{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,4]],"date-time":"2026-11-04T16:26:11Z","timestamp":1793809571024,"version":"4.6.1"},"publisher-location":"New York, NY","reference-count":36,"publisher":"Springer US","isbn-type":[{"value":"9781071651575","type":"print"},{"value":"9781071651582","type":"electronic"}],"license":[{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026]]},"DOI":"10.1007\/978-1-0716-5158-2_6","type":"book-chapter","created":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T22:58:40Z","timestamp":1788303520000},"page":"67-80","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Replacing\u00a0of Cysteine with Selenocysteine: Biochemical Considerations, Computational Modeling, and Protein Engineering Applications"],"prefix":"10.1007","author":[{"given":"Wick","family":"Lakshantha","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,7,2]]},"reference":[{"key":"6_CR1","doi-asserted-by":"publisher","first-page":"109421","DOI":"10.1016\/j.abb.2022.109421","volume":"726","author":"CZ Chung","year":"2022","unstructured":"Chung CZ, Krahn N (2022) The selenocysteine toolbox: a guide to studying the 21st amino acid. Arch Biochem Biophys 726:109421. https:\/\/doi.org\/10.1016\/j.abb.2022.109421","journal-title":"Arch Biochem Biophys"},{"issue":"12","key":"6_CR2","doi-asserted-by":"publisher","first-page":"10109","DOI":"10.3390\/ijms241210109","volume":"24","author":"J Chaudiere","year":"2023","unstructured":"Chaudiere J (2023) Biological and catalytic properties of selenoproteins. Int J Mol Sci 24(12):10109. https:\/\/doi.org\/10.3390\/ijms241210109","journal-title":"Int J Mol Sci"},{"issue":"14","key":"6_CR3","doi-asserted-by":"publisher","first-page":"7136","DOI":"10.1093\/nar\/gkv558","volume":"43","author":"SB Kotini","year":"2015","unstructured":"Kotini SB, Peske F, Rodnina MV (2015) Partitioning between recoding and termination at a stop codon\u2013selenocysteine insertion sequence. Nucleic Acids Res 43(14):7136\u20137148. https:\/\/doi.org\/10.1093\/nar\/gkv558","journal-title":"Nucleic Acids Res"},{"issue":"49","key":"6_CR4","doi-asserted-by":"publisher","first-page":"14441","DOI":"10.1002\/anie.201207567","volume":"52","author":"C Aldag","year":"2013","unstructured":"Aldag C, Br\u00f6cker MJ, Hohn MJ, Prat L, Hammond G, Plummer A, S\u00f6ll D (2013) Rewiring translation for elongation factor Tu-dependent selenocysteine incorporation. Angew Chem Int Ed Engl 52(49):14441\u201314444. https:\/\/doi.org\/10.1002\/anie.201207567","journal-title":"Angew Chem Int Ed Engl"},{"issue":"15","key":"6_CR5","doi-asserted-by":"publisher","first-page":"3312","DOI":"10.1093\/bioinformatics\/bti507","volume":"21","author":"A Busch","year":"2005","unstructured":"Busch A, Will S, Backofen R (2005) SECISDesign: a server to design SECIS elements within the coding sequence. Bioinformatics 21(15):3312\u20133313. https:\/\/doi.org\/10.1093\/bioinformatics\/bti507","journal-title":"Bioinformatics"},{"key":"6_CR6","first-page":"3","volume-title":"Recoding: expansion of decoding rules enriches gene expression","author":"VN Gladyshev","year":"2009","unstructured":"Gladyshev VN, Hatfield DL (2009) Selenocysteine biosynthesis, selenoproteins, and selenoproteomes. In: Atkins JF, Gesteland RF (eds) Recoding: expansion of decoding rules enriches gene expression. Springer, New York, pp 3\u201327. https:\/\/doi.org\/10.1007\/978-0-387-89382-2_1editors"},{"key":"6_CR7","volume-title":"Dissecting