Chemical modifications of proteins and their applications in metalloenzyme studies

Synthetic and Systems Biotechnology - Tập 6 - Trang 32-49 - 2021
Nathchar Naowarojna1, Ronghai Cheng1, Juan Lopez1, Christina Wong1, Lu Qiao1, Pinghua Liu1
1Department of Chemistry, Boston University, Boston, MA, 02215, United States

Tài liệu tham khảo

Sakamoto, 2018, Recent progress in chemical modification of proteins, Anal Sci, 35, 10.2116/analsci.18R003 Shadish, 2020, Site-selective protein modification: from functionalized proteins to functional biomaterials, Matter, 2, 50, 10.1016/j.matt.2019.11.011 Nischan, 2014, Site-specific PEGylation of proteins: recent developments, J Org Chem, 79, 10727, 10.1021/jo502136n Wurm, 2013, One-pot squaric acid diester mediated aqueous protein conjugation, Chem Commun, 49, 7815, 10.1039/c3cc44039g Spicer, 2014, Selective chemical protein modification, Nat Commun, 5, 4740, 10.1038/ncomms5740 DeForest, 2015, A photoreversible protein-patterning approach for guiding stem cell fate in three-dimensional gels, Nat Mater, 14, 523, 10.1038/nmat4219 Matos, 2018, Chemo- and regioselective lysine modification on native proteins, J Am Chem Soc, 140, 4004, 10.1021/jacs.7b12874 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 Dawson, 1994, Synthesis of proteins by native chemical ligation, Science, 266, 776, 10.1126/science.7973629 Muir, 2003, Semisynthesis of proteins by expressed protein ligation, Annu Rev Biochem, 72, 249, 10.1146/annurev.biochem.72.121801.161900 Vila-Perelló, 2013, Streamlined expressed protein ligation using split inteins, J Am Chem Soc, 135, 286, 10.1021/ja309126m Minnihan, 2009, Unnatural amino acids: better than the real things?, F1000 Biol Rep, 1, 88, 10.3410/B1-88 David, 2015, Chemical tagging and customizing of cellular chromatin states using ultrafast trans-splicing inteins, Nat Chem, 7, 394, 10.1038/nchem.2224 Gilmore, 2006, N-terminal protein modification through a biomimetic transamination reaction, Angew Chem Int, 45, 5307, 10.1002/anie.200600368 Scheck, 2007, Regioselective labeling of antibodies through N-terminal transamination, ACS Synth Biol, 2, 247 Scheck, 2008, Optimization of a biomimetic transamination reaction, J Am Chem Soc, 130, 11762, 10.1021/ja802495w Christman, 2007, Site-specific protein immobilization through N-terminal oxime linkages, J Mater Chem, 17, 2021, 10.1039/b618002g Jie, 2017, Development and applications of bioorthogonal cleavage reactions, Hua Hsueh Hsueh Pao, 75, 1173 Chalker, 2011, “tag-and-modify” approach to site-selective protein modification, Acc Chem Res, 44, 730, 10.1021/ar200056q Crankshaw, 1996, Modification of cysteine, Curr Protein Pept Sci, 3, 15 Goddard, 1935, Derivatives of keratin, J Biol Chem, 112, 361, 10.1016/S0021-9258(18)74993-4 Lundell, 1999, Sample preparation for peptide mapping-a pharmaceutical quality-control perspective, Anal Biochem, 266, 31, 10.1006/abio.1998.2919 Moore, 1956, Cross-linking of bovine plasma albumin and wool keratin, J Am Chem Soc, 78, 2414, 10.1021/ja01592a020 Tsao, 1953, The extraction, purification and some chemical properties of actin, Biochim Biophys Acta, 11, 102, 10.1016/0006-3002(53)90013-4 Gamblin, 2003, Glycosyl phenylthiosulfonates (Glyco-PTS): novel reagents for glycoprotein synthesis, Org Biomol Chem, 1, 3642, 10.1039/b306990g Bernardes, 2008, From disulfide-to thioether-linked glycoproteins, Angew Chem Int, 120, 2276, 10.1002/ange.200704381 Fontaine, 2015, Long-term stabilization of maleimide–thiol conjugates, Bioconjugate Chem, 26, 145, 10.1021/bc5005262 Lyon, 2014, Self-hydrolyzing maleimides improve the stability and pharmacological properties of antibody-drug conjugates, Nat Biotechnol, 32, 1059, 10.1038/nbt.2968 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 Koniev, 2014, Selective irreversible chemical tagging of cysteine with 3-arylpropiolonitriles, Bioconjugate Chem, 25, 202, 10.1021/bc400469d 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 Abbas, 2014, Allenamides as orthogonal handles for selective modification of cysteine in peptides and proteins, Angew Chem Int, 53, 7491, 10.1002/anie.201403121 Conte, 2011, Multi-molecule reaction of serum albumin can occur