Abstract
In nature, photoautotroph organisms are capable of converting solar energy into chemical energy. Inspired by this phenomenon, natural photosynthesis could serve as an inspiration for the generation of artificial photosynthetic platforms. In particular, connecting photo-catalysis with biocatalysis can provide an efficient biotransformation system, which is highly selective and environmentally benign. In this chapter, the photo-catalytic pathways involved have been discussed in detail. Further, the structural and catalytic mechanisms of enzymes involved in light-driven catalysis are categorized. Moreover, the chapter highlights the incorporation of nanoparticles in the photo-catalytic system as an enzyme activator to make the process efficient and cost-effective. The application of photo-biocatalysis in various biotransformations has been explained with the state-of-the-art examples in halogenations, decarboxylation, and epoxidation. The chapter mainly focuses on the enzymes associated with light-driven catalysis along with the probable mechanism involved. Several applications of enzyme-assisted photo-catalysis while exploring the correlation of factors affecting the overall process are comprehensively explored. Finally, strategies for the large-scale implementation of photobiocatalyst for the production of a variety of chemicals via biological route are briefly discussed.
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References
Adam D, Bösche L, Castañeda-Losada L, Winkler M, Apfel U, Happe T (2017) Sunlight-dependent hydrogen production by photosensitizer/hydrogenase systems. ChemSusChem 10:894–902
Aprile C, Corma A, Garcia H (2008) Enhancement of the photocatalytic activity of TiO2 through spatial structuring and particle size control: from subnanometric to submillimetric length scale. Phys Chem Chem Phys 10:769–783. https://doi.org/10.1039/b712168g
Aresta M, Dibenedetto A, Baran T, Angelini A, Łabuz P, Macyk W (2014) An integrated photocatalytic/enzymatic system for the reduction of CO2 to methanol in bioglycerol-water. Beilstein J Org Chem 10:2556–2565. https://doi.org/10.3762/bjoc.10.267
Balcerzak L, Lipok J, Strub D, Lochyński S (2014) Biotransformations of monoterpenes by photoautotrophic micro-organisms. J Appl Microbiol 117:1523–1536. https://doi.org/10.1111/jam.12632
Balke K, Kadow M, Mallin H, Saß S, Bornscheuer UT (2012) Discovery, application and protein engineering of Baeyer-Villiger monooxygenases for organic synthesis. Org Biomol Chem 10:6249–6265
Balke K, Beier A, Bornscheuer UT (2018) Hot spots for the protein engineering of Baeyer-Villiger monooxygenases. Biotechnol Adv 36:247–263
Bartsch M, Gassmeyer SK, Köninger K, Igarashi K, Liauw P, Dyczmons-Nowaczyk N, Miyamoto K, Nowaczyk MM, Kourist R (2015) Photosynthetic production of enantioselective biocatalysts. Microb Cell Fact 14:53. https://doi.org/10.1186/s12934-015-0233-5
Beatty JW, Douglas JJ, Cole KP, Stephenson CRJ (2015) A scalable and operationally simple radical trifluoromethylation. Nat Commun 6:1–6. https://doi.org/10.1038/ncomms8919
Bernard J, van Heerden E, Arends IWCE, Opperman DJ, Hollmann F (2012) Chemoenzymatic reduction of conjugated C=C double bonds. ChemCatChem 4:196–199. https://doi.org/10.1002/cctc.201100312
Bernhardt R (2006) Cytochromes P450 as versatile biocatalysts. J Biotechnol 124:128–145
Bhatia S, Bhatia S (2018) Introduction to enzymes and their applications. In: Introduction to pharmaceutical biotechnology, vol 2. https://doi.org/10.1088/978-0-7503-1302-5ch1
