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Yıl 2024, Cilt: 8 Sayı: 1, 18 - 24, 15.07.2024

Sara Taşkesenlioğlu

Öz

Kaynakça

  • [1]Klibanov AM. Improving Enzymes by Using Them in Organicmer Solvents. Nature(2001) 409:241–246.
  • [2]Bertini I, Luchinat C. The Reaction Pathways of Zinc Enzymes and Related Biological Catalysts, in Bioinorganic Chemistry: University Science Books (1994). 36–106.
  • [3]Bertini I, Drago RS, Luchinat C. The Coordination Chemistry of Metalloenzymes: The Role of Metals in Reactions Involving Water, Dioxygen and Related Species: D. Reidel Publishing Company (1982). 135–145.
  • [4]Bott AW. Redox Properties of Electron Transfer Metalloproteins18(1999). 47–54.
  • [5]Crabtree RH. The Organic Chemistry of Transition Metals: John Wiley& Sons Inc (2009). 436–464.
  • [6]Siegbahn P. Mechanisms of Metalloenzymes Studied by Quantum Chemical Metots. Q. Rev. Biophys(2003) 36:91–145.
  • [7]Kobayashi M, Shimizu S. Metalloenzyme nitrile hydratase: structure, regulation, and application to biotechnology. Nature Biotechnol(1998) 16:733–736.
  • [8]Kobayashi M, Shimizu S. Cobalt Proteins. Eur. J. Biochem(1999) 261:1–9.
  • [9]Holm RH, Kennepohl P, Solomon EI. Structural and Functional Aspects of Metal Sites in Biology. Chem. Rev(1996) 96:2239–2314.
  • [10]Riordan JF. The Role of Metals in Enzyme Activity. Ann Clin Lab Sci(2000) 7:119–129.
  • [11]O’Dell BL. Biochemistry and Physiology of Copper in Vertebrates. Trace Elements in Human Health and Disease, Zinc and Copper. New York: Academic Press (1976). 391–413.
  • [12]Prohaska JR. Biochemical changes in copper deficency. animals. J.Nutr. Biochem(1990) 1(9):452–461.
  • [13]Li TK, Vallee BL. The Biochemical and Nutritional Role of Trace Elements. Modem Nutrition in Health and Disease, Trace elements Section B(1973):372–399.[14]Boer JL, Mulrooney SB, Hausinger RP.Nickel-dependent Metalloenzymes. Arch of Biochem and Biophy(2014) 544:142–152.
  • [15]Tracey AS, Willsky GR, Takeuchi E. Biochemistry, Pharmacology and Practical Applications-Vanadium in Biological Systems. CRC Press(2007):152–170.
  • [16]Hille R. Molybdenum and tungsten in biology. TRENDS in Biochemical Sciences(2002) 27:360–367.
  • [17]Crichton RR. Biological Inorganic Chemistry, ISCN. Batiment Lavoisier(2012):323–342.
  • [18]Podgorsek A, Zupan M, Iskra J. Oxidative Halogenation with "Green" Oxidants: Oxygen and Hydrogen Peroxide. Angew. Chem. Int. Ed(2009) 48:8424–8450.
  • [19]Wittcoff HA, Reuben BG, Plotkin JS. Industrial organic chemicals. Hoboken N.J.: Wiley (2013). xxxvi, 807.
  • [20]Eissen M, Lenoir D. Electrophilic Bromination of Alkenes: Environmental, Health and Safety Aspects of New Alternative Metots. Chem-Eur J(2008) 14:9830–9841.
  • [21]Gunten UV, Oliveras Y. Kinetics of The Reactions Between Hydrogen Peroxide and Hypobromous Acid: Implication on Water Treatment and Natural Systems. Water Res(1997) 31:900–906.
  • [22]Dinesh CU, Kumar R, Pandey B, Kumar P. Catalytic Halogenation of Selected Organic-Compounds Mimicking Vanadate-Dependent Marine Metalloenzymes. J. Chem Soc-Chem Comm(1995) 6:611–612.
  • [23]Choudary BM, Sudha Y, Reddy PN. Regioselective Oxybromination of Activated Aromatic-Compounds Catalyzed by Ammonium Molybdate. Synlett(1994) 6:450.
  • [24]Neidleman SL, Geigert J. The enzymatic synthesis of heterogeneous dihalide derivatives: a unique biocatalytic discovery. Trends in Biotechnology(1983) 1(1):21–25.