through thiol-yne coupling, Chem Commun, 47, 11086, 10.1039/c1cc14402b Bernardim, 2016, Stoichiometric and irreversible cysteine-selective protein modification using carbonylacrylic reagents, Nat Commun, 7, 1, 10.1038/ncomms13128 Bernardim, 2019, Efficient and irreversible antibody–cysteine bioconjugation using carbonylacrylic reagents, Nat Protoc, 14, 86, 10.1038/s41596-018-0083-9 Gil de Montes, 2020, Stable pyrrole-linked bioconjugates through tetrazine-triggered azanorbornadiene fragmentation, Angew Chem Int, 132, 6255, 10.1002/ange.201914529 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 Kuan, 2016, Site-selective disulfide modification of proteins: expanding diversity beyond the proteome, Chem Eur J, 22, 17112, 10.1002/chem.201602298 Forte, 2018, Homogeneous antibody-drug conjugates via site-selective disulfide bridging, Drug Discov Today Technol, 30, 11, 10.1016/j.ddtec.2018.09.004 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 Lee, 2016, Next-generation disulfide stapling: reduction and functional re-bridging all in one, Chem Sci, 7, 799, 10.1039/C5SC02666K Jones, 2012, Direct peptide bioconjugation/PEGylation at tyrosine with linear and branched polymeric diazonium salts, J Am Chem Soc, 134, 7406, 10.1021/ja211855q 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 Seim, 2011, Oxidative modification of native protein residues using cerium (IV) ammonium nitrate, J Am Chem Soc, 133, 16970, 10.1021/ja206324q Tilley, 2006, Tyrosine-selective protein alkylation using π-allylpalladium complexes, J Am Chem Soc, 128, 1080, 10.1021/ja057106k Ruan, 2017, Manganese-catalyzed C-H alkynylation: expedient peptide synthesis and modification, Angew Chem Int, 56, 3172, 10.1002/anie.201611118 Schischko, 2017, Bioorthogonal diversification of peptides through selective ruthenium (II)-catalyzed C–H activation, Angew Chem Int, 56, 1576, 10.1002/anie.201609631 Siti, 2015, Photo-induced conjugation of tetrazoles to modified and native proteins, Org Biomol Chem, 13, 3202, 10.1039/C4OB02025A Seki, 2016, Transition metal-free tryptophan-selective bioconjugation of proteins, J Am Chem Soc, 138, 10798, 10.1021/jacs.6b06692 deGruyter, 2017, Malins LR, Baran PS. Residue-specific peptide modification: a chemist's guide, Biochemistry, 56, 3863, 10.1021/acs.biochem.7b00536 Hoyt, 2019, Contemporary approaches to site-selective protein modification, Nat Rev Chem., 3, 147, 10.1038/s41570-019-0079-1 Conibear, 2020, Deciphering protein post-translational modifications using chemical biology tools, Nat Rev Chem, 1 Drienovská, 2017, Design of an enantioselective artificial metallo-hydratase enzyme containing an unnatural metal-binding amino acid, Chem Sci, 8, 7228, 10.1039/C7SC03477F Drienovská, 2020, Expanding the enzyme universe with genetically encoded unnatural amino acids, Nat Catal, 1 Won, 2019, Recent advances in enzyme engineering through incorporation of unnatural amino acids, Biotechnol Bioproc Eng, 24, 1, 10.1007/s12257-019-0163-x Srinivasan, 2002, Pyrrolysine encoded by UAG in Archaea: charging of a UAG-decoding specialized tRNA, Science, 296, 1459, 10.1126/science.1069588 Böck, 1991, Selenocysteine: the 21st amino acid, Mol Microbiol, 5, 515, 10.1111/j.1365-2958.1991.tb00722.x 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 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 Liu, 2010, Adding new chemistries to the genetic code, Annu Rev Biochem, 79, 413, 10.1146/annurev.biochem.052308.105824 Chin, 2017, Expanding and reprogramming the genetic code, Nature, 550, 53, 10.1038/nature24031 Lajoie, 2013, Genomically recoded organisms expand biological functions, Science, 342, 357, 10.1126/science.1241459 Mukai, 2015, Highly reproductive Escherichia coli cells with no specific assignment to the UAG codon, Sci Rep, 5, 1, 10.1038/srep09699 Dumas, 2015, Designing logical codon reassignment-Expanding the chemistry in biology, Chem Sci, 6, 50, 10.1039/C4SC01534G Bryson, 2017, Continuous directed evolution of aminoacyl-tRNA synthetases, Nat Chem Biol, 13, 1253, 10.1038/nchembio.2474 Italia, 2017, An orthogonalized platform for genetic code expansion in both bacteria and eukaryotes, Nat Chem Biol, 13, 446, 10.1038/nchembio.2312 