Bisagni S, Summers B, Kara S, Hatti-Kaul R, Grogan G, Mamo G, Hollmann F (2014) Exploring the substrate specificity and enantioselectivity of a baeyer-villiger monooxygenase from dietzia sp. D5: oxidation of sulfides and aldehydes. Top Catal 57:366–375. https://doi.org/10.1007/s11244-013-0192-1
Brown KA, Wilker MB, Boehm M, Dukovic G, King PW (2012) Characterization of photochemical processes for H2 production by CdS nanorod–[FeFe] hydrogenase complexes. J Am Chem Soc 134:5627–5636
Brown KA, Wilker MB, Boehm M, Hamby H, Dukovic G, King PW (2016) Photocatalytic regeneration of nicotinamide cofactors by quantum dot-enzyme biohybrid complexes. ACS Catal 6:2201–2204. https://doi.org/10.1021/acscatal.5b02850
Caputo CA, Wang L, Beranek R, Reisner E (2015) Carbon nitride–TiO2 hybrid modified with hydrogenase for visible light driven hydrogen production. Chem Sci 6:5690–5694
Chaiyen P, Fraaije MW, Mattevi A (2012) The enigmatic reaction of flavins with oxygen. Trends Biochem Sci 37:373–380
Chen Y-H, Chen L-L, Shang N-C (2009) Photocatalytic degradation of dimethyl phthalate in an aqueous solution with Pt-doped TiO2-coated magnetic PMMA microspheres. J Hazard Mater 172:20–29
Choudhury S, Baeg J-O, Park N-J, Yadav RK (2012) A photocatalyst/enzyme couple that uses solar energy in the asymmetric reduction of acetophenones. Angew Chem Int Ed 51:11624–11628. https://doi.org/10.1002/anie.201206019
Choudhury S, Baeg JO, Park NJ, Yadav RK (2014) A solar light-driven, eco-friendly protocol for highly enantioselective synthesis of chiral alcohols via photocatalytic/biocatalytic cascades. Green Chem 16:4389–4400. https://doi.org/10.1039/c4gc00885e
Churakova E, Kluge M, Ullrich R, Arends I, Hofrichter M, Hollmann F (2011) Specific photobiocatalytic oxyfunctionalization reactions. Angew Chem 123:10904–10907. https://doi.org/10.1002/ange.201105308
Churakova E, Arends IWCE, Hollmann F (2013) Increasing the productivity of peroxidase-catalyzed oxyfunctionalization: a case study on the potential of two-liquid-phase systems. ChemCatChem 5:565–568. https://doi.org/10.1002/cctc.201200490
Dailey HA (1997) Enzymes of heme biosynthesis. JBIC J Biol Inorg Chem 2:411–417
Dawson JH (1988) Probing structure-function relations in heme-containing oxygenases and peroxidases. Science 240(80–):433–439
de Gonzalo G, Mihovilovic MD, Fraaije MW (2010) Recent developments in the application of Baeyer-Villiger monooxygenases as biocatalysts. ChemBioChem 11:2208–2231
Dobbek H, Svetlitchnyi V, Gremer L, Huber R, Meyer O (2001) Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni–4Fe–5S] cluster. Science 293(80–):1281–1285
Dong JJ, Fernández-Fueyo E, Hollmann F, Paul CE, Pesic M, Schmidt S, Wang Y, Younes S, Zhang W (2018) Biocatalytic oxidation reactions: a chemist’s perspective. Angew Chem Int Ed 57:9238–9261. https://doi.org/10.1002/anie.201800343
Dutta AK, Maji SK, Srivastava DN, Mondal A, Biswas P, Paul P, Adhikary B (2012) Synthesis of FeS and FeSe nanoparticles from a single source precursor: a study of their photocatalytic activity, peroxidase-like behavior, and electrochemical sensing of H2O2. ACS Appl Mater Interfaces 4:1919–1927
Ener ME, Lee YT, Winkler JR, Gray HB, Cheruzela L (2010) Photooxidation of cytochrome P450-BM3. Proc Natl Acad Sci U S A 107:18783–18786. https://doi.org/10.1073/pnas.1012381107
Evans DJ, Pickett CJ (2003) Chemistry and the hydrogenases. Chem Soc Rev 32:268–275
Fontecave M (2006) Iron-sulfur clusters: ever-expanding roles. Nat Chem Biol 2:171–174
