CoChat
Sign Up
Cited by 52Enzyme Catalysis and ImmobilizationClick Chemistry and ApplicationsMetal-Catalyzed Oxygenation Mechanisms

The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.

Chemical modifications of proteins and their applications in metalloenzyme studies

Open access
Naowarojna, Nathchar, Cheng, Ronghai, Lopez, Juan, Wong, Christina, Qiao, Lu, Liu, Pinghua·2021·Synthetic and Systems Biotechnology
DOI 10.1016/j.synbio.2021.01.001PMC PMC7897936
Open this paper in CoChat — free account

Abstract

Protein chemical modifications are important tools for elucidating chemical and biological functions of proteins. Several strategies have been developed to implement these modifications, including enzymatic tailoring reactions, unnatural amino acid incorporation using the expanded genetic codes, and recognition-driven transformations. These technologies have been applied in metalloenzyme studies, specifically in dissecting their mechanisms, improving their enzymatic activities, and creating artificial enzymes with non-natural activities. Herein, we summarize some of the recent efforts in these areas with an emphasis on a few metalloenzyme case studies.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.synbio.2021.01.001

Cites

6 of 6 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Proteomics does not fully capture protein modifications that significantly impact protein structure and function.

    “proteomics does not fully capture protein modifications that significantly impact protein structure and function [Zhong et al., 2023; Naowarojna et al., 2021].”

    From Cell signaling pathways discovery from multi-modal data (2025) · cites this paper as Naowarojna et al., 2021

    The Abstract says post-translational modifications diversify protein functions, and the section on protein modifications using ncAAs says some modifications may alter protein folding. Neither passage says that proteomics fails to fully capture these modifications; searches for that limitation found no supporting passage. Page numbers were not available in our copy. (LLM, conf=0.82)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 145