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 Rackham, 2005, A network of orthogonal ribosome· mRNA pairs, Nat Chem Biol, 1, 159, 10.1038/nchembio719 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 Neumann, 2010, Encoding multiple unnatural amino acids via evolution of a quadruplet-decoding ribosome, Nature, 464, 441, 10.1038/nature08817 Schmied, 2018, Controlling orthogonal ribosome subunit interactions enables evolution of new function, Nature, 564, 444, 10.1038/s41586-018-0773-z Riddle, 1973, Frameshift suppression: a nucleotide addition in the anticodon of a glycine transfer RNA, Nat New Biol, 242, 230, 10.1038/newbio242230a0 Fischer, 2020, New codons for efficient production of unnatural proteins in a semisynthetic organism, Nat Chem Biol, 1 Lang, 2014, Cellular incorporation of unnatural amino acids and bioorthogonal labeling of proteins, Chem Rev, 114, 4764, 10.1021/cr400355w 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 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 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 Krogager, 2018, Labeling and identifying cell-specific proteomes in the mouse brain, Nat Biotechnol, 36, 156, 10.1038/nbt.4056 Cañeque, 2018, Visualizing biologically active small molecules in cells using click chemistry, Nat Rev Chem., 2, 202, 10.1038/s41570-018-0030-x Thirumurugan, 2013, Click chemistry for drug development and diverse chemical–biology applications, Chem Rev, 113, 4905, 10.1021/cr200409f 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 Codelli, 2008, Second-generation difluorinated cyclooctynes for copper-free click chemistry, J Am Chem Soc, 130, 11486, 10.1021/ja803086r 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 Jewett, 2010, Rapid Cu-free click chemistry with readily synthesized biarylazacyclooctynones, J Am Chem Soc, 132, 3688, 10.1021/ja100014q Nikić, 2016, Debugging eukaryotic genetic code expansion for site-specific click-PAINT super-resolution microscopy, Angew Chem Int, 55, 16172, 10.1002/anie.201608284 Kim, 2019, Biomedical applications of copper-free click chemistry: in vitro, in vivo, and ex vivo, Chem Sci, 10, 7835, 10.1039/C9SC03368H Nguyen, 2020, Developing bioorthogonal probes to span a spectrum of reactivities, Nat Rev Chem, 1 Vrabel, 2016 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 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 Yu, 2012, Genetically encoded cyclopropene directs rapid, photoclick-chemistry-mediated protein labeling in mammalian cells, Angew Chem Int, 51, 10600, 10.1002/anie.201205352 Baneyx, 2007, Selection and analysis of solid-binding peptides, Curr Opin Biotechnol, 18, 312, 10.1016/j.copbio.2007.04.008 Tsukiji, 2009, Ligand-directed tosyl chemistry for protein labeling in vivo, Nat Chem Biol, 5, 341, 10.1038/nchembio.157 Tamura, 2018, Chemistry for covalent modification of endogenous/native proteins: from test tubes to complex biological systems, J Am Chem Soc, 141, 2782, 10.1021/jacs.8b11747 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 Akabori, 1956, An asymmetric catalyst, Nature, 178, 323, 10.1038/178323b0 Davis, 2019, Artificial metalloenzymes: challenges and opportunities, ACS Cent Sci, 5, 1120, 10.1021/acscentsci.9b00397 Miller, 2020, Artificial iron proteins: modeling the active sites in non-heme dioxygenases, Inorg Chem, 59, 6000, 10.1021/acs.inorgchem.9b03791 Solomon, 2003, Non-heme iron enzymes: contrasts to heme catalysis, Proc Natl Acad Sci Unit States Am, 100, 3589, 10.1073/pnas.0336792100 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 Song, 2019 Poulos, 2014, Heme enzyme structure and function, Chem Rev, 114, 3919, 10.1021/cr400415k 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 Schwizer, 2018, Artificial metalloenzymes: reaction scope and optimization Strategies, Chem Rev, 118, 142, 10.1021/acs.chemrev.7b00014 Himiyama, 2020, Artificial metalloenzymes: from selective chemical transformations to biochemical applications, Molecules, 25, 2989, 10.3390/molecules25132989 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 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 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 Li, 