Gabruk M, Mysliwa-Kurdziel B (2015) Light-dependent protochlorophyllide oxidoreductase: phylogeny, regulation, and catalytic properties. Biochemistry 54:5255–5262
Gacs J, Zhang W, Knaus T, Mutti FG, Arends IWCE, Hollmann F (2019) A photo-enzymatic cascade to transform racemic alcohols into enantiomerically pure amines. Catalysts 9:1–11. https://doi.org/10.3390/catal9040305
Garrone A, Archipowa N, Zipfel PF, Hermann G, Dietzek B (2015) Plant protochlorophyllide oxidoreductases A and B catalytic efficiency and initial reaction steps. J Biol Chem 290:28530–28539
Girvan HM, Munro AW (2016) Applications of microbial cytochrome P450 enzymes in biotechnology and synthetic biology. Curr Opin Chem Biol 31:136–145
Górak M, Zymańczyk-Duda E (2015) Application of cyanobacteria for chiral phosphonate synthesis. Green Chem 17:4570–4578. https://doi.org/10.1039/c5gc01195g
Granone LI, Sieland F, Zheng N, Dillert R, Bahnemann DW (2018) Photocatalytic conversion of biomass into valuable products: a meaningful approach? Green Chem 20:1169–1192. https://doi.org/10.1039/c7gc03522e
Grau MM, Van Der Toorn JC, Otten LG, Macheroux P, Taglieber A, Zilly FE, Arends IWCE, Hollmann F (2009) Photoenzymatic reduction of C=C double bonds. Adv Synth Catal 351:3279–3286. https://doi.org/10.1002/adsc.200900560
Hanf R, Fey S, Schmitt M, Hermann G, Dietzek B, Popp J (2012) Catalytic efficiency of a photoenzyme—an adaptation to natural light conditions. ChemPhysChem 13:2013–2015
Höfler GT, Fernández-Fueyo E, Pesic M, Younes SH, Choi E, Kim YH, Urlacher VB, Arends IWCE, Hollmann F (2018) A photoenzymatic NADH regeneration system. ChemBioChem 19:2344–2347. https://doi.org/10.1002/cbic.201800530
Hofrichter M, Ullrich R, Pecyna MJ, Liers C, Lundell T (2010) New and classic families of secreted fungal heme peroxidases. Appl Microbiol Biotechnol 87:871–897
Hollmann F, Taglieber A, Schulz F, Reetz MT (2007) A light-driven stereoselective biocatalytic oxidation. Angew Chem Int Ed 46:2903–2906. https://doi.org/10.1002/anie.200605169
Hollmann F, Arends IWCE, Buehler K (2010) Biocatalytic redox reactions for organic synthesis: nonconventional regeneration methods. ChemCatChem 2:762–782. https://doi.org/10.1002/cctc.201000069
Holtmann D, Hollmann F (2016) The oxygen dilemma: a severe challenge for the application of monooxygenases? ChemBioChem 17:1391–1398. https://doi.org/10.1002/cbic.201600176
Huijbers MME, Montersino S, Westphal AH, Tischler D, van Berkel WJH (2014) Flavin dependent monooxygenases. Arch Biochem Biophys 544:2–17
Husain Q (2010) Peroxidase mediated decolorization and remediation of wastewater containing industrial dyes: a review. Rev Environ Sci Bio/Technol 9:117–140
Jeoung J-H, Fesseler J, Goetzl S, Dobbek H (2014) Carbon monoxide. Toxic gas and fuel for anaerobes and aerobes: carbon monoxide dehydrogenases. In: The metal-driven biogeochemistry of gaseous compounds in the environment. Springer, pp 37–69
Johnson DC, Dean DR, Smith AD, Johnson MK (2005) Structure, function, and formation of biological iron-sulfur clusters. Annu Rev Biochem 74:247–281
Jones JP, O’Hare EJ, Wong L (2001) Oxidation of polychlorinated benzenes by genetically engineered CYP101 (cytochrome P450cam). Eur J Biochem 268:1460–1467
Joosten V, van Berkel WJH (2007) Flavoenzymes. Curr Opin Chem Biol 11:195–202
Kalsoom U, Bhatti HN, Asgher M (2015) Characterization of plant peroxidases and their potential for degradation of dyes: a review. Appl Biochem Biotechnol 176:1529–1550
