ΠΠ·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ ΠΊΠΎΠ±Π°Π»Π°ΠΌΠΈΠ½ΠΎΠ² ΠΈ ΠΊΠΎΠ±ΠΈΠ½Π°ΠΌΠΈΠ΄Π° Ρ ΡΠ΅ΡΠΎΡΠΎΠ΄Π΅ΡΠΆΠ°ΡΠΈΠΌΠΈ Π²ΠΎΡΡΡΠ°Π½ΠΎΠ²ΠΈΡΠ΅Π»ΡΠΌΠΈ, ΡΠΈΠΎΡΠΈΠ°Π½Π°ΡΠΎΠΌ ΠΈ ΠΌΠΎΠ½ΠΎ-ΡΠ°Ρ Π°ΡΠΈΠ΄Π°ΠΌΠΈ
ΠΠΈΡΡΠ΅ΡΡΠ°ΡΠΈΡ
ΠΠ·ΡΡΠ΅Π½ΠΎ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ Π‘ΠΎ (Π¨) ΠΈ Π‘ΠΎ (Π)-ΡΠΎΡΠΌ ΠΊΠΎΠ±Π°Π»Π°ΠΌΠΈΠ½Π° ΠΈ ΠΊΠΎΠ±ΠΈΠ½Π°ΠΌΠΈΠ΄Π° Ρ ΡΠΈΠΎΡΠΈΠ°Π½Π°ΡΠΎΠΌ, ΠΎΠΏΡΠ΅Π΄Π΅Π»Π΅Π½Ρ ΠΊΠΈΠ½Π΅ΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΏΠ°ΡΠ°ΠΌΠ΅ΡΡΡ ΡΠ΅Π°ΠΊΡΠΈΠΉ. ΠΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ ΡΠΈΠΎΡΠΈΠ°Π½Π°Ρ ΡΡΡΠ΅ΡΡΠ²Π΅Π½Π½ΠΎ Π·Π°ΠΌΠ΅Π΄Π»ΡΠ΅Ρ ΡΠ²ΡΠ·ΡΠ²Π°Π½ΠΈΠ΅ ΡΠΈΠ°Π½ΠΈΠ΄Π° ΠΊΠΎΠ±Π°Π»Π°ΠΌΠΈΠ½ΠΎΠΌ (Π¨), ΠΎΠ΄Π½Π°ΠΊΠΎ Π½Π΅ Π²Π»ΠΈΡΠ΅Ρ Π½Π° ΡΠ΅Π°ΠΊΡΠΈΡ ΠΊΠΎΠ±ΠΈΠ½Π°ΠΌΠΈΠ΄Π° (III) