{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,31]],"date-time":"2026-03-31T23:42:40Z","timestamp":1775000560738,"version":"3.50.1"},"reference-count":37,"publisher":"Proceedings of the National Academy of Sciences","issue":"1","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2011,1,4]]},"abstract":"<jats:p>\n            The class II chelatases associated with heme, siroheme, and cobalamin biosynthesis are structurally related enzymes that insert a specific metal ion (Fe\n            <jats:sup>2+<\/jats:sup>\n            or Co\n            <jats:sup>2+<\/jats:sup>\n            ) into the center of a modified tetrapyrrole (protoporphyrin or sirohydrochlorin). The structures of two related class II enzymes, CbiX\n            <jats:sup>S<\/jats:sup>\n            from\n            <jats:italic>Archaeoglobus fulgidus<\/jats:italic>\n            and CbiK from\n            <jats:italic>Salmonella enterica<\/jats:italic>\n            , that are responsible for the insertion of cobalt along the cobalamin biosynthesis pathway are presented in complex with their metallated product. A further structure of a CbiK from\n            <jats:italic>Desulfovibrio vulgaris<\/jats:italic>\n            Hildenborough reveals how cobalt is bound at the active site. The crystal structures show that the binding of sirohydrochlorin is distinctly different to porphyrin binding in the protoporphyrin ferrochelatases and provide a molecular overview of the mechanism of chelation. The structures also give insights into the evolution of chelatase form and function. Finally, the structure of a periplasmic form of\n            <jats:italic>Desulfovibrio vulgaris<\/jats:italic>\n            Hildenborough CbiK reveals a novel tetrameric arrangement of its subunits that are stabilized by the presence of a heme\n            <jats:italic>b<\/jats:italic>\n            cofactor. Whereas retaining colbaltochelatase activity, this protein has acquired a central cavity with the potential to chaperone or transport metals across the periplasmic space, thereby evolving a new use for an ancient protein subunit.\n          <\/jats:p>","DOI":"10.1073\/pnas.1014298108","type":"journal-article","created":{"date-parts":[[2010,12,21]],"date-time":"2010-12-21T04:23:52Z","timestamp":1292905432000},"page":"97-102","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":45,"title":["Evolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerization"],"prefix":"10.1073","volume":"108","author":[{"given":"C\u00e9lia V.","family":"Rom\u00e3o","sequence":"first","affiliation":[{"name":"Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica, Universidade Nova de Lisboa, Avenida da Rep\u00fablica (EAN), 2780-157 Oeiras, Portugal;"}]},{"given":"Dimitrios","family":"Ladakis","sequence":"additional","affiliation":[{"name":"Centre for Molecular Processing, School of Biosciences, University of Kent, Giles Lane, Canterbury, Kent CT2 7NJ, United Kingdom; and"}]},{"given":"Susana A. L.","family":"Lobo","sequence":"additional","affiliation":[{"name":"Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica, Universidade Nova de Lisboa, Avenida da Rep\u00fablica (EAN), 2780-157 Oeiras, Portugal;"}]},{"given":"Maria A.","family":"Carrondo","sequence":"additional","affiliation":[{"name":"Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica, Universidade Nova de Lisboa, Avenida da Rep\u00fablica (EAN), 2780-157 Oeiras, Portugal;"}]},{"given":"Amanda A.","family":"Brindley","sequence":"additional","affiliation":[{"name":"Centre for Molecular Processing, School of Biosciences, University of Kent, Giles Lane, Canterbury, Kent CT2 7NJ, United Kingdom; and"}]},{"given":"Evelyne","family":"Deery","sequence":"additional","affiliation":[{"name":"Centre for Molecular Processing, School of Biosciences, University of Kent, Giles Lane, Canterbury, Kent CT2 7NJ, United Kingdom; and"}]},{"given":"Pedro M.","family":"Matias","sequence":"additional","affiliation":[{"name":"Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica, Universidade Nova de Lisboa, Avenida da Rep\u00fablica (EAN), 2780-157 Oeiras, Portugal;"}]},{"given":"Richard W.","family":"Pickersgill","sequence":"additional","affiliation":[{"name":"School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London E1 4NS, United Kingdom"}]},{"given":"L\u00edgia M.","family":"Saraiva","sequence":"additional","affiliation":[{"name":"Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica, Universidade Nova de Lisboa, Avenida da Rep\u00fablica (EAN), 2780-157 Oeiras, Portugal;"}]},{"given":"Martin J.","family":"Warren","sequence":"additional","affiliation":[{"name":"Centre for Molecular Processing, School of Biosciences, University of Kent, Giles Lane, Canterbury, Kent CT2 7NJ, United Kingdom; and"}]}],"member":"341","published-online":{"date-parts":[[2010,12,20]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.tibs.2006.01.001","article-title":"Chelatases: Distort to select?","volume":"31","author":"Al-Karadaghi S","year":"2006","unstructured":"S Al-Karadaghi, et al., Chelatases: Distort to select? 