Kamada K, Moriyasu A, Soh N (2012) Visible-light-driven enzymatic reaction of peroxidase adsorbed on doped hematite thin films. J Phys Chem C 116:20694–20699
Karmee SK, Roosen C, Kohlmann C, Lütz S, Greiner L, Leitner W (2009) Chemo-enzymatic cascade oxidation in supercritical carbon dioxide/water biphasic media. Green Chem 11:1052–1055
Karplus PA, Fox KM, Massey V (1995) Structure-function relations for old yellow enzyme. FASEB J 9:1518–1526
Kato M, Nguyen D, Gonzalez M, Cortez A, Mullen SE, Cheruzel LE (2014) Regio- and stereoselective hydroxylation of 10-undecenoic acid with a light-driven P450 BM3 biocatalyst yielding a valuable synthon for natural product synthesis. Bioorganic Med Chem 22:5687–5691. https://doi.org/10.1016/j.bmc.2014.05.046
Kellner DG, Maves SA, Sligar SG (1997) Engineering cytochrome P450s for bioremediation. Curr Opin Biotechnol 8:274–278
Khalid NR, Ahmed E, Rasheed A, Ahmad M, Ramzan M, Shakoor A, Elahi A, Abbas SM, Hussain R, Niaz NA (2015) Co-doping effect of carbon and yttrium on photocatalytic activity of tio 2 nanoparticles for methyl orange degradation. J Ovonic Res 11:107–112
Kim J, Lee SH, Tieves F, Choi DS, Hollmann F, Paul CE, Park CB (2018) Biocatalytic C=C bond reduction through carbon nanodot-sensitized regeneration of NADH analogues. Angew Chem 130:14021–14024. https://doi.org/10.1002/ange.201804409
Kim J, Lee SH, Tieves F, Paul CE, Hollmann F, Park CB (2019) Nicotinamide adenine dinucleotide as a photocatalyst. Sci Adv 5. https://doi.org/10.1126/sciadv.aax0501
König B, Kümmel S, Svobodová E, Cibulka R (2019) Flavin photocatalysis. Phys Sci Rev 3:1–17. https://doi.org/10.1515/psr-2017-0168
Lam Q, Cortez A, Nguyen TT, Kato M, Cheruzel L (2016) Chromogenic nitrophenolate-based substrates for light-driven hybrid P450 BM3 enzyme assay. J Inorg Biochem 158:86–91. https://doi.org/10.1016/j.jinorgbio.2015.12.005
Lauder K, Toscani A, Qi Y, Lim J, Charnock SJ, Korah K, Castagnolo D (2018) Photo-biocatalytic one-pot cascades for the enantioselective synthesis of 1,3-mercaptoalkanol volatile sulfur compounds. Angew Chem 130:5905–5909. https://doi.org/10.1002/ange.201802135
Lee SH, Kwon Y-C, Kim D-M, Park CB (2013) Cytochrome P450-catalyzed O-dealkylation coupled with photochemical NADPH regeneration. Biotechnol Bioeng 110:383–390. https://doi.org/10.1002/bit.24729
Lee JS, Nam DH, Kuk SK, Park CB (2014) Near-infrared-light-driven artificial photosynthesis by nanobiocatalytic assemblies. Chem A Eur J 20:3584–3588. https://doi.org/10.1002/chem.201400136
Lee SH, Choi DS, Pesic M, Lee YW, Paul CE, Hollmann F, Park CB (2017) Cofactor-free, direct photoactivation of enoate reductases for the asymmetric reduction of C=C bonds. Angew Chem Int Ed 56:8681–8685. https://doi.org/10.1002/anie.201702461
Lee SH, Choi DS, Kuk SK, Park CB (2018) Photobiocatalysis: activating redox enzymes by direct or indirect transfer of photoinduced electrons. Angew Chem Int Ed 57:7958–7985. https://doi.org/10.1002/anie.201710070
Lee C-Y, Zou J, Bullock J, Wallace GG (2019) Emerging approach in semiconductor photocatalysis: towards 3D architectures for efficient solar fuels generation in semi-artificial photosynthetic systems. J Photochem Photobiol C Photochem Rev 39:142–160
Lee BI, Chung YJ, Park CB (2019) Photosensitizing materials and platforms for light-triggered modulation of Alzheimer’s β-amyloid self-assembly. Biomaterials 190:121–132
Leisch H, Morley K, Lau PCK (2011) Baeyer−Villiger monooxygenases: more than just green chemistry. Chem Rev 111:4165–4222
Lill R (2009) Function and biogenesis of iron–sulphur proteins. Nature 460:831