  1. Sakamoto, 2018, Recent progress in chemical modification of proteins, Anal Sci, 35, 10.2116/analsci.18R003 · DOI
  2. Shadish, 2020, Site-selective protein modification: from functionalized proteins to functional biomaterials, Matter, 2, 50, 10.1016/j.matt.2019.11.011 · DOI
  3. Nischan, 2014, Site-specific PEGylation of proteins: recent developments, J Org Chem, 79, 10727, 10.1021/jo502136n · DOI
  4. Wurm, 2013, One-pot squaric acid diester mediated aqueous protein conjugation, Chem Commun, 49, 7815, 10.1039/c3cc44039g · DOI
  5. Spicer, 2014, Selective chemical protein modification, Nat Commun, 5, 4740, 10.1038/ncomms5740 · DOI
  6. Matos, 2018, Chemo- and regioselective lysine modification on native proteins, J Am Chem Soc, 140, 4004, 10.1021/jacs.7b12874 · DOI
  7. Nanna, 2017, Harnessing a catalytic lysine residue for the one-step preparation of homogeneous antibody-drug conjugates, Nat Commun, 8, 1112, 10.1038/s41467-017-01257-1 · DOI
  8. Dawson, 1994, Synthesis of proteins by native chemical ligation, Science, 266, 776, 10.1126/science.7973629 · DOI
  9. Muir, 2003, Semisynthesis of proteins by expressed protein ligation, Annu Rev Biochem, 72, 249, 10.1146/annurev.biochem.72.121801.161900 · DOI
  10. Vila-Perelló, 2013, Streamlined expressed protein ligation using split inteins, J Am Chem Soc, 135, 286, 10.1021/ja309126m · DOI
  11. Minnihan, 2009, Unnatural amino acids: better than the real things?, F1000 Biol Rep, 1, 88, 10.3410/B1-88 · DOI
  12. David, 2015, Chemical tagging and customizing of cellular chromatin states using ultrafast trans-splicing inteins, Nat Chem, 7, 394, 10.1038/nchem.2224 · DOI
  13. Gilmore, 2006, N-terminal protein modification through a biomimetic transamination reaction, Angew Chem Int, 45, 5307, 10.1002/anie.200600368 · DOI
  14. Scheck, 2007, Regioselective labeling of antibodies through N-terminal transamination, ACS Synth Biol, 2, 247
  15. Scheck, 2008, Optimization of a biomimetic transamination reaction, J Am Chem Soc, 130, 11762, 10.1021/ja802495w · DOI
  16. Christman, 2007, Site-specific protein immobilization through N-terminal oxime linkages, J Mater Chem, 17, 2021, 10.1039/b618002g · DOI
  17. Jie, 2017, Development and applications of bioorthogonal cleavage reactions, Hua Hsueh Hsueh Pao, 75, 1173
  18. Chalker, 2011, “tag-and-modify” approach to site-selective protein modification, Acc Chem Res, 44, 730, 10.1021/ar200056q · DOI
  19. Crankshaw, 1996, Modification of cysteine, Curr Protein Pept Sci, 3, 15
  20. Goddard, 1935, Derivatives of keratin, J Biol Chem, 112, 361, 10.1016/S0021-9258(18)74993-4 · DOI
  21. Lundell, 1999, Sample preparation for peptide mapping-a pharmaceutical quality-control perspective, Anal Biochem, 266, 31, 10.1006/abio.1998.2919 · DOI
  22. Moore, 1956, Cross-linking of bovine plasma albumin and wool keratin, J Am Chem Soc, 78, 2414, 10.1021/ja01592a020 · DOI
  23. Tsao, 1953, The extraction, purification and some chemical properties of actin, Biochim Biophys Acta, 11, 102, 10.1016/0006-3002(53)90013-4 · DOI
  24. Gamblin, 2003, Glycosyl phenylthiosulfonates (Glyco-PTS): novel reagents for glycoprotein synthesis, Org Biomol Chem, 1, 3642, 10.1039/b306990g · DOI
  25. Bernardes, 2008, From disulfide-to thioether-linked glycoproteins, Angew Chem Int, 120, 2276, 10.1002/ange.200704381 · DOI
  26. Fontaine, 2015, Long-term stabilization of maleimide–thiol conjugates, Bioconjugate Chem, 26, 145, 10.1021/bc5005262 · DOI
  27. Lyon, 2014, Self-hydrolyzing maleimides improve the stability and pharmacological properties of antibody-drug conjugates, Nat Biotechnol, 32, 1059, 10.1038/nbt.2968 · DOI
  28. Shiu, 2014, Phosphorescent proteins for bio-imaging and site selective bio-conjugation of peptides and proteins with luminescent cyclometalated iridium (III) complexes, Chem Commun, 50, 4375, 10.1039/c3cc48376b · DOI
