{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,4]],"date-time":"2026-05-04T12:45:59Z","timestamp":1777898759369,"version":"3.51.4"},"reference-count":29,"publisher":"Elsevier","isbn-type":[{"value":"9780443346477","type":"print"}],"license":[{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001407","name":"Department of Biotechnology, Ministry of Science and Technology, India","doi-asserted-by":"publisher","award":["BT\/PR45880\/BCE\/8\/1634\/2022"],"award-info":[{"award-number":["BT\/PR45880\/BCE\/8\/1634\/2022"]}],"id":[{"id":"10.13039\/501100001407","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024]]},"DOI":"10.1016\/bs.mie.2024.05.014","type":"book-chapter","created":{"date-parts":[[2024,6,8]],"date-time":"2024-06-08T14:21:19Z","timestamp":1717856479000},"page":"39-58","source":"Crossref","is-referenced-by-count":1,"title":["Expression, purification, kinetics, and crystallization of non-heme mononuclear iron enzymes: Biphenyl, Phthalate, and Terephthalate dioxygenases"],"prefix":"10.1016","author":[{"given":"Jai Krishna","family":"Mahto","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Arpan","family":"Kayastha","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pravindra","family":"Kumar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"10","key":"10.1016\/bs.mie.2024.05.014_bib1","doi-asserted-by":"crossref","first-page":"2362","DOI":"10.1021\/cs400087p","article-title":"Mechanism and catalytic diversity of Rieske non-heme iron-dependent oxygenases","volume":"3","author":"Barry","year":"2013","journal-title":"ACS Catalysis"},{"issue":"5","key":"10.1016\/bs.mie.2024.05.014_bib2","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1021\/acsenvironau.2c00023","article-title":"Elucidating the role of O2 uncoupling in the oxidative biodegradation of organic contaminants by rieske non-heme iron dioxygenases","volume":"2","author":"Bopp","year":"2022","journal-title":"ACS Environmental Au"},{"issue":"1","key":"10.1016\/bs.mie.2024.05.014_bib3","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0052550","article-title":"Structural characterization of Pandoraea pnomenusa B-356 biphenyl dioxygenase reveals features of potent polychlorinated biphenyl-degrading enzymes","volume":"8","author":"Colbert","year":"2013","journal-title":"PLoS One"},{"issue":"10","key":"10.1016\/bs.mie.2024.05.014_bib4","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1128\/JB.00952-15","article-title":"Structural basis of the enhanced pollutant-degrading capabilities of an engineered biphenyl dioxygenase","volume":"198","author":"Dhindwal","year":"2016","journal-title":"Journal of Bacteriology"},{"issue":"1","key":"10.1016\/bs.mie.2024.05.014_bib5","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.bbrc.2005.08.222","article-title":"Rieske business: Structure\u2013function of Rieske non-heme oxygenases","volume":"338","author":"Ferraro","year":"2005","journal-title":"Biochemical and Biophysical Research Communications"},{"issue":"15","key":"10.1016\/bs.mie.2024.05.014_bib6","doi-asserted-by":"crossref","first-page":"5705","DOI":"10.1128\/JB.01476-06","article-title":"Characterization of biphenyl dioxygenase of Pandoraea pnomenusa B-356 as a potent polychlorinated biphenyl-degrading enzyme","volume":"189","author":"G\u00f3mez-Gil","year":"2007","journal-title":"Journal of Bacteriology"},{"issue":"51","key":"10.1016\/bs.mie.2024.05.014_bib7","doi-asserted-by":"crossref","first-page":"21637","DOI":"10.1021\/jacs.1c10051","article-title":"A reactive, photogenerated high-spin (S=2) FeIV(O) complex via O2 activation","volume":"143","author":"Gordon","year":"2021","journal-title":"Journal of the American Chemical Society"},{"issue":"6","key":"10.1016\/bs.mie.2024.05.014_bib8","doi-asserted-by":"crossref","DOI":"10.1128\/AEM.01629-20","article-title":"Structural and biochemical analysis reveals a distinct catalytic site of salicylate 5-monooxygenase NagGH from Rieske dioxygenases","volume":"87","author":"Hou","year":"2021","journal-title":"Applied