Litman ZC, Wang Y, Zhao H, Hartwig JF (2018) Cooperative asymmetric reactions combining photocatalysis and enzymatic catalysis. Nature 560:355–359. https://doi.org/10.1038/s41586-018-0413-7
Losi A (2007) Flavin-based blue-light photosensors: a photobiophysics update. Photochem Photobiol 83:1283–1300
Lu C, Shen F, Wang S, Wang Y, Liu J, Bai WJ, Wang X (2018) An engineered self-sufficient biocatalyst enables scalable production of linear α-olefins from carboxylic acids. ACS Catal 8:5794–5798. https://doi.org/10.1021/acscatal.8b01313
Lubitz W, Ogata H, Rüdiger O, Reijerse E (2014) Hydrogenases. Chem Rev 114:4081–4148
Lubner CE, Applegate AM, Knörzer P, Ganago A, Bryant DA, Happe T, Golbeck JH (2011) Solar hydrogen-producing bionanodevice outperforms natural photosynthesis. Proc Natl Acad Sci U S A 108:20988–20991. https://doi.org/10.1073/pnas.1114660108
Maciá-Agulló JA, Corma A, Garcia H (2015) Photobiocatalysis: the power of combining photocatalysis and enzymes. Chem A Eur J 21:10940–10959. https://doi.org/10.1002/chem.201406437
Malito E, Alfieri A, Fraaije MW, Mattevi A (2004) Crystal structure of a Baeyer-Villiger monooxygenase. Proc Natl Acad Sci U S A 101:13157–13162. https://doi.org/10.1073/pnas.0404538101
Maurya SS, Nadar SS, Rathod VK (2020a) A rapid self-assembled hybrid bio-microflowers of alpha–amylase with enhanced activity. J Biotechnol 317:27–33. https://doi.org/10.1016/j.jbiotec.2020.04.010
Maurya SS, Nadar SS, Rathod VK (2020b) Dual activity of laccase-lysine hybrid organic–inorganic nanoflowers for dye decolourization. Environ Technol Innov 19:100798. https://doi.org/10.1016/j.eti.2020.100798
Mifsud M, Gargiulo S, Iborra S, Arends IWCE, Hollmann F, Corma A (2014a) Photobiocatalytic chemistry of oxidoreductases using water as the electron donor. Nat Commun 5. https://doi.org/10.1038/ncomms4145
Mifsud M, Gargiulo S, Iborra S, Arends IWCE, Hollmann F, Corma A (2014b) Photobiocatalytic chemistry of oxidoreductases using water as the electron donor. Nat Commun 5:1–6. https://doi.org/10.1038/ncomms4145
Monti D, Ottolina G, Carrea G, Riva S (2011) Redox reactions catalyzed by isolated enzymes. Chem Rev 111:4111–4140. https://doi.org/10.1021/cr100334x
Nadar SS, Vaidya L, Rathod VK (2020) Enzyme embedded metal organic framework (enzyme–MOF): De novo approaches for immobilization. Int J Biol Macromol 149:861–876. https://doi.org/10.1016/j.ijbiomac.2020.01.240
Nakamura K, Yamanaka R, Tohi K, Hamada H (2000) Cyanobacterium-catalyzed asymmetric reduction of ketones. Tetrahedron Lett 41:6799–6802. https://doi.org/10.1016/S0040-4039(00)01132-1
Nehme SI, Crocker L, Fruk L (2020) Flavin-conjugated iron oxide nanoparticles as enzyme-inspired photocatalysts for azo dye degradation. Catalysts 10:324. https://doi.org/10.3390/catal10030324
Park JH, Lee SH, Cha GS, Choi DS, Nam DH, Lee JH, Lee J-K, Yun C-H, Jeong KJ, Park CB (2015) Cofactor-free light-driven whole-cell cytochrome P450 catalysis. Angew Chem 127:983–987. https://doi.org/10.1002/ange.201410059
Parkin A, Goldet G, Cavazza C, Fontecilla-Camps JC, Armstrong FA (2008) The difference a Se makes? Oxygen-tolerant hydrogen production by the [NiFeSe]-hydrogenase from Desulfomicrobium baculatum. J Am Chem Soc 130:13410–13416
Patil PD, Yadav GD (2018) Rapid in situ encapsulation of laccase into metal-organic framework support (ZIF-8) under biocompatible conditions. Chem Sel 3:4669–4675. https://doi.org/10.1002/slct.201702852