  29. Koniev, 2014, Selective irreversible chemical tagging of cysteine with 3-arylpropiolonitriles, Bioconjugate Chem, 25, 202, 10.1021/bc400469d · DOI
  30. Kolodych, 2015, CBTF: new amine-to-thiol coupling reagent for preparation of antibody conjugates with increased plasma stability, Bioconjugate Chem, 26, 197, 10.1021/bc500610g · DOI
  31. Conte, 2011, Multi-molecule reaction of serum albumin can occur through thiol-yne coupling, Chem Commun, 47, 11086, 10.1039/c1cc14402b · DOI
  32. Bernardim, 2016, Stoichiometric and irreversible cysteine-selective protein modification using carbonylacrylic reagents, Nat Commun, 7, 1, 10.1038/ncomms13128 · DOI
  33. Bernardim, 2019, Efficient and irreversible antibody–cysteine bioconjugation using carbonylacrylic reagents, Nat Protoc, 14, 86, 10.1038/s41596-018-0083-9 · DOI
  34. Gil de Montes, 2020, Stable pyrrole-linked bioconjugates through tetrazine-triggered azanorbornadiene fragmentation, Angew Chem Int, 132, 6255, 10.1002/ange.201914529 · DOI
  35. Bernardim, 2020, Precise installation of diazo-tagged side-chains on proteins to enable in vitro and in-cell site-specific labeling, Bioconjugate Chem, 31, 1604, 10.1021/acs.bioconjchem.0c00232 · DOI
  36. Kuan, 2016, Site-selective disulfide modification of proteins: expanding diversity beyond the proteome, Chem Eur J, 22, 17112, 10.1002/chem.201602298 · DOI
  37. Forte, 2018, Homogeneous antibody-drug conjugates via site-selective disulfide bridging, Drug Discov Today Technol, 30, 11, 10.1016/j.ddtec.2018.09.004 · DOI
  38. Martínez-Sáez, 2017, Oxetane grafts installed site-selectively on native disulfides to enhance protein stability and activity in vivo, Angew Chem Int, 56, 14963, 10.1002/anie.201708847 · DOI
  39. Lee, 2016, Next-generation disulfide stapling: reduction and functional re-bridging all in one, Chem Sci, 7, 799, 10.1039/C5SC02666K · DOI
  40. Jones, 2012, Direct peptide bioconjugation/PEGylation at tyrosine with linear and branched polymeric diazonium salts, J Am Chem Soc, 134, 7406, 10.1021/ja211855q · DOI
  41. Chen, 2009, New approach for local structure analysis of the tyrosine domain in proteins by using a site-specific and polarity-sensitive fluorescent probe, Chembiochem, 10, 1200, 10.1002/cbic.200900003 · DOI
  42. Seim, 2011, Oxidative modification of native protein residues using cerium (IV) ammonium nitrate, J Am Chem Soc, 133, 16970, 10.1021/ja206324q · DOI
  43. Tilley, 2006, Tyrosine-selective protein alkylation using π-allylpalladium complexes, J Am Chem Soc, 128, 1080, 10.1021/ja057106k · DOI
  44. Ruan, 2017, Manganese-catalyzed C-H alkynylation: expedient peptide synthesis and modification, Angew Chem Int, 56, 3172, 10.1002/anie.201611118 · DOI
  45. Schischko, 2017, Bioorthogonal diversification of peptides through selective ruthenium (II)-catalyzed C–H activation, Angew Chem Int, 56, 1576, 10.1002/anie.201609631 · DOI
  46. Siti, 2015, Photo-induced conjugation of tetrazoles to modified and native proteins, Org Biomol Chem, 13, 3202, 10.1039/C4OB02025A · DOI
  47. Seki, 2016, Transition metal-free tryptophan-selective bioconjugation of proteins, J Am Chem Soc, 138, 10798, 10.1021/jacs.6b06692 · DOI
  48. deGruyter, 2017, Malins LR, Baran PS. Residue-specific peptide modification: a chemist's guide, Biochemistry, 56, 3863, 10.1021/acs.biochem.7b00536 · DOI
  49. Hoyt, 2019, Contemporary approaches to site-selective protein modification, Nat Rev Chem., 3, 147, 10.1038/s41570-019-0079-1 · DOI
  50. Conibear, 2020, Deciphering protein post-translational modifications using chemical biology tools, Nat Rev Chem, 1
  51. Drienovská, 2017, Design of an enantioselective artificial metallo-hydratase enzyme containing an unnatural metal-binding amino acid, Chem Sci, 8, 7228, 10.1039/C7SC03477F · DOI
  52. Drienovská, 2020, Expanding the enzyme universe with genetically encoded unnatural amino acids, Nat Catal, 1
  53. Won, 2019, Recent advances in enzyme engineering through incorporation of unnatural amino acids, Biotechnol Bioproc Eng, 24, 1, 10.1007/s12257-019-0163-x · DOI