  • [25]Murphy CD. New Frontiers in Biological Halogenation. J. Appl. Microbiol(2003) 94:539–548.
  • [26]Dembitsky VM. Oxidation, Epoxidation and Sulfoxidation Reactions Catalysed by Haloperoxidases. Tetrahedron(2002) 59:4701–4720. 24International Journal of Innovative Research and Reviews8(1) 18-24.
  • [27]Franssen M. Haloperoxidases-Useful Catalysts for Halogenation and Oxidation Reactions. Catal. Today(1994) 22:441–457.
  • [28]Vaillancourt FH, Yeh E, Vosburg DA, Garneau-Tsodikova S, Walsh CT. Nature’s Inventory of Halogenation Catalysts: Oxidative Strategies Predominate. Chem. Rev(2006) 106:3364–3378.
  • [29]van Pee KH, Dong CJ, Flecks S, Naismith J, Patallo EP, Wage T. Biological Halogenation has moved far beyond haloperoxidases. Adv. Appl. Microbiol(2006) 59:127–157.
  • [30]Franssen M, Vanboven HG, Vanderplas HC. Enzymatic Halogenation of Pyrazoles and Pyridine-Derivatives. J. Heterocyclic Chem(1987) 24:1313–1316.
  • [31]Duhalta RV, Ayala M, Marquez-Rochab FJ. Biocatalytic Chlorination of Aromatic Hydrocarbons by Chloroperoxidase of Caldariomyces Fumago. Phytochem(2001) 58:929–933.
  • [32]Vanschijndel J, Vollenbroek E, Wever R. The Chloroperoxidase from the Fungus Curvularia-Inaequalis -a Novel Vanadium Enzyme. Biochim. Biophys. Acta(1993) 1161:249–256.
  • [33]Krenn BE, Tromp M, Wever, R.The Brown Alga Ascophyllum-. Nodosum Contains 2 Different Vanadium Bromoperoxidases. J. Biolog. Chem(1989) 264:19287–19292.
  • [34]Deboer E, Tromp M, Plat H, Krenn GE, Wever R. Vanadium (V) as an Essential Element for Haloperoxidase Activity in Marine Brown Algae Purification and Characterization of a Vanadium(V)-Containing Bromoperoxidase from Laminaria-Saccharina. Biochim. Biophys. Acta(1986) 872:104–115.
  • [35]Deboer E, Plat H, Tromp M, Wever R, Franssen M, Vanderplas HC, et al. Vanadium Containing Bromoperoxidase -an Example of an Oxidoreductase with High Operational Stability in Aqueous and Organic Media. Biotechnol. Bioeng(1987) 30(5):607–610.
  • [36]Rehder D. Biological and Medicinal Aspects of Vanadium. Inorg Chem Commun(2003) 6:604–617.
  • [37]Butler A. Mechanistic Considerations of The Vanadium Haloperoxidases. Coord. Chem. Rev(1999) 187:17–35.
  • [38]Butler A, Walker JV. Marine haloperoxidases. Chem. Rev(1993) 93:1937–1944.
  • [39]Soedjak HS, Walker JV, Butler A. Inhibition and Inactivation of Vanadium Bromoperoxidase by The Substrate Hydrogen Peroxide and Further Mechanistic Studiest. Biochem(1995) 34:12689–12696.
  • [40]Forenza S, Minale L, Riccio R, Fattorusso E. New Bromo-pyrrole Derivatives from the Sponge Agelas Oroides. J. Chem. Soc. Chem(1971) Commun.18:1129–1130.
  • [41]Hartung J, Dumont Y, Greb M, Hach D, Köhler F, Schulz H, et al. On the reactivity of bromoperoxidase I(Ascophyllum nodosum) in buffered organicmedia: Formation of carbon bromine bonds. Pure Appl. Chem(2009) 81(7):1251–1264.
  • [42]Wischang D, Brücher O, Hartung. J.Bromoperoxidases and Functional Enzyme mimics as Catalysts for Oxidative Bromination-A Sustainable Synthetic Approach. Coord. Chem. Rev(2011) 255:2204–2217.
  • [43]Li M, Scheuer PJ. Halogenated Blue Pigments of a Deep Sea Gorgonian. Tetrahedron Lett(1984) 25:587–590.
  • [44]Smith TS, Pecoraro VL. Oxidation of organic sulfides by vanadium haloperoxidase model complexes. Inorg. Chem(2002) 41(25):6754–6760.
  • [45]Pushie MJ, Cotelesage JJ, George GN. Molybdenum and tungsten oxygen transferases –structural and functional diversity within a common active site motif. Metallomics(2014) 6(1):15–24.