Patil PD, Yadav GD (2019) Exploring the untapped potential of solar pretreatment for deconstruction of recalcitrant Kraft lignin in fungal biotransformation. Clean Technol Environ Policy 21:579–590. https://doi.org/10.1007/s10098-018-1656-6
Paul CE, Churakova E, Maurits E, Girhard M, Urlacher VB, Hollmann F (2014) In situ formation of H2O2 for P450 peroxygenases. Bioorg Med Chem 22:5692–5696
Pazmino DET, Dudek HM, Fraaije MW (2010) Baeyer-Villiger monooxygenases: recent advances and future challenges. Curr Opin Chem Biol 14:138–144
Peers MK, Toogood HS, Heyes DJ, Mansell D, Coe BJ, Scrutton NS (2016) Light-driven biocatalytic reduction of α, β-unsaturated compounds by ene reductases employing transition metal complexes as photosensitizers. Catal Sci Technol 6:169–177. https://doi.org/10.1039/c5cy01642h
Perez DI, Grau MM, Arends IWCE, Hollmann F (2009) Visible light-driven and chloroperoxidase-catalyzed oxygenation reactions. Chem Commun 44:6848–6850. https://doi.org/10.1039/b915078a
Pesic M, Fernández-Fueyo E, Hollmann F (2017) Characterization of the old yellow enzyme homolog from Bacillus subtilis (YqjM). Chem Select 2:3866–3871
Poulos TL (2014) Heme enzyme structure and function. Chem Rev 114:3919–3962
Qin P, Zhu H, Edvinsson T, Boschloo G, Hagfeldt A, Sun L (2008) Design of an organic chromophore for p-type dye-sensitized solar cells. J Am Chem Soc 130:8570–8571
Rauch MCR, Huijbers MME, Pabst M, Paul CE, Pešić M, Arends I, Hollmann F (2020) Photochemical regeneration of flavoenzymes—an old yellow enzyme case-study. Biochim Biophys Acta (BBA)-Proteins Proteomics 1868:140303
Reisner E, Powell DJ, Cavazza C, Fontecilla-Camps JC, Armstrong FA (2009) Visible light-driven H2 production by hydrogenases attached to dye-sensitized TiO2 nanoparticles. J Am Chem Soc 131:18457–18466
Romero E, Gómez Castellanos JR, Gadda G, Fraaije MW, Mattevi A (2018) Same substrate, many reactions: oxygen activation in flavoenzymes. Chem Rev 118:1742–1769
Roth LE, Nguyen JC, Tezcan FA (2010) ATP-and iron−protein-independent activation of nitrogenase catalysis by light. J Am Chem Soc 132:13672–13674
Sabuzi F, Churakova E, Galloni P, Wever R, Hollmann F, Floris B, Conte V (2015) Thymol bromination—a comparison between enzymatic and chemical catalysis. Eur J Inorg Chem 2015:3519–3525. https://doi.org/10.1002/ejic.201500086
Sakai T, Mersch D, Reisner E (2013) Photocatalytic hydrogen evolution with a hydrogenase in a mediator-free system under high levels of oxygen. Angew Chem Int Ed 52:12313–12316
Schmermund L, Jurkaš V, Özgen FF, Barone GD, Büchsenschütz HC, Winkler CK, Schmidt S, Kourist R, Kroutil W (2019) Photo-biocatalysis: biotransformations in the presence of light. ACS Catal 9:4115–4144. https://doi.org/10.1021/acscatal.9b00656
Schroeder L, Frese M, Müller C, Sewald N, Kottke T (2018) Photochemically driven biocatalysis of halogenases for the green production of chlorinated compounds. ChemCatChem 10:3336–3341. https://doi.org/10.1002/cctc.201800280
Seel CJ, Gulder T (2019) Biocatalysis fueled by light: on the versatile combination of photocatalysis and enzymes. ChemBioChem 20:1871–1897. https://doi.org/10.1002/cbic.201800806
Seel CJ, Králík A, Hacker M, Frank A, König B, Gulder T (2018) Atom-economic electron donors for photobiocatalytic halogenations. ChemCatChem 10:3960–3963. https://doi.org/10.1002/cctc.201800886
Shaik S, Munro AW, Sen S, Mowat C, Nam W, Derat E, Bugg T, Proshlyakov DA, Hausinger RP, Straganz GD (2011) Iron-containing enzymes: versatile catalysts of hydroxylation reactions in nature. Royal Society of Chemistry