  54. Srinivasan, 2002, Pyrrolysine encoded by UAG in Archaea: charging of a UAG-decoding specialized tRNA, Science, 296, 1459, 10.1126/science.1069588 · DOI
  55. Böck, 1991, Selenocysteine: the 21st amino acid, Mol Microbiol, 5, 515, 10.1111/j.1365-2958.1991.tb00722.x · DOI
  56. Munier, 1959, Incorporation of structural analogues of amino acids into bacterial proteins during their synthesis in vivo, Biochim Biophys Acta, 31, 378, 10.1016/0006-3002(59)90011-3 · DOI
  57. Yang, 1990, Structure of ribonuclease H phased at 2 Å resolution by MAD analysis of the selenomethionyl protein, Science, 249, 1398, 10.1126/science.2169648 · DOI · Paper page
  58. Chin, 2017, Expanding and reprogramming the genetic code, Nature, 550, 53, 10.1038/nature24031 · DOI
  59. Lajoie, 2013, Genomically recoded organisms expand biological functions, Science, 342, 357, 10.1126/science.1241459 · DOI
  60. Mukai, 2015, Highly reproductive Escherichia coli cells with no specific assignment to the UAG codon, Sci Rep, 5, 1, 10.1038/srep09699 · DOI
  61. Dumas, 2015, Designing logical codon reassignment-Expanding the chemistry in biology, Chem Sci, 6, 50, 10.1039/C4SC01534G · DOI
  62. Bryson, 2017, Continuous directed evolution of aminoacyl-tRNA synthetases, Nat Chem Biol, 13, 1253, 10.1038/nchembio.2474 · DOI
  63. Italia, 2017, An orthogonalized platform for genetic code expansion in both bacteria and eukaryotes, Nat Chem Biol, 13, 446, 10.1038/nchembio.2312 · DOI
  64. Italia, 2019, Mutually orthogonal nonsense-suppression systems and conjugation chemistries for precise protein labeling at up to three distinct sites, J Am Chem Soc, 141, 6204, 10.1021/jacs.8b12954 · DOI
  65. Rackham, 2005, A network of orthogonal ribosome· mRNA pairs, Nat Chem Biol, 1, 159, 10.1038/nchembio719 · DOI
  66. Hui, 1987, Specialized ribosome system: preferential translation of a single mRNA species by a subpopulation of mutated ribosomes in Escherichia coli, Proc Natl Acad Sci Unit States Am, 84, 4762, 10.1073/pnas.84.14.4762 · DOI
  67. Schmied, 2018, Controlling orthogonal ribosome subunit interactions enables evolution of new function, Nature, 564, 444, 10.1038/s41586-018-0773-z · DOI
  68. Riddle, 1973, Frameshift suppression: a nucleotide addition in the anticodon of a glycine transfer RNA, Nat New Biol, 242, 230, 10.1038/newbio242230a0 · DOI
  69. Fischer, 2020, New codons for efficient production of unnatural proteins in a semisynthetic organism, Nat Chem Biol, 1
  70. Lang, 2014, Cellular incorporation of unnatural amino acids and bioorthogonal labeling of proteins, Chem Rev, 114, 4764, 10.1021/cr400355w · DOI
  71. Rostovtsev, 2002, A stepwise Huisgen cycloaddition process: copper (I)-catalyzed regioselective “ligation” of azides and terminal alkynes, Angew Chem Int, 41, 2596, 10.1002/1521-3773(20020715)41:14<2596::AID-ANIE2596>3.0.CO;2-4 · DOI · Paper page
  72. Tornøe, 2002, Peptidotriazoles on solid phase: [1,2,3]-triazoles by regiospecific copper(I)-catalyzed 1,3-dipolar cycloadditions of terminal alkynes to azides, J Org Chem, 67, 3057, 10.1021/jo011148j · DOI · Paper page
  73. Dieterich, 2006, Selective identification of newly synthesized proteins in mammalian cells using bioorthogonal noncanonical amino acid tagging (BONCAT), Proc Natl Acad Sci Unit States Am, 103, 9482, 10.1073/pnas.0601637103 · DOI · Paper page
  74. Krogager, 2018, Labeling and identifying cell-specific proteomes in the mouse brain, Nat Biotechnol, 36, 156, 10.1038/nbt.4056 · DOI
  75. Cañeque, 2018, Visualizing biologically active small molecules in cells using click chemistry, Nat Rev Chem., 2, 202, 10.1038/s41570-018-0030-x · DOI
  76. Thirumurugan, 2013, Click chemistry for drug development and diverse chemical–biology applications, Chem Rev, 113, 4905, 10.1021/cr200409f · DOI