the role of selenothiol- versus thiol-based catalysis using the model enzyme glutathione peroxidase 4 (GPx4). Dissertation","author":"AM Mannes","year":"2019","unstructured":"Mannes AM (2019) Dissecting the role of selenothiol- versus thiol-based catalysis using the model enzyme glutathione peroxidase 4 (GPx4). Dissertation, Ludwig Maximilian University of Munich"},{"key":"6_CR8","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1007\/978-94-007-5787-5_7","volume-title":"Oxidative stress and redox regulation","author":"SM Marino","year":"2013","unstructured":"Marino SM, Roos G, Gladyshev VN (2013) Computational redox biology: methods and applications. In: Jacob C, Winyard PG (eds) Oxidative stress and redox regulation. Springer, Dordrecht, pp 187\u2013211. https:\/\/doi.org\/10.1007\/978-94-007-5787-5_7editors."},{"issue":"7","key":"6_CR9","doi-asserted-by":"publisher","first-page":"881","DOI":"10.1089\/ars.2009.2878","volume":"12","author":"J Donovan","year":"2010","unstructured":"Donovan J, Copeland PR (2010) Threading the needle: getting selenocysteine into proteins. Antioxid Redox Signal 12(7):881\u2013892. https:\/\/doi.org\/10.1089\/ars.2009.2878","journal-title":"Antioxid Redox Signal"},{"issue":"17","key":"6_CR10","doi-asserted-by":"publisher","first-page":"3096","DOI":"10.1039\/b505299h","volume":"3","author":"PP Phadnis","year":"2005","unstructured":"Phadnis PP, Mugesh G (2005) Internally stabilised selenocysteine derivatives: syntheses, 77Se NMR and biomimetic studies. Org Biomol Chem 3(17):3096\u20133102. https:\/\/doi.org\/10.1039\/b505299h","journal-title":"Org Biomol Chem"},{"issue":"1","key":"6_CR11","doi-asserted-by":"publisher","first-page":"164","DOI":"10.1016\/0003-9861(67)90222-2","volume":"122","author":"RE Huber","year":"1967","unstructured":"Huber RE, Criddle RS (1967) Comparison of the chemical properties of selenocysteine and selenocystine with their sulfur analogs. Arch Biochem Biophys 122(1):164\u2013173. https:\/\/doi.org\/10.1016\/0003-9861(67)90222-2","journal-title":"Arch Biochem Biophys"},{"issue":"18","key":"6_CR12","doi-asserted-by":"publisher","first-page":"9028","DOI":"10.1093\/nar\/gkv833","volume":"43","author":"Y Itoh","year":"2015","unstructured":"Itoh Y, Sekine S, Yokoyama S (2015) Crystal structure of the full-length bacterial selenocysteine-specific elongation factor SelB. Nucleic Acids Res 43(18):9028\u20139038. https:\/\/doi.org\/10.1093\/nar\/gkv833","journal-title":"Nucleic Acids Res"},{"issue":"5","key":"6_CR13","doi-asserted-by":"publisher","first-page":"1456","DOI":"10.1016\/j.jmb.2008.08.042","volume":"385","author":"Y Itoh","year":"2009","unstructured":"Itoh Y, Sekine SI, Matsumoto E, Akasaka R, Takemoto C, Shirouzu M, Yokoyama S (2009) Structure of selenophosphate synthetase essential for selenium incorporation into proteins and RNAs. J Mol Biol 385(5):1456\u20131469. https:\/\/doi.org\/10.1016\/j.jmb.2008.08.042","journal-title":"J Mol Biol"},{"issue":"19","key":"6_CR14","doi-asserted-by":"publisher","first-page":"6259","DOI":"10.1093\/nar\/gkp648","volume":"37","author":"Y Itoh","year":"2009","unstructured":"Itoh Y, Chiba S, Sekine SI, Yokoyama S (2009) Crystal structure of human selenocysteine tRNA. Nucleic Acids Res 37(19):6259\u20136268. https:\/\/doi.org\/10.1093\/nar\/gkp648","journal-title":"Nucleic Acids Res"},{"issue":"35","key":"6_CR15","doi-asserted-by":"publisher","first-page":"8513","DOI":"10.1002\/chem.201900892","volume":"25","author":"O