  • [46]Cramer SP, Wahl R, Rajagopalan K. V.Molybdenum sites of Sulfite Oxidase and Xanthine Dehydrogenase. A comparison by EXAFS. J. Am. Chem. Soc(1981) 103:7721–7727.
  • [47]Hille R, Sprecher H. On the Mechanism of Action of Xanthine Oxidase. The Journal of Biologıcal Chemıstry(1987) 262:10914–10917.
  • [48]Hille R. The Mononuclear Molybdenum Enzymes. Chemical Reviews(1996) 96(7):2757–2816.
  • [49]Enemark JH, Cooney JA, Wang JJ, Holm RH. Synthetic Analogues and Reaction Systems Relevant to the Molybdenumand Tungsten Oxotransferases. Chem. Rev(2004) 104(1175).
  • [50]Ueyama N, Oku H, Kondo M, Okamura T, Yoshinaga N, Nakamura. A. trans Influence of Oxo and Dithiolene Coordination in Oxidized Models of Molybdenum Oxidoreductase: Synthesis, Structures, and Properties of Q2[MoVIO2(1,2-benzenedithiolato)2] (Q = NEt4, PPh4) and Related Complexes. Inorg. Chem(1996) 35:643–650.
  • [51]Oku H, Ueyama N, Kondo M, Nakamura A. Oxygen atom transfer systems in which the .mu.-oxodimolybdenum(V) complex formation does not occur: syntheses, structures, and reactivities of monooxomolybdenum(IV) benzenedithiolato complexes as models of molybdenum oxidoreductases. Inorganic Chemistry(1994) 33(2):209–216.
  • [52]Geibig D, Wilcken R, Bangesh M, Plass W. Transition Metal Centers in Biological Matrices: Why Nature Has Chosen Vanadate as Cofactor for Haloperoxidase. NIC Symposium-NIC Series(2008) 39(BN):978–3–9810843–5–1, 71–78.
  • [53]McEwan AG, Wetzstein HG, Ferguson SJ. Jackson Periplasmic location of the terminal reductase in trimethylamine N-oxide and dimethylsulphoxide respiration in the photosynthetic bacterium Rhodopseudomonas capsulata. J. B. Biochim. Biophys. Acta(1985) 806(3):410–417.
  • [54]Satoh T, Kurihara FN. Purification and Properties of Dimethylsulfoxide Reductase Containing a Molybdenum Cofactor from a Photodenitrifier, Rhodopseudomonas sphaeroides f.s. denitrificans, J. Biochem(1987) 102(1):191–197.
  • [55]Schultz BE, Holm RH. Kinetics of Oxygen Atom Transfer In An Analogue Reaction System of The Molybdenum Oxotransferases. Inorg. Chem.,(199332:4244–4248.
  • [56]George GN, Hilton J, Rajagopalan K. X-ray Absorption Spectroscopy of Dimethyl Sulfoxide Reductase from Rhodobacter sphaeroides. J. Am. Chem. Soc(1996) 118(5):1113–1117.
  • [57]Das SK, Chaudhury PK, Biswas D, Sarkar S. Modeling for the Active Site of Sulfite Oxidase: Synthesis,Characterization, and Reactivity of [MoVIC>2(mnt)2]2-(mnt2-=1,2-Dicyanoethylenedithiolate. J. Am. Chem. Soc(1994) 116:9061–9070.
  • [58]Hernanadez-Marin E, Ziegler T. A kinetic study of dimethyl sulfoxide reductase based on density functional theory, Can. J. Chem(2010) 88:683–693.
  • [59]George GN, Kipke CA, Prince RC, Sunde RA, Enemark JH, Cramer SP. Structure of The Active Site of Sulfite Oxidase. X-ray Absorption Spectroscopy of The Molybdenum (IV. Molybdenum(V), and Molybdenum(VI) Oxidation States. Biochemistry(1989) 28(12):5075–5080.
  • [60]Debnar-Daumler C, Seubert A, Schmitt G, Heider J. Simultaneous involvement of a tungsten-containing aldehyde:ferredoxin oxidoreductase and a phenylacetaldehyde dehydrogenase in anaerobic phenylalanine metabolism. J. of Bacteriol(2014) 196:483–492.
  • [61]Liao RZ, Yub JG, Himo F. Mechanism of Tungsten-dependent Acetylene Hydratase from Quantum Chemical Calculations. Proc. Natl. Acad. Sci(2010) 107:22523–22527.