  77. Agard, 2004, A strain-promoted [3 + 2] azide−alkyne cycloaddition for covalent modification of biomolecules in living systems, J Am Chem Soc, 126, 15046, 10.1021/ja044996f · DOI
  78. Codelli, 2008, Second-generation difluorinated cyclooctynes for copper-free click chemistry, J Am Chem Soc, 130, 11486, 10.1021/ja803086r · DOI
  79. Ning, 2008, Visualizing metabolically labeled glycoconjugates of living cells by copper-free and fast huisgen cycloadditions, Angew Chem Int, 47, 2253, 10.1002/anie.200705456 · DOI
  80. Jewett, 2010, Rapid Cu-free click chemistry with readily synthesized biarylazacyclooctynones, J Am Chem Soc, 132, 3688, 10.1021/ja100014q · DOI · Paper page
  81. Nikić, 2016, Debugging eukaryotic genetic code expansion for site-specific click-PAINT super-resolution microscopy, Angew Chem Int, 55, 16172, 10.1002/anie.201608284 · DOI
  82. Kim, 2019, Biomedical applications of copper-free click chemistry: in vitro, in vivo, and ex vivo, Chem Sci, 10, 7835, 10.1039/C9SC03368H · DOI
  83. Nguyen, 2020, Developing bioorthogonal probes to span a spectrum of reactivities, Nat Rev Chem, 1
  84. Ramil, 2014, Photoclick chemistry: a fluorogenic light-triggered in vivo ligation reaction, Curr Opin Chem Biol, 21, 89, 10.1016/j.cbpa.2014.05.024 · DOI
  85. Song, 2008, Selective functionalization of a genetically encoded alkene-containing protein via “photoclick chemistry” in bacterial cells, J Am Chem Soc, 130, 9654, 10.1021/ja803598e · DOI
  86. Yu, 2012, Genetically encoded cyclopropene directs rapid, photoclick-chemistry-mediated protein labeling in mammalian cells, Angew Chem Int, 51, 10600, 10.1002/anie.201205352 · DOI
  87. Baneyx, 2007, Selection and analysis of solid-binding peptides, Curr Opin Biotechnol, 18, 312, 10.1016/j.copbio.2007.04.008 · DOI
  88. Tsukiji, 2009, Ligand-directed tosyl chemistry for protein labeling in vivo, Nat Chem Biol, 5, 341, 10.1038/nchembio.157 · DOI
  89. Tamura, 2018, Rapid labelling and covalent inhibition of intracellular native proteins using ligand-directed N-acyl-N-alkyl sulfonamide, Nat Commun, 9, 1870, 10.1038/s41467-018-04343-0 · DOI · Paper page
  90. Akabori, 1956, An asymmetric catalyst, Nature, 178, 323, 10.1038/178323b0 · DOI
  91. Davis, 2019, Artificial metalloenzymes: challenges and opportunities, ACS Cent Sci, 5, 1120, 10.1021/acscentsci.9b00397 · DOI
  92. Miller, 2020, Artificial iron proteins: modeling the active sites in non-heme dioxygenases, Inorg Chem, 59, 6000, 10.1021/acs.inorgchem.9b03791 · DOI
  93. Solomon, 2003, Non-heme iron enzymes: contrasts to heme catalysis, Proc Natl Acad Sci Unit States Am, 100, 3589, 10.1073/pnas.0336792100 · DOI
  94. Gao, 2018, Recent examples of α-ketoglutarate-dependent mononuclear non-haem iron enzymes in natural product biosyntheses, Nat Prod Rep, 35, 792, 10.1039/C7NP00067G · DOI
  95. Brandenberg, 2017, Exploiting and engineering hemoproteins for abiological carbene and nitrene transfer reactions, Curr Opin Biotechnol, 47, 102, 10.1016/j.copbio.2017.06.005 · DOI
  96. Schwizer, 2018, Artificial metalloenzymes: reaction scope and optimization Strategies, Chem Rev, 118, 142, 10.1021/acs.chemrev.7b00014 · DOI
  97. Himiyama, 2020, Artificial metalloenzymes: from selective chemical transformations to biochemical applications, Molecules, 25, 2989, 10.3390/molecules25132989 · DOI
  98. Liang, 2019, Artificial metalloenzymes based on the biotin–streptavidin technology: enzymatic cascades and directed evolution, Acc Chem Res, 52, 585, 10.1021/acs.accounts.8b00618 · DOI
  99. Siakkou, 2011, Correlating crosslink formation with enzymatic activity in cysteine dioxygenase, Biochim Biophys Acta Protein Proteonomics, 1814, 2003, 10.1016/j.bbapap.2011.07.019 · DOI
  100. Dominy, 2008, Synthesis of amino acid cofactor in cysteine dioxygenase is regulated by substrate and represents a novel post-translational regulation of activity, J Biol Chem, 283, 12188, 10.1074/jbc.M800044200 · DOI