Sono M, Roach MP, Coulter ED, Dawson JH (1996) Heme-containing oxygenases. Chem Rev 96:2841–2888
Sosa V, Melkie M, Sulca C, Li J, Tang L, Li J, Faris J, Foley B, Banh T, Kato M, Cheruzel LE (2018) Selective light-driven chemoenzymatic trifluoromethylation/hydroxylation of substituted arenes. ACS Catal 8:2225–2229. https://doi.org/10.1021/acscatal.7b04160
Stiborová M, Mikšanová M, Martínek V, Frei E (2000) Heme peroxidases: structure, function, mechanism and involvement in activation of carcinogens. A review. Collect Czechoslov Chem Commun 65:297–325
Taglieber A, Schulz F, Hollman F, Rusek M, Reetz MT (2008) Light-driven biocatalytic oxidation and reduction reactions: Scope and limitations. ChemBioChem 9:565–572. https://doi.org/10.1002/cbic.200700435
Toogood HS, Gardiner JM, Scrutton NS (2010) Biocatalytic reductions and chemical versatility of the old yellow enzyme family of flavoprotein oxidoreductases. ChemCatChem 2:892–914
Torkian L, Amereh E (2016) Nano sized Ni/TiO2 @ NaX zeolite with enhanced photocatalytic activity. J Nanostruct 6:307–311. https://doi.org/10.22052/jns.2016.34328
Torres Pazmiño DE, Snajdrova R, Baas B-J, Ghobrial M, Mihovilovic MD, Fraaije MW (2008) Self-sufficient Baeyer–Villiger monooxygenases: effective coenzyme regeneration for biooxygenation by fusion engineering. Angew Chem 120:2307–2310. https://doi.org/10.1002/ange.200704630
Tran NH, Huynh N, Bui T, Nguyen Y, Huynh P, Cooper ME, Cheruzel LE (2011) Light-initiated hydroxylation of lauric acid using hybrid P450 BM3 enzymes. Chem Commun 47:11936–11938. https://doi.org/10.1039/c1cc15124j
Tran NH, Nguyen D, Dwaraknath S, Mahadevan S, Chavez G, Nguyen A, Dao T, Mullen S, Nguyen TA, Cheruzel LE (2013) An efficient light-driven P450 BM3 biocatalyst. J Am Chem Soc 135:14484–14487. https://doi.org/10.1021/ja409337v
Tremblay PL, Xu M, Chen Y, Zhang T (2020) Nonmetallic abiotic-biological hybrid photocatalyst for visible water splitting and carbon dioxide reduction. iScience 23:100784. https://doi.org/10.1016/j.isci.2019.100784
Tseng TK, Lin YS, Chen YJ, Chu H (2010) A review of photocatalysts prepared by sol–gel method for VOCs removal. Int J Mol Sci 11(6):2336–2361. https://doi.org/10.3390/ijms11062336
Turner NJ (2018) Enzymes team up with light-activated catalysts. Nature 560:310–311. https://doi.org/10.1038/d41586-018-05933-0
Urlacher VB, Girhard M (2012) Cytochrome P450 monooxygenases: an update on perspectives for synthetic application. Trends Biotechnol 30:26–36
Urlacher VB, Girhard M (2019) Cytochrome P450 monooxygenases in biotechnology and synthetic biology. Trends Biotechnol 37(8):882
Urlacher VB, Lutz-Wahl S, Schmid RD (2004) Microbial P450 enzymes in biotechnology. Appl Microbiol Biotechnol 64:317–325
Vaidya LB, Nadar SS, Rathod VK (2020) Biological metal organic framework (bio-MOF) of glucoamylase with enhanced stability. Coll Surf B Biointerf 193:111052. https://doi.org/10.1016/j.colsurfb.2020.111052
Van Berkel WJH, Kamerbeek NM, Fraaije MW (2006) Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts. J Biotechnol 124:670–689
Van Schie MMCH, Paul CE, Arends IWCE, Hollmann F (2019) Photoenzymatic epoxidation of styrenes. Chem Commun 55:1790–1792. https://doi.org/10.1039/c8cc08149b
Walsh CT, Wencewicz TA (2013) Flavoenzymes: versatile catalysts in biosynthetic pathways. Nat Prod Rep 30:175–200
Whitehouse CJC, Bell SG, Wong LL (2012) P450 BM3 (CYP102A1): connecting the dots. Chem Soc Rev 41:1218–1260. https://doi.org/10.1039/c1cs15192d