The Role of Some Transition Metals in Enzymatic Reactions in Context of Eco-Friendly Oxidative Halogenation

Yıl 2024, Cilt: 8 Sayı: 1, 18 - 24, 15.07.2024

Sara Taşkesenlioğlu

Öz

Catalysts are a fundamental part of the chemical industry andtoday they are involved in the manufacture of approximately 90% of chemical-based products. Among the many types of catalysis, metal transfer catalysis is particularly important due to their ability ofto form various oxidation stages. Therefore,it opensup protocols that demonstrate unprecedented complexity, efficiency and selectivity compared to classical reactions. In nature, catalytic processes are mediated by enzymes. Many of all known enzymes require one or more metal ions for catalytic activity. The natural enzymes constitute the state of the art in catalysis and can perform a wide range of transformations with efficiency and selectivity that often exceed man-made systems. In recent years, with the discovery of naturally occurring metal-containing enzymes in various organisms, numerous studies have been conducted on the role of these enzymes in enzymatic reactions. As a result of these studies, researchers have focused on investigating the active roles of these metals in halogenation reactions and developing environmentally friendly metal-catalyzed halogenation reactions based on the presence of iron, vanadium, molybdenum, and tungsten in the structure of various haloperoxidases. This review summarizes the roles of some transition metals in biologicalsystems, as well as their functions of natural haloperoxidases and oxidative halogenation reactions.