  101. Li, 2018, Cleavage of a carbon–fluorine bond by an engineered cysteine dioxygenase, Nat Chem Biol, 14, 853, 10.1038/s41589-018-0085-5 · DOI
  102. Li, 2019, Probing the Cys-Tyr cofactor biogenesis in cysteine dioxygenase by the genetic incorporation of fluorotyrosine, Biochemistry, 58, 2218, 10.1021/acs.biochem.9b00006 · DOI
  103. Simmons, 2006, Crystal structure of mammalian cysteine dioxygenase a novel mononuclear iron center for cysteine thiol oxidation, J Biol Chem, 281, 18723, 10.1074/jbc.M601555200 · DOI
  104. Chen, 2018, Use of a tyrosine analogue to modulate the two activities of a nonheme iron enzyme ovoA in ovothiol biosynthesis, cysteine oxidation versus oxidative C–S bond formation, J Am Chem Soc, 140, 4604, 10.1021/jacs.7b13628 · DOI
  105. Yan, 2015, Endoperoxide formation by an α-ketoglutarate-dependent mononuclear non-haem iron enzyme, Nature, 527, 539, 10.1038/nature15519 · DOI
  106. Yu, 2015, Defining the role of tyrosine and rational tuning of oxidase activity by genetic incorporation of unnatural tyrosine analogs, J Am Chem Soc, 137, 4594, 10.1021/ja5109936 · DOI
  107. Zhou, 2013, Probing the function of the Tyr-Cys cross-link in metalloenzymes by the genetic incorporation of 3-methylthiotyrosine, Angew Chem Int, 52, 1203, 10.1002/anie.201207229 · DOI
  108. Liu, 2012, Significant increase of oxidase activity through the genetic incorporation of a tyrosine-histidine cross-link in a myoglobin model of heme-copper oxidase, Angew Chem Int, 51, 4312, 10.1002/anie.201108756 · DOI
  109. Cheah, 2012, Ergothioneine; antioxidant potential, physiological function and role in disease, Biochim Biophys Acta (BBA) - Mol Basis Dis, 1822, 784, 10.1016/j.bbadis.2011.09.017 · DOI · Paper page
  110. Ames, 2018, Prolonging healthy aging: longevity vitamins and proteins, Proc Natl Acad Sci Unit States Am, 115, 10836, 10.1073/pnas.1809045115 · DOI
  111. Seebeck, 2010, In vitro reconstitution of mycobacterial ergothioneine biosynthesis, J Am Chem Soc, 132, 6632, 10.1021/ja101721e · DOI
  112. Hu, 2014, Bioinformatic and biochemical characterizations of C-S bond formation and cleavage enzymes in the fungus Neurospora crassa ergothioneine biosynthetic pathway, Org Lett, 16, 5382, 10.1021/ol502596z · DOI
  113. Irani, 2018, Snapshots of C-S cleavage in Egt2 reveals substrate specificity and reaction mechanism, Cell Chem Biol., 25, 519, 10.1016/j.chembiol.2018.02.002 · DOI
  114. Braunshausen, 2011, Identification and characterization of the first ovothiol biosynthetic enzyme, J Am Chem Soc, 133, 1757, 10.1021/ja109378e · DOI
  115. Naowarojna, 2018, Mini-review: ergothioneine and ovothiol biosyntheses, an unprecedented trans-sulfur strategy in natural product biosynthesis, Biochemistry, 57, 3309, 10.1021/acs.biochem.8b00239 · DOI
  116. Goncharenko, 2015, Structure of the sulfoxide synthase EgtB from the ergothioneine biosynthetic pathway, Angew Chem Int, 54, 2821, 10.1002/anie.201410045 · DOI
  117. Naowarojna, 2019, Crystal structure of the ergothioneine sulfoxide synthase from Candidatus Chloracidobacterium thermophilum and structure-guided engineering to modulate tts substrate selectivity, ACS Catal, 9, 6955, 10.1021/acscatal.9b02054 · DOI
  118. Stampfli, 2019, An alternative active site architecture for O2 activation in the ergothioneine biosynthetic EgtB from Chloracidobacterium thermophilum, J Am Chem Soc, 141, 5275, 10.1021/jacs.8b13023 · DOI
  119. Faponle, 2017, Sulfoxide synthase versus cysteine dioxygenase reactivity in a nonheme iron enzyme, J Am Chem Soc, 139, 9259, 10.1021/jacs.7b04251 · DOI
  120. Wei, 2017, Theoretical study of the mechanism of the non-heme iron enzyme EgtB, Inorg Chem, 56, 3589, 10.1021/acs.inorgchem.6b03177 · DOI
  121. Tian, 2018, Mechanism of sulfoxidation and C–S bond formation involved in the biosynthesis of ergothioneine catalyzed by ergothioneine synthase (EgtB), ACS Catal, 8, 5875, 10.1021/acscatal.8b01473 · DOI
