{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T07:31:18Z","timestamp":1761636678841,"version":"build-2065373602"},"reference-count":31,"publisher":"Elsevier","isbn-type":[{"type":"print","value":"9780443415739"}],"license":[{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["1R01GM141086"],"award-info":[{"award-number":["1R01GM141086"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2025]]},"DOI":"10.1016\/bs.mie.2025.06.029","type":"book-chapter","created":{"date-parts":[[2025,7,23]],"date-time":"2025-07-23T08:32:54Z","timestamp":1753259574000},"page":"293-311","source":"Crossref","is-referenced-by-count":0,"title":["Breaking symmetry: Metal-guided assembly of heterotrimeric coiled coils"],"prefix":"10.1016","member":"78","reference":[{"key":"10.1016\/bs.mie.2025.06.029_bib1","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1016\/S0022-2836(02)00624-1","article-title":"The 2.0 \u00e5 resolution structure of the catalytic portion of a cyanobacterial membrane-bound manganese superoxide dismutase","volume":"321","author":"Atzenhofer","year":"2002","journal-title":"Journal of Molecular Biology"},{"year":"2007","series-title":"Biological inorganic chemistry: Structure and reactivity","author":"Bertini","key":"10.1016\/bs.mie.2025.06.029_bib2"},{"key":"10.1016\/bs.mie.2025.06.029_bib3","doi-asserted-by":"crossref","DOI":"10.1002\/chem.202304367","article-title":"Co(II) substitution enhances the esterase activity of a de novo designed Zn(II) carbonic anhydrase","volume":"30","author":"Borghesani","year":"2024","journal-title":"Chemistry \u2013 A European Journal"},{"key":"10.1016\/bs.mie.2025.06.029_bib4","doi-asserted-by":"crossref","first-page":"15786","DOI":"10.1002\/ange.201707637","article-title":"A de novo heterodimeric Due Ferri protein minimizes the release of reactive intermediates in dioxygen-dependent oxidation","volume":"129","author":"Chino","year":"2017","journal-title":"Angewandte Chemie International Edition"},{"key":"10.1016\/bs.mie.2025.06.029_bib5","doi-asserted-by":"crossref","first-page":"13687","DOI":"10.1021\/bi001649j","article-title":"Structural influence of hydrophobic core residues on metal binding and specificity in carbonic anhydrase II","volume":"39","author":"Cox","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/bs.mie.2025.06.029_bib6","doi-asserted-by":"crossref","first-page":"6195","DOI":"10.1021\/ja964351i","article-title":"De novo design of mercury-binding two- and three-helical bundles","volume":"119","author":"Dieckmann","year":"1997","journal-title":"Journal of the American Chemical Society"},{"key":"10.1016\/bs.mie.2025.06.029_bib7","doi-asserted-by":"crossref","first-page":"7902","DOI":"10.1021\/ic048939z","article-title":"Understanding metalloprotein folding using a de novo design strategy","volume":"43","author":"Ghosh","year":"2004","journal-title":"Inorganic Chemistry"},{"key":"10.1016\/bs.mie.2025.06.029_bib8","doi-asserted-by":"crossref","first-page":"2199","DOI":"10.1021\/bi035661y","article-title":"The role of Tyr41 and His155 in the functional properties of superoxide dismutase from the archaeon sulfolobus solfataricus","volume":"43","author":"Gogliettino","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/bs.mie.2025.06.029_bib9","doi-asserted-by":"crossref","first-page":"1654","DOI":"10.1016\/0006-291X(72)90799-1","article-title":"Magnetic circular dichroism of cobalt metalloenzyme derivatives","volume":"46","author":"Kaden","year":"1972","journal-title":"Biochemical and Biophysical Research Communications"},{"key":"10.1016\/bs.mie.2025.06.029_bib10","doi-asserted-by":"crossref","first-page":"11566","DOI":"10.1073\/pnas.0404387101","article-title":"De novo design of catalytic