Anahtar Kelimeler

Oxidative Halogenation Metal Catalyst Enzimatic Reactions Haloperoxidases

Kaynakça

  • [1]Klibanov AM. Improving Enzymes by Using Them in Organicmer Solvents. Nature(2001) 409:241–246.
  • [2]Bertini I, Luchinat C. The Reaction Pathways of Zinc Enzymes and Related Biological Catalysts, in Bioinorganic Chemistry: University Science Books (1994). 36–106.
  • [3]Bertini I, Drago RS, Luchinat C. The Coordination Chemistry of Metalloenzymes: The Role of Metals in Reactions Involving Water, Dioxygen and Related Species: D. Reidel Publishing Company (1982). 135–145.
  • [4]Bott AW. Redox Properties of Electron Transfer Metalloproteins18(1999). 47–54.
  • [5]Crabtree RH. The Organic Chemistry of Transition Metals: John Wiley& Sons Inc (2009). 436–464.
  • [6]Siegbahn P. Mechanisms of Metalloenzymes Studied by Quantum Chemical Metots. Q. Rev. Biophys(2003) 36:91–145.
  • [7]Kobayashi M, Shimizu S. Metalloenzyme nitrile hydratase: structure, regulation, and application to biotechnology. Nature Biotechnol(1998) 16:733–736.
  • [8]Kobayashi M, Shimizu S. Cobalt Proteins. Eur. J. Biochem(1999) 261:1–9.
  • [9]Holm RH, Kennepohl P, Solomon EI. Structural and Functional Aspects of Metal Sites in Biology. Chem. Rev(1996) 96:2239–2314.
  • [10]Riordan JF. The Role of Metals in Enzyme Activity. Ann Clin Lab Sci(2000) 7:119–129.
  • [11]O’Dell BL. Biochemistry and Physiology of Copper in Vertebrates. Trace Elements in Human Health and Disease, Zinc and Copper. New York: Academic Press (1976). 391–413.
  • [12]Prohaska JR. Biochemical changes in copper deficency. animals. J.Nutr. Biochem(1990) 1(9):452–461.
  • [13]Li TK, Vallee BL. The Biochemical and Nutritional Role of Trace Elements. Modem Nutrition in Health and Disease, Trace elements Section B(1973):372–399.[14]Boer JL, Mulrooney SB, Hausinger RP.Nickel-dependent Metalloenzymes. Arch of Biochem and Biophy(2014) 544:142–152.
  • [15]Tracey AS, Willsky GR, Takeuchi E. Biochemistry, Pharmacology and Practical Applications-Vanadium in Biological Systems. CRC Press(2007):152–170.
  • [16]Hille R. Molybdenum and tungsten in biology. TRENDS in Biochemical Sciences(2002) 27:360–367.
  • [17]Crichton RR. Biological Inorganic Chemistry, ISCN. Batiment Lavoisier(2012):323–342.
  • [18]Podgorsek A, Zupan M, Iskra J. Oxidative Halogenation with "Green" Oxidants: Oxygen and Hydrogen Peroxide. Angew. Chem. Int. Ed(2009) 48:8424–8450.
  • [19]Wittcoff HA, Reuben BG, Plotkin JS. Industrial organic chemicals. Hoboken N.J.: Wiley (2013). xxxvi, 807.
  • [20]Eissen M, Lenoir D. Electrophilic Bromination of Alkenes: Environmental, Health and Safety Aspects of New Alternative Metots. Chem-Eur J(2008) 14:9830–9841.
  • [21]Gunten UV, Oliveras Y. Kinetics of The Reactions Between Hydrogen Peroxide and Hypobromous Acid: Implication on Water Treatment and Natural Systems. Water Res(1997) 31:900–906.
  • [22]Dinesh CU, Kumar R, Pandey B, Kumar P. Catalytic Halogenation of Selected Organic-Compounds Mimicking Vanadate-Dependent Marine Metalloenzymes. J. Chem Soc-Chem Comm(1995) 6:611–612.
  • [23]Choudary BM, Sudha Y, Reddy PN. Regioselective Oxybromination of Activated Aromatic-Compounds Catalyzed by Ammonium Molybdate. Synlett(1994) 6:450.
  • [24]Neidleman SL, Geigert J. The enzymatic synthesis of heterogeneous dihalide derivatives: a unique biocatalytic discovery. Trends in Biotechnology(1983) 1(1):21–25.
  • [25]Murphy CD. New Frontiers in Biological Halogenation. J. Appl. Microbiol(2003) 94:539–548.
  • [26]Dembitsky VM. Oxidation, Epoxidation and Sulfoxidation Reactions Catalysed by Haloperoxidases. Tetrahedron(2002) 59:4701–4720. 24International Journal of Innovative Research and Reviews8(1) 18-24.
  • [27]Franssen M. Haloperoxidases-Useful Catalysts for Halogenation and Oxidation Reactions. Catal. Today(1994) 22:441–457.
  • [28]Vaillancourt FH, Yeh E, Vosburg DA, Garneau-Tsodikova S, Walsh CT. Nature’s Inventory of Halogenation Catalysts: Oxidative Strategies Predominate. Chem. Rev(2006) 106:3364–3378.
  • [29]van Pee KH, Dong CJ, Flecks S, Naismith J, Patallo EP, Wage T. Biological Halogenation has moved far beyond haloperoxidases. Adv. Appl. Microbiol(2006) 59:127–157.
  • [30]Franssen M, Vanboven HG, Vanderplas HC. Enzymatic Halogenation of Pyrazoles and Pyridine-Derivatives. J. Heterocyclic Chem(1987) 24:1313–1316.
  • [31]Duhalta RV, Ayala M, Marquez-Rochab FJ. Biocatalytic Chlorination of Aromatic Hydrocarbons by Chloroperoxidase of Caldariomyces Fumago. Phytochem(2001) 58:929–933.
  • [32]Vanschijndel J, Vollenbroek E, Wever R. The Chloroperoxidase from the Fungus Curvularia-Inaequalis -a Novel Vanadium Enzyme. Biochim. Biophys. Acta(1993) 1161:249–256.
  • [33]Krenn BE, Tromp M, Wever, R.The Brown Alga Ascophyllum-. Nodosum Contains 2 Different Vanadium Bromoperoxidases. J. Biolog. Chem(1989) 264:19287–19292.
  • [34]Deboer E, Tromp M, Plat H, Krenn GE, Wever R. Vanadium (V) as an Essential Element for Haloperoxidase Activity in Marine Brown Algae Purification and Characterization of a Vanadium(V)-Containing Bromoperoxidase from Laminaria-Saccharina. Biochim. Biophys. Acta(1986) 872:104–115.
  • [35]Deboer E, Plat H, Tromp M, Wever R, Franssen M, Vanderplas HC, et al. Vanadium Containing Bromoperoxidase -an Example of an Oxidoreductase with High Operational Stability in Aqueous and Organic Media. Biotechnol. Bioeng(1987) 30(5):607–610.
  • [36]Rehder D. Biological and Medicinal Aspects of Vanadium. Inorg Chem Commun(2003) 6:604–617.
  • [37]Butler A. Mechanistic Considerations of The Vanadium Haloperoxidases. Coord. Chem. Rev(1999) 187:17–35.
  • [38]Butler A, Walker JV. Marine haloperoxidases. Chem. Rev(1993) 93:1937–1944.
  • [39]Soedjak HS, Walker JV, Butler A. Inhibition and Inactivation of Vanadium Bromoperoxidase by The Substrate Hydrogen Peroxide and Further Mechanistic Studiest. Biochem(1995) 34:12689–12696.
  • [40]Forenza S, Minale L, Riccio R, Fattorusso E. New Bromo-pyrrole Derivatives from the Sponge Agelas Oroides. J. Chem. Soc. Chem(1971) Commun.18:1129–1130.
  • [41]Hartung J, Dumont Y, Greb M, Hach D, Köhler F, Schulz H, et al. On the reactivity of bromoperoxidase I(Ascophyllum nodosum) in buffered organicmedia: Formation of carbon bromine bonds. Pure Appl. Chem(2009) 81(7):1251–1264.
  • [42]Wischang D, Brücher O, Hartung. J.Bromoperoxidases and Functional Enzyme mimics as Catalysts for Oxidative Bromination-A Sustainable Synthetic Approach. Coord. Chem. Rev(2011) 255:2204–2217.
  • [43]Li M, Scheuer PJ. Halogenated Blue Pigments of a Deep Sea Gorgonian. Tetrahedron Lett(1984) 25:587–590.
  • [44]Smith TS, Pecoraro VL. Oxidation of organic sulfides by vanadium haloperoxidase model complexes. Inorg. Chem(2002) 41(25):6754–6760.
  • [45]Pushie MJ, Cotelesage JJ, George GN. Molybdenum and tungsten oxygen transferases –structural and functional diversity within a common active site motif. Metallomics(2014) 6(1):15–24.
  • [46]Cramer SP, Wahl R, Rajagopalan K. V.Molybdenum sites of Sulfite Oxidase and Xanthine Dehydrogenase. A comparison by EXAFS. J. Am. Chem. Soc(1981) 103:7721–7727.
  • [47]Hille R, Sprecher H. On the Mechanism of Action of Xanthine Oxidase. The Journal of Biologıcal Chemıstry(1987) 262:10914–10917.