  122. Song, 2014, Cysteine oxidation reactions catalyzed by a mononuclear non-heme iron enzyme (OvoA) in ovothiol biosynthesis, Org Lett, 16, 2122, 10.1021/ol5005438 · DOI
  123. Chen, 2019, Mechanistic studies of a nonheme iron enzyme OvoA in ovothiol biosynthesis using a tyrosine analogue, 2-amino-3-(4-hydroxy-3-(methoxyl) phenyl) propanoic acid (MeOTyr), ACS Catal, 9, 253, 10.1021/acscatal.8b03903 · DOI
  124. Yu, 2015, Significant improvement of oxidase activity through the genetic incorporation of a redox-active unnatural amino acid, Chem Sci, 6, 3881, 10.1039/C5SC01126D · DOI
  125. Kato, 2011, Gene disruption and biochemical characterization of verruculogen synthase of Aspergillus fumigatus, Chembiochem, 12, 711, 10.1002/cbic.201000562 · DOI
  126. Steffan, 2009, FtmOx1, a non-heme Fe(II) and α-ketoglutarate-dependent dioxygenase, catalyses the endoperoxide formation of verruculogen in Aspergillus fumigatus, Org Biomol Chem, 7, 4082, 10.1039/b908392h · DOI
  127. Dunham, 2019, Hydrogen donation but not abstraction by a tyrosine (Y68) during endoperoxide installation by verruculogen synthase (FtmOx1), J Am Chem Soc, 141, 9964, 10.1021/jacs.9b03567 · DOI
  128. Chan, 1990, Cytochrome c oxidase: understanding nature's design of a proton pump, Biochemistry, 29, 1, 10.1021/bi00453a001 · DOI
  129. Collman, 2007, A cytochrome c oxidase model catalyzes oxygen to water reduction under rate-limiting electron flux, Science, 315, 1565, 10.1126/science.1135844 · DOI
  130. Kaila, 2010, Wikström M. Proton-coupled electron transfer in cytochrome oxidase, Chem Rev, 110, 7062, 10.1021/cr1002003 · DOI
  131. Carey, 2004, A site-selective dual anchoring strategy for artificial metalloprotein design, J Am Chem Soc, 126, 10812, 10.1021/ja046908x · DOI
  132. Yeung, 2009, Rational design of a structural and functional nitric oxide reductase, Nature, 462, 1079, 10.1038/nature08620 · DOI
  133. Lin, 2018, Rational design of artificial metalloenzymes: case studies in myoglobin, Prog Chem, 30, 1464
  134. Lin, 2017, Rational design of metalloenzymes: from single to multiple active sites, Coord Chem Rev, 336, 1, 10.1016/j.ccr.2017.01.001 · DOI
  135. Nastri, 2016, Design and engineering of artificial oxygen-activating metalloenzymes, Chem Soc Rev, 45, 5020, 10.1039/C5CS00923E · DOI
  136. Reetz, 2019, Directed evolution of artificial metalloenzymes: a universal means to tune the selectivity of transition metal catalysts?, Acc Chem Res, 52, 336, 10.1021/acs.accounts.8b00582 · DOI
  137. Sigman, 2000, From myoglobin to heme-copper oxidase: design and engineering of a CuB center into sperm whale myoglobin, J Am Chem Soc, 122, 8192, 10.1021/ja0015343 · DOI
  138. Miner, 2012, A designed functional metalloenzyme that reduces O2 to H2O with over one thousand turnovers, Angew Chem Int, 51, 5589, 10.1002/anie.201201981 · DOI
  139. Bhagi-Damodaran, 2014, Systematic tuning of heme redox potentials and its effects on O2 reduction rates in a designed oxidase in myoglobin, J Am Chem Soc, 136, 11882, 10.1021/ja5054863 · DOI
  140. Reynolds, 2016, An evolved orthogonal enzyme/cofactor pair, J Am Chem Soc, 138, 12451, 10.1021/jacs.6b05847 · DOI
  141. Liu, 2014, Metalloproteins containing cytochrome, iron–sulfur, or copper redox centers, Chem Rev, 114, 4366, 10.1021/cr400479b · DOI
  142. Festa, 2011, Copper: an essential metal in biology, Curr Biol, 21, R877, 10.1016/j.cub.2011.09.040 · DOI
  143. Berry, 2003, Probing the role of axial methionine in the blue copper center of azurin with unnatural amino acids, J Am Chem Soc, 125, 8760, 10.1021/ja029699u · DOI
  144. Garner, 2006, Reduction potential tuning of the blue copper center in Pseudomonas aeruginosa azurin by the axial methionine as probed by unnatural amino acids, J Am Chem Soc, 128, 15608, 10.1021/ja062732i · DOI
  145. Hwang, 2005, Blue ferrocenium azurin: an organometalloprotein with tunable redox properties, J Am Chem Soc, 127, 15356, 10.1021/ja054983h · DOI