Weil-Ktorza","year":"2019","unstructured":"Weil-Ktorza O, Rege N, Lansky S, Shalev D, Shoham G, Weiss M, Metanis N (2019) Substitution of an internal disulfide bridge with a diselenide enhances both foldability and stability of human insulin. Chem Eur J 25(35):8513\u20138521. https:\/\/doi.org\/10.1002\/chem.201900892","journal-title":"Chem Eur J"},{"key":"6_CR16","doi-asserted-by":"publisher","first-page":"30","DOI":"10.1038\/s42004-021-00463-9","volume":"4","author":"R Mousa","year":"2021","unstructured":"Mousa R, Hidmi T, Pomyalov S, Lansky S, Khouri L, Shalev DE, Shoham G, Metanis N (2021) Diselenide crosslinks for enhanced and simplified oxidative protein folding. Commun Chem 4:30. https:\/\/doi.org\/10.1038\/s42004-021-00463-9","journal-title":"Commun Chem"},{"issue":"1","key":"6_CR17","doi-asserted-by":"publisher","first-page":"322","DOI":"10.1039\/C4SC02379J","volume":"6","author":"N Metanis","year":"2015","unstructured":"Metanis N, Hilvert D (2015) Harnessing selenocysteine reactivity for oxidative protein folding. Chem Sci 6(1):322\u2013325. https:\/\/doi.org\/10.1039\/C4SC02379J","journal-title":"Chem Sci"},{"key":"6_CR18","doi-asserted-by":"publisher","first-page":"258","DOI":"10.1038\/s42004-023-01056-4","volume":"6","author":"K Arai","year":"2023","unstructured":"Arai K, Okumura M, Lee YH, Katayama H, Mizutani K, Lin Y, Park SY, Sawada K, Toyoda M, Hojo H, Inaba K (2023) Diselenide-bond replacement of the external disulfide bond of insulin increases its oligomerisation, leading to sustained activity. Commun Chem 6:258. https:\/\/doi.org\/10.1038\/s42004-023-01056-4","journal-title":"Commun Chem"},{"issue":"3","key":"6_CR19","doi-asserted-by":"publisher","first-page":"14","DOI":"10.11299\/metallomicsresearch.MR202407","volume":"4","author":"Y He","year":"2024","unstructured":"He Y, Hojo H (2024) Chemical synthesis and diselenide metathesis in selenocysteine-containing peptides. Met Res 4(3):14\u201328. https:\/\/doi.org\/10.11299\/metallomicsresearch.MR202407 rev","journal-title":"Met Res"},{"issue":"29","key":"6_CR20","doi-asserted-by":"publisher","first-page":"9727","DOI":"10.1021\/jp0614998","volume":"110","author":"R Spezia","year":"2006","unstructured":"Spezia R, Tournois G, Cartailler T, Tortajada J, Jeanvoine Y (2006) Co\u00b2\u207a binding cysteine and selenocysteine: a DFT study. J Phys Chem A 110(29):9727\u20139735. https:\/\/doi.org\/10.1021\/jp0614998","journal-title":"J Phys Chem A"},{"key":"6_CR21","doi-asserted-by":"publisher","first-page":"100035","DOI":"10.1016\/j.rbc.2024.100035","volume":"9","author":"A Messias","year":"2024","unstructured":"Messias A, Rauber A, Vuletich S, Zeida A, Semelak JA, Estrin DA (2024) Comparing thiol and selenol reactivity towards peroxynitrite by computer simulation. Redox Biochem Chem 9:100035. https:\/\/doi.org\/10.1016\/j.rbc.2024.100035","journal-title":"Redox Biochem Chem"},{"key":"6_CR22","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1007\/978-3-319-41283-2_7","volume-title":"Selenium: its molecular biology and role in human health","author":"RN Dardashti","year":"2016","unstructured":"Dardashti RN, Dery L, Mousa R, Dery S, Reddy PS, Metanis N (2016) The chemistry of selenocysteine in proteins. In: Hatfield DL, Schweizer U, Tsuji PA, Gladyshev VN (eds) Selenium: its molecular biology and role in human health, 3rd ed. Springer, Cham, pp 