Williams RE, Rathbone DA, Scrutton NS, Bruce NC (2004) Biotransformation of explosives by the old yellow enzyme family of flavoproteins. Appl Environ Microbiol 70:3566–3574
Willot SJP, Fernández-Fueyo E, Tieves F, Pesic M, Alcalde M, Arends IWCE, Park CB, Hollmann F (2019) Expanding the spectrum of light-driven peroxygenase reactions. ACS Catal 9:890–894. https://doi.org/10.1021/acscatal.8b03752
Winkler CK, Faber K, Hall M (2018) Biocatalytic reduction of activated CC-bonds and beyond: emerging trends. Curr Opin Chem Biol 43:97–105
Woolerton TW, Sheard S, Reisner E, Pierce E, Ragsdale SW, Armstrong FA (2010) Efficient and clean photoreduction of CO2 to CO by enzyme-modified TiO2 nanoparticles using visible light. J Am Chem Soc 132:2132–2133
Woolerton TW, Sheard S, Pierce E, Ragsdale SW, Armstrong FA (2011) CO2 photoreduction at enzyme-modified metal oxide nanoparticles. Energy Environ Sci 4:2393–2399
Yamanaka R, Nakamura K, Murakami M, Murakami A (2015) Selective synthesis of cinnamyl alcohol by cyanobacterial photobiocatalysts. Tetrahedron Lett 56:1089–1091. https://doi.org/10.1016/j.tetlet.2015.01.092
Yang Q, Zhao F, Zhang N, Liu M, Hu H, Zhang J, Zhou S (2018) Mild dynamic kinetic resolution of amines by coupled visible-light photoredox and enzyme catalysis. Chem Commun 54:14065–14068. https://doi.org/10.1039/c8cc07990k
Zachos I, Gaßmeyer SK, Bauer D, Sieber V, Hollmann F, Kourist R (2015) Photobiocatalytic decarboxylation for olefin synthesis. Chem Commun 51:1918–1921. https://doi.org/10.1039/c4cc07276f
Zanger UM, Schwab M (2013) Cytochrome P450 enzymes in drug metabolism: regulation of gene expression, enzyme activities, and impact of genetic variation. Pharmacol Ther 138:103–141
Zhang W, Fernández-Fueyo E, Ni Y, Van Schie M, Gacs J, Renirie R, Wever R, Mutti FG, Rother D, Alcalde M, Hollmann F (2018) Selective aerobic oxidation reactions using a combination of photocatalytic water oxidation and enzymatic oxyfunctionalizations. Nat Catal 1:55–62. https://doi.org/10.1038/s41929-017-0001-5
Zhang W, Ma M, Huijbers MME, Filonenko GA, Pidko EA, Van Schie M, De Boer S, Burek BO, Bloh JZ, Van Berkel WJH, Smith WA, Hollmann F (2019a) Hydrocarbon synthesis via photoenzymatic decarboxylation of carboxylic acids. J Am Chem Soc 141:3116–3120. https://doi.org/10.1021/jacs.8b12282
Zhang W, Fueyo EF, Hollmann F, Martin LL, Pesic M, Wardenga R, Höhne M, Schmidt S (2019b) Combining photo-organo redox- and enzyme catalysis facilitates asymmetric C–H bond functionalization. Eur J Org Chem 2019:80–84. https://doi.org/10.1002/ejoc.201801692
Zhao Y, Anderson NC, Ratzloff MW, Mulder DW, Zhu K, Turner JA, Neale NR, King PW, Branz HM (2016) Proton reduction using a hydrogenase-modified nanoporous black silicon photoelectrode. ACS Appl Mater Interfaces 8:14481–14487
Zhou J, Zhang Y, Zhao XS, Ray AK (2006) Photodegradation of benzoic acid over metal-doped TiO2. Indu Eng Chem Res 4:3503–3511
Zilly FE, Taglieber A, Schulz F, Hollmann F, Reetz MT (2009) Deazaflavins as mediators in light-driven cytochrome P450 catalyzed hydroxylations. Chem Commun 46:7152–7154. https://doi.org/10.1039/b913863c
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Patil, P.D., Nadar, S.S., Marghade, D.T. (2021). Photo-Enzymatic Green Synthesis: The Potential of Combining Photo-Catalysis and Enzymes. In: Inamuddin, Boddula, R., Ahamed, M.I., Khan, A. (eds) Advances in Green Synthesis. Advances in Science, Technology & Innovation. Springer, Cham. https://doi.org/10.1007/978-3-030-67884-5_9
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