proteins","volume":"101","author":"Kaplan","year":"2004","journal-title":"Proceedings of the National Academy of Science of the United States of America"},{"key":"10.1016\/bs.mie.2025.06.029_bib11","doi-asserted-by":"crossref","first-page":"27458","DOI":"10.1016\/S0021-9258(19)74269-0","article-title":"Structural and functional importance of a conserved hydrogen bond network in human carbonic anhydrase II","volume":"268","author":"Krebs","year":"1993","journal-title":"Journal of Biological Chemistry"},{"key":"10.1016\/bs.mie.2025.06.029_bib12","doi-asserted-by":"crossref","DOI":"10.1016\/j.cbpa.2025.102586","article-title":"Recent advances in de novo designed metallopeptides as tailored enzyme mimics","volume":"86","author":"La Gatta","year":"2025","journal-title":"Current Opinion in Chemical Biology"},{"key":"10.1016\/bs.mie.2025.06.029_bib13","doi-asserted-by":"crossref","first-page":"4263","DOI":"10.1021\/bi00799a017","article-title":"Spectral properties of cobalt carboxypeptidase. Effects of substrates and inhibitors","volume":"10","author":"Latt","year":"1971","journal-title":"Biochemistry"},{"key":"10.1016\/bs.mie.2025.06.029_bib14","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1038\/nature11880","article-title":"Control of substrate access to the active site in methane monooxygenase","volume":"494","author":"Lee","year":"2013","journal-title":"Nature"},{"key":"10.1016\/bs.mie.2025.06.029_bib15","doi-asserted-by":"crossref","first-page":"1288","DOI":"10.1126\/science.8446897","article-title":"Crystal structure of a synthetic triple-stranded \u03b1-helical bundle","volume":"259","author":"Lovejoy","year":"1993","journal-title":"Science (New York, N. Y.)"},{"key":"10.1016\/bs.mie.2025.06.029_bib16","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.tibs.2016.10.007","article-title":"Coiled coils \u2013 a model system for the 21st century","volume":"42","author":"Lupas","year":"2017","journal-title":"Trends in Biochemical Sciences"},{"key":"10.1016\/bs.mie.2025.06.029_bib17","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1016\/j.jmb.2008.11.028","article-title":"A periodic table of coiled-coil protein structures","volume":"385","author":"Moutevelis","year":"2009","journal-title":"Journal of Molecular Biology"},{"key":"10.1016\/bs.mie.2025.06.029_bib18","doi-asserted-by":"crossref","first-page":"8177","DOI":"10.1002\/anie.201004429","article-title":"Probing a homoleptic PbS3 coordination environment in a designed peptide using 207Pb NMR spectroscopy: Implications for understanding the molecular basis of lead toxicity","volume":"49","author":"Neupane","year":"2010","journal-title":"Angewandte Chemie International Edition"},{"key":"10.1016\/bs.mie.2025.06.029_bib19","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1016\/0959-440X(95)80008-5","article-title":"Di-iron\u2014carboxylate proteins","volume":"5","author":"Nordlund","year":"1995","journal-title":"Current Opinion in Structural Biology"},{"key":"10.1016\/bs.mie.2025.06.029_bib20","doi-asserted-by":"crossref","first-page":"2411","DOI":"10.1002\/pro.5560041120","article-title":"How to measure and predict the molar absorption coefficient of a protein","volume":"4","author":"Pace","year":"1995","journal-title":"Protein Science"},{"key":"10.1016\/bs.mie.2025.06.029_bib21","doi-asserted-by":"crossref","first-page":"900","DOI":"10.1038\/nchem.1454","article-title":"Alteration of the oxygen-dependent reactivity of de novo Due Ferri proteins","volume":"4","author":"Reig","year":"2012","journal-title":"Nature Chemistry"},{"key":"10.1016\/bs.mie.2025.06.029_bib22","doi-asserted-by":"crossref","first-page":"11979","DOI":"10.1021\/jacs.6b07165","article-title":"A crystallographic examination of predisposition versus