73\u201383. https:\/\/doi.org\/10.1007\/978-3-319-41283-2_7","edition":"3rd ed"},{"key":"6_CR23","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1016\/j.jinorgbio.2011.11.005","volume":"108","author":"F Saccoccia","year":"2012","unstructured":"Saccoccia F, Angelucci F, Boumis G, Brunori M, Miele AE, Williams DL, Bellelli A (2012) On the mechanism and rate of gold incorporation into thiol-dependent flavoreductases. J Inorg Biochem 108:105\u2013111. https:\/\/doi.org\/10.1016\/j.jinorgbio.2011.11.005","journal-title":"J Inorg Biochem"},{"issue":"1","key":"6_CR24","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1002\/wcms.81","volume":"2","author":"F Neese","year":"2012","unstructured":"Neese F (2012) The ORCA program system. Wiley Interdiscip Rev Comput Mol Sci 2(1):73\u201378. https:\/\/doi.org\/10.1002\/wcms.81","journal-title":"Wiley Interdiscip Rev Comput Mol Sci"},{"issue":"18","key":"6_CR25","doi-asserted-by":"publisher","first-page":"3297","DOI":"10.1039\/b508541a","volume":"7","author":"F Weigend","year":"2005","unstructured":"Weigend F, Ahlrichs R (2005) Balanced basis sets of split valence, triple zeta valence and quadruple zeta valence quality for H to Rn: design and assessment of accuracy. Phys Chem Chem Phys 7(18):3297\u20133305. https:\/\/doi.org\/10.1039\/b508541a","journal-title":"Phys Chem Chem Phys"},{"issue":"5","key":"6_CR26","doi-asserted-by":"publisher","first-page":"799","DOI":"10.1039\/p29930000799","volume":"2","author":"A Klamt","year":"1993","unstructured":"Klamt A, Sch\u00fc\u00fcrmann G (1993) COSMO: a new approach to dielectric screening in solvents with explicit expressions for the screening energy and its gradient. J Chem Soc Perkin Trans 2(5):799\u2013805. https:\/\/doi.org\/10.1039\/p29930000799","journal-title":"J Chem Soc Perkin Trans"},{"issue":"6","key":"6_CR27","doi-asserted-by":"publisher","first-page":"4597","DOI":"10.1063\/1.466059","volume":"99","author":"E van Lenthe","year":"1993","unstructured":"van Lenthe E, Baerends EJ, Snijders JG (1993) Relativistic regular two-component Hamiltonians. J Chem Phys 99(6):4597\u20134610. https:\/\/doi.org\/10.1063\/1.466059","journal-title":"J Chem Phys"},{"issue":"6","key":"6_CR28","doi-asserted-by":"publisher","first-page":"908","DOI":"10.1021\/ct800047t","volume":"4","author":"DA Pantazis","year":"2008","unstructured":"Pantazis DA, Chen XY, Landis CR, Neese F (2008) All-electron scalar relativistic basis sets for third-row transition metal atoms. J Chem Theory Comput 4(6):908\u2013919. https:\/\/doi.org\/10.1021\/ct800047t","journal-title":"J Chem Theory Comput"},{"issue":"23","key":"6_CR29","doi-asserted-by":"publisher","first-page":"8251","DOI":"10.1021\/ja00179a005","volume":"112","author":"K Wolinski","year":"1990","unstructured":"Wolinski K, Hinton JF, Pulay P (1990) Efficient implementation of the gauge-independent atomic orbital method for NMR chemical shift calculations. J Am Chem Soc 112(23):8251\u20138260. https:\/\/doi.org\/10.1021\/ja00179a005","journal-title":"J Am Chem Soc"},{"issue":"31","key":"6_CR30","doi-asserted-by":"publisher","first-page":"7314","DOI":"10.1021\/ja010509j","volume":"123","author":"MD Liptak","year":"2001","unstructured":"Liptak MD, Shields GC (2001) Accurate pKa calculations for carboxylic acids using complete basis set and Gaussian-n models combined with CPCM continuum solvation methods. J Am Chem Soc 123(31):7314\u20137319. https:\/\/doi.org\/10.1021\/ja010509j","journal-title":"J Am Chem