Cited by

Sorted by citations

Metadata

Authors
Naowarojna, N., Cheng, R., Lopez, J., Wong, C., Qiao, L., & Liu, P.
Affiliations
Boston University (US)
Corresponding author
Liu, Pinghua
ORCID
Venue
Synthetic and Systems Biotechnology
Publisher
Elsevier BV
Published
2021-03
Volume
6
Issue
1
Pages
32-49
ISSN
  • 2097-1206 (ISSN-L)
  • 2405-805X
DOI
10.1016/j.synbio.2021.01.001
PMC
PMC7897936
OpenAlex
W3133314164
Cited by
52
References
6
Citations by year
2026: 6 · 2025: 12 · 2024: 12 · 2023: 5 · 2022: 11 · 2021: 5
FWCI
0.89
Type
journal article
Language
en
Open access
Licence
Locations
  • Synthetic and Systems Biotechnology (publishedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • OpenBU (Boston University) (publishedVersion, cc-by-nc-nd)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
National Science Foundation (CHE-2004109)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
  • Physical Sciences › Chemistry › Organic Chemistry › Click Chemistry and Applications
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Keywords
protein chemical modification, metalloenzymes, unnatural amino acid incorporation, genetic code expansion, enzyme mechanism, enzyme activity enhancement, enzyme mimics

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review