the-Catalysis-and"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,10,21]]},"references-count":56,"journal-issue":{"issue":"44","published-online":{"date-parts":[[2014,10,21]]},"published-print":{"date-parts":[[2014,11,11]]}},"URL":"https:\/\/doi.org\/10.1021\/bi500623c","relation":{},"ISSN":["0006-2960","1520-4995"],"issn-type":[{"value":"0006-2960","type":"print"},{"value":"1520-4995","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,10,21]]}}}