{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T09:36:17Z","timestamp":1793093777985,"version":"4.5.0"},"reference-count":53,"publisher":"American Chemical Society (ACS)","license":[{"start":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T00:00:00Z","timestamp":1793059200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T00:00:00Z","timestamp":1793059200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T00:00:00Z","timestamp":1793059200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35GM126961"],"award-info":[{"award-number":["R35GM126961"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Nicotinamidases catalyze the metal-dependent hydrolysis of nicotinamide in the NAD+ salvage pathway in most nonmammalian organisms. Their essential role in pathogenic bacteria, but not mammals, has made them an attractive target for new antibiotic treatments. Most of the characterized nicotinamidases rely on a ZnII active site for catalysis, which has limited spectroscopic studies of these enzymes. Herein, we employ CoII-substitution as a spectroscopic probe to investigate the mechanism of nicotinamidase from the pathogen Streptococcus pneumoniae (SpPncA). The CoII-substituted enzyme features a spin S = 3\/2 EPR signal with resolved hyperfine splitting consistent with a five-coordinate metal center. Analysis of a conserved second-sphere Asp9 residue via site-directed mutagenesis reveals an unexpected role in maintaining the geometry of the metal coordination site through an extended network of electrostatic interactions. Characterization of substrate, intermediate, product, and inhibitor-bound complexes demonstrates that subtle changes in the ligand impact the rhombicity of the EPR spectrum. Leveraging these spectroscopic features, we characterize a catalytically relevant thioester intermediate formed during turnover with nicotinamide for the first time. Together, these results provide new mechanistic insights into nicotinamidase catalysis.<\/jats:p>","DOI":"10.1021\/acs.inorgchem.6c04023","type":"journal-article","created":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T09:01:37Z","timestamp":1793091697000},"source":"Crossref","is-referenced-by-count":0,"title":["Mechanistic\nInsights into Nicotinamidase by CoII EPR Spectroscopy"],"prefix":"10.1021","author":[{"given":"Isabella E.","family":"Acosta","sequence":"first","affiliation":[{"name":"University of California , , , ,","place":["Davis, California, United States, 95616"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8979-0584","authenticated-orcid":true,"given":"Melissa M.","family":"Bollmeyer","sequence":"additional","affiliation":[{"name":"University of California , , , ,","place":["Davis, California, United States, 95616"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0889-8436","authenticated-orcid":true,"given":"R. David","family":"Britt","sequence":"additional","affiliation":[{"name":"University of California , , , ,","place":["Davis, California, United States, 95616"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,10,27]]},"reference":[{"issue":"44","key":"2026102705013361500_cit1","doi-asserted-by":"publisher","first-page":"9613","DOI":"10.1021\/bi1011157","article-title":"Kinetics and Inhibition of Nicotinamidase\nfrom M. tuberculosis","volume":"49","author":"Seiner","year":"2010","journal-title":"Biochemistry"},{"issue":"49","key":"2026102705013361500_cit2","doi-asserted-by":"publisher","first-page":"10421","DOI":"10.1021\/bi1012518","article-title":"Characterization\nof Nicotinamidases: Steady State Kinetic\nParameters, Classwide Inhibition by Nicotinaldehydes, and Catalytic\nMechanism","volume":"49","author":"French","year":"2010","journal-title":"Biochemistry"},{"issue":"4","key":"2026102705013361500_cit3","doi-asserted-by":"publisher","first-page":"753","DOI":"10.1111\/j.1742-4658.2007.06241.x","article-title":"Characterization of M. tuberculosis Nicotinamidase\/Pyrazinamidase","volume":"275","author":"Zhang","year":"2008","journal-title":"FEBS J."},{"issue":"47","key":"2026102705013361500_cit4","doi-asserted-by":"publisher","first-page":"14166","DOI":"10.1021\/bi0115479","article-title":"Crystal Structure\nand Mechanism of Catalysis of a Pyrazinamidase\nfrom Pyrococcus horikoshii","volume":"40","author":"Du","year":"2001","journal-title":"Biochemistry"},{"issue":"1","key":"2026102705013361500_cit5","doi-asserted-by":"publisher","first-page":"54","DOI":"10.1134\/S0006297914010088","article-title":"Nicotinamidase from the Thermophilic\nArchaeon Acidilobus Saccharovorans: Structural and Functional Characteristics","volume":"79","author":"Stekhanova","year":"2014","journal-title":"Biochemistry (Moscow)"},{"issue":"3","key":"2026102705013361500_cit6","doi-asserted-by":"publisher","first-page":"529","DOI":"10.1128\/MMBR.00042-08","article-title":"Microbial\nNAD Metabolism: Lessons from Comparative Genomics","volume":"73","author":"Gazzaniga","year":"2009","journal-title":"Microbiol. 