and Environmental Microbiology"},{"key":"10.1016\/bs.mie.2024.05.014_bib9","doi-asserted-by":"crossref","first-page":"3338","DOI":"10.1039\/b702158e","article-title":"Cysteine dioxygenase: Structure and mechanism","volume":"32","author":"Joseph","year":"2007","journal-title":"Chemical Communications"},{"issue":"5609","key":"10.1016\/bs.mie.2024.05.014_bib10","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1126\/science.1078020","article-title":"Crystal structure of naphthalene dioxygenase: Side-on binding of dioxygen to iron","volume":"299","author":"Karlsson","year":"2003","journal-title":"Science (New York, N. Y.)"},{"issue":"13","key":"10.1016\/bs.mie.2024.05.014_bib11","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2121426119","article-title":"Biochemical and structural characterization of an aromatic ring\u2013hydroxylating dioxygenase for terephthalic acid catabolism","volume":"119","author":"Kincannon","year":"2022","journal-title":"Proceedings of the National Academy of Sciences"},{"key":"10.1016\/bs.mie.2024.05.014_bib12","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1007\/s00775-005-0624-x","article-title":"The 2-His-1-carboxylate facial triad: A versatile platform for dioxygen activation by mononuclear non-heme iron (II) enzymes. JBIC","volume":"10","author":"Koehntop","year":"2005","journal-title":"Journal of Biological Inorganic Chemistry"},{"issue":"3","key":"10.1016\/bs.mie.2024.05.014_bib13","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1038\/nchembio.71","article-title":"Versatility of biological non-heme Fe (II) centers in oxygen activation reactions","volume":"4","author":"Kovaleva","year":"2008","journal-title":"Nature Chemical Biology"},{"issue":"Pt 1","key":"10.1016\/bs.mie.2024.05.014_bib14","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1107\/S1744309110043393","article-title":"Anaerobic crystallization and initial X-ray diffraction data of biphenyl 2,3-dioxygenase from Burkholderia xenovorans LB400: Addition of agarose improved the quality of the crystals","volume":"67","author":"Kumar","year":"2011","journal-title":"Acta Crystallographica. Section F, Structural Biology and Crystallization Communications"},{"issue":"4","key":"10.1016\/bs.mie.2024.05.014_bib15","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1016\/j.bbrc.2012.04.078","article-title":"Structural insights into the metabolism of 2-chlorodibenzofuran by an evolved biphenyl dioxygenase","volume":"421","author":"Kumar","year":"2012","journal-title":"Biochemical and Biophysical Research Communications"},{"issue":"1","key":"10.1016\/bs.mie.2024.05.014_bib16","doi-asserted-by":"crossref","first-page":"1301","DOI":"10.1038\/s41467-021-21567-9","article-title":"Structure-guided insights into heterocyclic ring-cleavage catalysis of the non-heme Fe (II) dioxygenase NicX","volume":"12","author":"Liu","year":"2021","journal-title":"Nature Communications"},{"issue":"1","key":"10.1016\/bs.mie.2024.05.014_bib17","doi-asserted-by":"crossref","first-page":"2991","DOI":"10.1038\/s41467-020-16729-0","article-title":"Structural basis for divergent C\u2013H hydroxylation selectivity in two Rieske oxygenases","volume":"11","author":"Lukowski","year":"2020","journal-title":"Nature Communications"},{"issue":"3","key":"10.1016\/bs.mie.2024.05.014_bib18","doi-asserted-by":"crossref","DOI":"10.1128\/jb.00543-21","article-title":"Structural insights into dihydroxylation of terephthalate, a product of polyethylene terephthalate degradation","volume":"204","author":"Mahto","year":"2022","journal-title":"Journal of Bacteriology"},{"issue":"6","key":"10.1016\/bs.mie.2024.05.014_bib19","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.101416","article-title":"Molecular insights into substrate recognition and catalysis by phthalate dioxygenase from Comamonas testosteroni","volume":"297","author":"Mahto","year":"2021","journal-title":"The Journal of Biological