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Biochemistry 41, 13499\u201313506 (2002).","journal-title":"Biochemistry"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1021\/bi061760a","article-title":"Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX","volume":"46","author":"Hansson MD","year":"2007","unstructured":"MD Hansson, T Karlberg, MA Rahardja, S Al-Karadaghi, M Hansson, Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX. Biochemistry 46, 87\u201394 (2007).","journal-title":"Biochemistry"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"9821","DOI":"10.1021\/bi010012c","article-title":"Human ferrochelatase: Characterization of substrate-iron binding and proton-abstracting residues","volume":"40","author":"Sellers VM","year":"2001","unstructured":"VM Sellers, CK Wu, TA Dailey, HA Dailey, Human ferrochelatase: Characterization of substrate-iron binding and proton-abstracting residues. Biochemistry 40, 9821\u20139827 (2001).","journal-title":"Biochemistry"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1146\/annurev.biochem.74.082803.133029","article-title":"Protein families and their evolution-a structural perspective","volume":"74","author":"Orengo CA","year":"2005","unstructured":"CA Orengo, JM Thornton, Protein families and their evolution-a structural perspective. Annu Rev Biochem 74, 867\u2013900 (2005).","journal-title":"Annu Rev Biochem"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1093\/bioinformatics\/16.6.566","article-title":"DaliLite workbench for protein structure comparison","volume":"16","author":"Holm L","year":"2000","unstructured":"L Holm, J Park, DaliLite workbench for protein structure comparison. Bioinformatics 16, 566\u2013567 (2000).","journal-title":"Bioinformatics"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"1549","DOI":"10.1002\/chem.200400298","article-title":"Reaction mechanism of porphyrin metallation studied by theoretical methods","volume":"11","author":"Shen Y","year":"2005","unstructured":"Y Shen, U Ryde, Reaction mechanism of porphyrin metallation studied by theoretical methods. Chemistry 11, 1549\u20131564 (2005).","journal-title":"Chemistry"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"1006","DOI":"10.1016\/j.jmb.2007.08.040","article-title":"A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase","volume":"373","author":"Medlock AE","year":"2007","unstructured":"AE Medlock, TA Dailey, TA Ross, HA Dailey, WN Lanzilotta, A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase. J Mol Biol 373, 1006\u20131016 (2007).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1107\/S0021889800014655","article-title":"CHOOCH: A program for deriving anomalous-scattering factors from X-ray fluorescence spectra","volume":"34","author":"Evans G","year":"2001","unstructured":"G Evans, RF Pettifer, CHOOCH: A program for deriving anomalous-scattering factors from X-ray fluorescence spectra. 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Methods Enzymol 277, 620\u2013633 (1997).","journal-title":"Methods Enzymol"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1524\/zkri.217.12.644.20662","article-title":"Macromolecular phasing with SHELXE","volume":"217","author":"Sheldrick GM","year":"2002","unstructured":"GM Sheldrick, Macromolecular phasing with SHELXE. Z Kristallogr 217, 644\u2013650 (2002).","journal-title":"Z Kristallogr"},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1038\/8263","article-title":"Automated protein model building combined with iterative structure refinement","volume":"6","author":"Perrakis A","year":"1999","unstructured":"A Perrakis, R Morris, VS Lamzin, Automated protein model building combined with iterative structure refinement. Nat Struct Biol 6, 458\u2013463 (1999).","journal-title":"Nat Struct Biol"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1107\/S0907444905001617","article-title":"Likelihood-enhanced fast translation functions","volume":"61","author":"McCoy AJ","year":"2005","unstructured":"AJ McCoy, RW Grosse-Kunstleve, LC Storoni, RJ Read, Likelihood-enhanced fast translation functions. Acta Crystallogr D 61, 458\u2013464 (2005).","journal-title":"Acta Crystallogr D"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","first-page":"1022","DOI":"10.1107\/S0021889897006766","article-title":"MOLREP: An automated program for molecular replacement","volume":"30","author":"Vagin A","year":"1997","unstructured":"A Vagin, A Teplyakov, MOLREP: An automated program for molecular replacement. 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