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Hyg."},{"issue":"1","key":"2026102705013361500_cit32","doi-asserted-by":"publisher","first-page":"42","DOI":"10.1016\/j.jmr.2005.08.013","article-title":"EasySpin, a Comprehensive Software Package for Spectral\nSimulation and Analysis in EPR","volume":"178","author":"Stoll","year":"2006","journal-title":"J. Magn. Reson."},{"issue":"1","key":"2026102705013361500_cit33","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1002\/wcms.81","article-title":"The ORCA Program\nSystem","volume":"2","author":"Neese","year":"2012","journal-title":"WIREs Comput. Mol. Sci."},{"issue":"12","key":"2026102705013361500_cit34","doi-asserted-by":"publisher","DOI":"10.1103\/PhysRevB.33.8822","article-title":"Density-Functional\nApproximation for the Correlation Energy of the Inhomogeneous Electron\nGas","volume":"33","author":"Perdew","year":"1986","journal-title":"Phys. Rev. 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Am. Chem. Soc."},{"issue":"10","key":"2026102705013361500_cit46","doi-asserted-by":"publisher","first-page":"2737","DOI":"10.1021\/ic9513548","article-title":"EPR and Magnetic\nSusceptibility Studies of Cobalt(II)- and Nickel(II)-Substituted Azurins\nfrom Pseudomonas aeruginosa. Electronic\nStructure of the Active Sites","volume":"35","author":"Jime\u0301nez","year":"1996","journal-title":"Inorg. Chem."},{"issue":"35","key":"2026102705013361500_cit47","doi-asserted-by":"publisher","first-page":"12282","DOI":"10.1021\/ja0532234","article-title":"Kinetic and\nSpectroscopic Characterization of ACMSD from Pseudomonas fluorescens Reveals a Pentacoordinate Mononuclear\nMetallocofactor","volume":"127","author":"Li","year":"2005","journal-title":"J. Am. Chem. Soc."},{"issue":"7","key":"2026102705013361500_cit48","doi-asserted-by":"publisher","first-page":"2148","DOI":"10.1021\/ja039257y","article-title":"Definitive Spectroscopic\nDetermination of Zero-Field\nSplitting in High-Spin Cobalt(II)","volume":"126","author":"Krzystek","year":"2004","journal-title":"J. Am. Chem.\nSoc."},{"issue":"32","key":"2026102705013361500_cit49","doi-asserted-by":"publisher","first-page":"9837","DOI":"10.1021\/bi970735p","article-title":"Spectroscopically Distinct Cobalt(II) Sites in Heterodimetallic\nForms of the Aminopeptidase from Aeromonas proteolytica: Characterization of Substrate Binding","volume":"36","author":"Bennett","year":"1997","journal-title":"Biochemistry"},{"issue":"19","key":"2026102705013361500_cit50","doi-asserted-by":"publisher","first-page":"5376","DOI":"10.1128\/JB.184.19.5376-5384.2002","article-title":"Purification,\nSubstrate Range, and Metal Center of AtzC: The N-Isopropylammelide\nAminohydrolase Involved in Bacterial Atrazine Metabolism","volume":"184","author":"Shapir","year":"2002","journal-title":"J. Bacteriol."},{"issue":"40","key":"2026102705013361500_cit51","doi-asserted-by":"publisher","first-page":"14100","DOI":"10.1021\/ja054081g","article-title":"argE-Encoded N-Acetyl-l-Ornithine Deacetylase from E. coli Contains a Dinuclear Metalloactive Site","volume":"127","author":"McGregor","year":"2005","journal-title":"J. Am. Chem. Soc."},{"issue":"12","key":"2026102705013361500_cit52","doi-asserted-by":"publisher","first-page":"11074","DOI":"10.1074\/jbc.M412582200","article-title":"A Five-Coordinate\nMetal Center in\nCo(II)-Substituted VanX","volume":"280","author":"Breece","year":"2005","journal-title":"J. Biol. Chem."},{"issue":"4","key":"2026102705013361500_cit53","doi-asserted-by":"publisher","first-page":"1313","DOI":"10.1021\/bi051105n","article-title":"Sequential Binding of Cobalt(II) to Metallo-\u03b2-Lactamase\nCcrA","volume":"45","author":"Periyannan","year":"2006","journal-title":"Biochemistry"}],"container-title":["Inorganic Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.inorgchem.6c04023","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/inocaj\/article-pdf\/doi\/10.1021\/acs.inorgchem.6c04023\/68988614\/acs.inorgchem.6c04023.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/inocaj\/article-pdf\/doi\/10.1021\/acs.inorgchem.6c04023\/68988614\/acs.inorgchem.6c04023.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T09:09:11Z","timestamp":1793092151000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/inocaj\/article\/doi\/10.1021\/acs.inorgchem.6c04023\/5458743\/Mechanistic-Insights-into-Nicotinamidase-by-CoII"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10,27]]},"references-count":53,"URL":"https:\/\/doi.org\/10.1021\/acs.inorgchem.6c04023","relation":{},"ISSN":["0020-1669","1520-510X"],"issn-type":[{"value":"0020-1669","type":"print"},{"value":"1520-510X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,10,27]]}}}