Chemistry"},{"issue":"11","key":"10.1016\/bs.mie.2024.05.014_bib20","doi-asserted-by":"crossref","first-page":"6444","DOI":"10.1021\/acscatal.2c00383","article-title":"Substrate-specific coupling of O2 activation to hydroxylations of aromatic compounds by Rieske non-heme iron dioxygenases","volume":"12","author":"Pati","year":"2022","journal-title":"ACS Catalysis"},{"issue":"7","key":"10.1016\/bs.mie.2024.05.014_bib21","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1039\/C8NP00004B","article-title":"Rieske non-heme iron-dependent oxygenases catalyse diverse reactions in natural product biosynthesis","volume":"35","author":"Perry","year":"2018","journal-title":"Natural Product Reports"},{"issue":"46","key":"10.1016\/bs.mie.2024.05.014_bib22","doi-asserted-by":"crossref","first-page":"3497","DOI":"10.1021\/acs.biochem.1c00370","article-title":"Mechanisms of O2 activation by mononuclear non-heme iron enzymes","volume":"60","author":"Solomon","year":"2021","journal-title":"Biochemistry"},{"issue":"46","key":"10.1016\/bs.mie.2024.05.014_bib23","doi-asserted-by":"crossref","first-page":"6363","DOI":"10.1021\/acs.biochem.6b00635","article-title":"O2 activation by non-heme iron enzymes","volume":"55","author":"Solomon","year":"2016","journal-title":"Biochemistry"},{"issue":"11","key":"10.1016\/bs.mie.2024.05.014_bib24","doi-asserted-by":"crossref","first-page":"2725","DOI":"10.1021\/ar400149m","article-title":"Geometric and electronic structure contributions to function in non-heme iron enzymes","volume":"46","author":"Solomon","year":"2013","journal-title":"Accounts of Chemical Research"},{"issue":"1","key":"10.1016\/bs.mie.2024.05.014_bib25","doi-asserted-by":"crossref","first-page":"5858","DOI":"10.1038\/s41467-023-41428-x","article-title":"Custom tuning of Rieske oxygenase reactivity","volume":"14","author":"Tian","year":"2023","journal-title":"Nature Communications"},{"issue":"9","key":"10.1016\/bs.mie.2024.05.014_bib26","doi-asserted-by":"crossref","first-page":"5489","DOI":"10.1021\/acscatal.2c01143","article-title":"Are vanadium intermediates suitable mimics in non-heme iron enzymes? An electronic structure analysis","volume":"12","author":"Vennelakanti","year":"2022","journal-title":"ACS Catalysis"},{"key":"10.1016\/bs.mie.2024.05.014_bib27","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1016\/j.cbpa.2016.02.017","article-title":"Catalytic strategies of the non-heme iron dependent oxygenases and their roles in plant biology","volume":"31","author":"White","year":"2016","journal-title":"Current Opinion in Chemical Biology"},{"issue":"17","key":"10.1016\/bs.mie.2024.05.014_bib28","doi-asserted-by":"crossref","first-page":"10913","DOI":"10.1021\/acscatal.2c00954","article-title":"Role of secondary coordination sphere residues in halogenation catalysis of non-heme iron enzymes","volume":"12","author":"Wilson","year":"2022","journal-title":"ACS Catalysis"},{"issue":"6","key":"10.1016\/bs.mie.2024.05.014_bib29","doi-asserted-by":"crossref","first-page":"3587","DOI":"10.1021\/acs.est.1c08532","article-title":"Oxygen and chlorine dual vacancies enable photocatalytic O2 dissociation into monatomic reactive oxygen on BiOCl for refractory aromatic pollutant removal","volume":"56","author":"Yang","year":"2022","journal-title":"Environmental Science & Technology"}],"container-title":["Methods in Enzymology","Mononuclear Non-heme Iron Dependent Enzymes Part B"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0076687924002258?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0076687924002258?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,10,11]],"date-time":"2024-10-11T19:44:21Z","timestamp":1728675861000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0076687924002258"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024]]},"ISBN":["9780443346477"],"references-count":29,"URL":"https:\/\/doi.org\/10.1016\/bs.mie.2024.05.014","relation":{},"ISSN":["0076-6879"],"issn-type":[{"value":"0076-6879","type":"print"}],"subject":[],"published":{"date-parts":[[2024]]}}}