preorganization in de novo designed metalloproteins","volume":"138","author":"Ruckthong","year":"2016","journal-title":"Journal of the American Chemical Society"},{"key":"10.1016\/bs.mie.2025.06.029_bib23","doi-asserted-by":"crossref","first-page":"30600","DOI":"10.1074\/jbc.M400710200","article-title":"Crystal structure of the toluene\/o-xylene monooxygenase hydroxylase from pseudomonas stutzeri OX1","volume":"279","author":"Sazinsky","year":"2004","journal-title":"Journal of Biological Chemistry"},{"key":"10.1016\/bs.mie.2025.06.029_bib24","doi-asserted-by":"crossref","first-page":"5001","DOI":"10.1021\/ic050281h","article-title":"Corroborative models of the cobalt(II) inhibited Fe\/Mn superoxide dismutases","volume":"44","author":"Scarpellini","year":"2005","journal-title":"Inorganic Chemistry"},{"key":"10.1016\/bs.mie.2025.06.029_bib25","doi-asserted-by":"crossref","first-page":"R29","DOI":"10.1016\/S1359-0278(98)00011-X","article-title":"Analysis and design of three-stranded coiled coils and three-helix bundles","volume":"3","author":"Schneider","year":"1998","journal-title":"Folding and Design"},{"key":"10.1016\/bs.mie.2025.06.029_bib26","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.cbpa.2014.12.034","article-title":"Artificial metalloenzymes derived from three-helix bundles","volume":"25","author":"Tebo","year":"2015","journal-title":"Current Opinion in Chemical Biology"},{"key":"10.1016\/bs.mie.2025.06.029_bib27","doi-asserted-by":"crossref","first-page":"21234","DOI":"10.1073\/pnas.1212893110","article-title":"Designing a functional type 2 copper center that has nitrite reductase activity within \u03b1-helical coiled coils","volume":"109","author":"Tegoni","year":"2012","journal-title":"Proceedings of the National Academy of Science of the United States of America"},{"key":"10.1016\/bs.mie.2025.06.029_bib28","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1038\/s41557-020-0423-6","article-title":"Heteromeric three-stranded coiled coils designed using a Pb(II)(Cys)3 template mediated strategy","volume":"12","author":"Tolbert","year":"2020","journal-title":"Nature Chemistry"},{"key":"10.1016\/bs.mie.2025.06.029_bib29","doi-asserted-by":"crossref","first-page":"2930","DOI":"10.1021\/ja500215j","article-title":"Long-range electron tunneling","volume":"136","author":"Winkler","year":"2014","journal-title":"Journal of the American Chemical Society"},{"key":"10.1016\/bs.mie.2025.06.029_bib30","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1002\/prot.340150110","article-title":"Crystallographic analysis of Thr-200 \u2192 his human carbonic anhydrase II and its complex with the substrate, HCO","volume":"15","author":"Xue","year":"1993","journal-title":"Proteins: Structure, Function, and Bioinformatics"},{"key":"10.1016\/bs.mie.2025.06.029_bib31","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1038\/nchem.1201","article-title":"Hydrolytic catalysis and structural stabilization in a designed metalloprotein","volume":"4","author":"Zastrow","year":"2012","journal-title":"Nature Chemistry"}],"container-title":["Methods in Enzymology","Artificial Metalloproteins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S007668792500237X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S007668792500237X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T07:26:53Z","timestamp":1761636413000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S007668792500237X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025]]},"ISBN":["9780443415739"],"references-count":31,"URL":"https:\/\/doi.org\/10.1016\/bs.mie.2025.06.029","relation":{},"ISSN":["0076-6879"],"issn-type":[{"type":"print","value":"0076-6879"}],"subject":[],"published":{"date-parts":[[2025]]}}}