2018, Cleavage of a carbon–fluorine bond by an engineered cysteine dioxygenase, Nat Chem Biol, 14, 853, 10.1038/s41589-018-0085-5 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 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 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 Yan, 2015, Endoperoxide formation by an α-ketoglutarate-dependent mononuclear non-haem iron enzyme, Nature, 527, 539, 10.1038/nature15519 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 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 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 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 Ames, 2018, Prolonging healthy aging: longevity vitamins and proteins, Proc Natl Acad Sci Unit States Am, 115, 10836, 10.1073/pnas.1809045115 Seebeck, 2010, In vitro reconstitution of mycobacterial ergothioneine biosynthesis, J Am Chem Soc, 132, 6632, 10.1021/ja101721e 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 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 Braunshausen, 2011, Identification and characterization of the first ovothiol biosynthetic enzyme, J Am Chem Soc, 133, 1757, 10.1021/ja109378e 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 Goncharenko, 2015, Structure of the sulfoxide synthase EgtB from the ergothioneine biosynthetic pathway, Angew Chem Int, 54, 2821, 10.1002/anie.201410045 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 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 Faponle, 2017, Sulfoxide synthase versus cysteine dioxygenase reactivity in a nonheme iron enzyme, J Am Chem Soc, 139, 9259, 10.1021/jacs.7b04251 Wei, 2017, Theoretical study of the mechanism of the non-heme iron enzyme EgtB, Inorg Chem, 56, 3589, 10.1021/acs.inorgchem.6b03177 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 Song, 2014, Cysteine oxidation reactions catalyzed by a mononuclear non-heme iron enzyme (OvoA) in ovothiol biosynthesis, Org Lett, 16, 2122, 10.1021/ol5005438 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 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 Kato, 2011, Gene disruption and biochemical characterization of verruculogen synthase of Aspergillus fumigatus, Chembiochem, 12, 711, 10.1002/cbic.201000562 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 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 Chan, 1990, Cytochrome c oxidase: understanding nature's design of a proton pump, Biochemistry, 29, 1, 10.1021/bi00453a001 Collman, 2007, A cytochrome c oxidase model catalyzes oxygen to water reduction under rate-limiting electron flux, Science, 315, 1565, 10.1126/science.1135844 Kaila, 2010, Wikström M. Proton-coupled electron transfer in cytochrome oxidase, Chem Rev, 110, 7062, 10.1021/cr1002003 Carey, 2004, A site-selective dual anchoring strategy for artificial metalloprotein design, J Am Chem Soc, 126, 10812, 10.1021/ja046908x Yeung, 2009, Rational design of a structural and functional nitric oxide reductase, Nature, 462, 1079, 10.1038/nature08620 Lin, 2018, Rational design of artificial metalloenzymes: case studies in myoglobin, Prog Chem, 30, 1464 Lin, 2017, Rational design of metalloenzymes: from single to multiple active sites, Coord Chem Rev, 336, 1, 10.1016/j.ccr.2017.01.001 Nastri, 2016, Design and engineering of artificial oxygen-activating metalloenzymes, Chem Soc Rev, 45, 5020, 10.1039/C5CS00923E 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 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 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 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 Reynolds, 2016, An evolved orthogonal enzyme/cofactor pair, J Am Chem Soc, 138, 12451, 10.1021/jacs.6b05847 Liu, 2014, Metalloproteins containing cytochrome, iron–sulfur, or copper redox centers, Chem Rev, 114, 4366, 10.1021/cr400479b Festa, 2011, Copper: an essential metal in biology, Curr Biol, 21, R877, 10.1016/j.cub.2011.09.040 Messerschmidt, 2010 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 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 Hwang, 2005, Blue ferrocenium azurin: an organometalloprotein with tunable redox properties, J Am Chem Soc, 127, 15356, 10.1021/ja054983h