Soc"},{"issue":"1","key":"6_CR31","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1071\/CH09320","volume":"63","author":"J Ho","year":"2010","unstructured":"Ho J, Coote ML (2010) pKa calculation of small molecules: a review of recent approaches. Aust J Chem 63(1):1\u201313. https:\/\/doi.org\/10.1071\/CH09320","journal-title":"Aust J Chem"},{"issue":"32","key":"6_CR32","doi-asserted-by":"publisher","first-page":"16066","DOI":"10.1021\/jp063552y","volume":"110","author":"CP Kelly","year":"2006","unstructured":"Kelly CP, Cramer CJ, Truhlar DG (2006) Aqueous solvation free energies of ions and ion\u2013water clusters based on an accurate value for the absolute aqueous solvation free energy of the proton. J Phys Chem B 110(32):16066\u201316081. https:\/\/doi.org\/10.1021\/jp063552y","journal-title":"J Phys Chem B"},{"issue":"20","key":"6_CR33","doi-asserted-by":"publisher","first-page":"11727","DOI":"10.1039\/d1cp01126a","volume":"23","author":"M Busch","year":"2021","unstructured":"Busch M, Ahlberg E, Laasonen K (2021) From absolute potentials to a generalised computational standard hydrogen electrode for aqueous and non-aqueous solvents. Phys Chem Chem Phys 23(20):11727\u201311737. https:\/\/doi.org\/10.1039\/d1cp01126a","journal-title":"Phys Chem Chem Phys"},{"issue":"3","key":"6_CR34","doi-asserted-by":"publisher","first-page":"239","DOI":"10.1016\/0301-4622(92)87031-8","volume":"43","author":"RA Alberty","year":"1992","unstructured":"Alberty RA (1992) Calculation of transformed thermodynamic properties of biochemical reactants at specified pH and pMg. Biophys Chem 43(3):239\u2013254. https:\/\/doi.org\/10.1016\/0301-4622(92)87031-8","journal-title":"Biophys Chem"},{"issue":"18","key":"6_CR35","doi-asserted-by":"publisher","first-page":"6378","DOI":"10.1021\/jp810292n","volume":"113","author":"AV Marenich","year":"2009","unstructured":"Marenich AV, Cramer CJ, Truhlar DG (2009) Universal solvation model based on solute electron density and on a continuum model of the solvent defined by the bulk dielectric constant and atomic surface tensions. J Phys Chem B 113(18):6378\u20136396. https:\/\/doi.org\/10.1021\/jp810292n","journal-title":"J Phys Chem B"},{"issue":"8","key":"6_CR36","doi-asserted-by":"publisher","first-page":"2161","DOI":"10.1021\/cr960149m","volume":"99","author":"CJ Cramer","year":"1999","unstructured":"Cramer CJ, Truhlar DG (1999) Implicit solvation models: equilibria, structure, spectra, and dynamics. Chem Rev 99(8):2161\u20132200. https:\/\/doi.org\/10.1021\/cr960149m","journal-title":"Chem Rev"}],"container-title":["Methods in Molecular Biology","Functional Disulphide Bonds"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/978-1-0716-5158-2_6","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,11,4]],"date-time":"2026-11-04T15:49:46Z","timestamp":1793807386000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/chapter\/10.1007\/978-1-0716-5158-2_6"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026]]},"ISBN":["9781071651575","9781071651582"],"references-count":36,"URL":"https:\/\/doi.org\/10.1007\/978-1-0716-5158-2_6","relation":{},"ISSN":["1064-3745","1940-6029"],"issn-type":[{"value":"1064-3745","type":"print"},{"value":"1940-6029","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026]]},"assertion":[{"value":"2 July 2026","order":1,"name":"first_online","label":"First Online","group":{"name":"ChapterHistory","label":"Chapter History"}}]}}