  • [48]Hille R. The Mononuclear Molybdenum Enzymes. Chemical Reviews(1996) 96(7):2757–2816.
  • [49]Enemark JH, Cooney JA, Wang JJ, Holm RH. Synthetic Analogues and Reaction Systems Relevant to the Molybdenumand Tungsten Oxotransferases. Chem. Rev(2004) 104(1175).
  • [50]Ueyama N, Oku H, Kondo M, Okamura T, Yoshinaga N, Nakamura. A. trans Influence of Oxo and Dithiolene Coordination in Oxidized Models of Molybdenum Oxidoreductase: Synthesis, Structures, and Properties of Q2[MoVIO2(1,2-benzenedithiolato)2] (Q = NEt4, PPh4) and Related Complexes. Inorg. Chem(1996) 35:643–650.
  • [51]Oku H, Ueyama N, Kondo M, Nakamura A. Oxygen atom transfer systems in which the .mu.-oxodimolybdenum(V) complex formation does not occur: syntheses, structures, and reactivities of monooxomolybdenum(IV) benzenedithiolato complexes as models of molybdenum oxidoreductases. Inorganic Chemistry(1994) 33(2):209–216.
  • [52]Geibig D, Wilcken R, Bangesh M, Plass W. Transition Metal Centers in Biological Matrices: Why Nature Has Chosen Vanadate as Cofactor for Haloperoxidase. NIC Symposium-NIC Series(2008) 39(BN):978–3–9810843–5–1, 71–78.
  • [53]McEwan AG, Wetzstein HG, Ferguson SJ. Jackson Periplasmic location of the terminal reductase in trimethylamine N-oxide and dimethylsulphoxide respiration in the photosynthetic bacterium Rhodopseudomonas capsulata. J. B. Biochim. Biophys. Acta(1985) 806(3):410–417.
  • [54]Satoh T, Kurihara FN. Purification and Properties of Dimethylsulfoxide Reductase Containing a Molybdenum Cofactor from a Photodenitrifier, Rhodopseudomonas sphaeroides f.s. denitrificans, J. Biochem(1987) 102(1):191–197.
  • [55]Schultz BE, Holm RH. Kinetics of Oxygen Atom Transfer In An Analogue Reaction System of The Molybdenum Oxotransferases. Inorg. Chem.,(199332:4244–4248.
  • [56]George GN, Hilton J, Rajagopalan K. X-ray Absorption Spectroscopy of Dimethyl Sulfoxide Reductase from Rhodobacter sphaeroides. J. Am. Chem. Soc(1996) 118(5):1113–1117.
  • [57]Das SK, Chaudhury PK, Biswas D, Sarkar S. Modeling for the Active Site of Sulfite Oxidase: Synthesis,Characterization, and Reactivity of [MoVIC>2(mnt)2]2-(mnt2-=1,2-Dicyanoethylenedithiolate. J. Am. Chem. Soc(1994) 116:9061–9070.
  • [58]Hernanadez-Marin E, Ziegler T. A kinetic study of dimethyl sulfoxide reductase based on density functional theory, Can. J. Chem(2010) 88:683–693.
  • [59]George GN, Kipke CA, Prince RC, Sunde RA, Enemark JH, Cramer SP. Structure of The Active Site of Sulfite Oxidase. X-ray Absorption Spectroscopy of The Molybdenum (IV. Molybdenum(V), and Molybdenum(VI) Oxidation States. Biochemistry(1989) 28(12):5075–5080.
  • [60]Debnar-Daumler C, Seubert A, Schmitt G, Heider J. Simultaneous involvement of a tungsten-containing aldehyde:ferredoxin oxidoreductase and a phenylacetaldehyde dehydrogenase in anaerobic phenylalanine metabolism. J. of Bacteriol(2014) 196:483–492.
  • [61]Liao RZ, Yub JG, Himo F. Mechanism of Tungsten-dependent Acetylene Hydratase from Quantum Chemical Calculations. Proc. Natl. Acad. Sci(2010) 107:22523–22527.
Toplam 60 adet kaynakça vardır.

Ayrıntılar

Birincil Dil İngilizce
Konular Moleküler ve Organik Elektronik
Bölüm Reviews
Yazarlar

Sara Taşkesenlioğlu

Yayımlanma Tarihi 15 Temmuz 2024
Gönderilme Tarihi 8 Ocak 2024
Kabul Tarihi 11 Haziran 2024
Yayımlandığı Sayı Yıl 2024 Cilt: 8 Sayı: 1

Kaynak Göster

APA Taşkesenlioğlu, S. (2024). The Role of Some Transition Metals in Enzymatic Reactions in Context of Eco-Friendly Oxidative Halogenation. International Journal of Innovative Research and Reviews, 8(1), 18-24.
 Kapak Resmi İndir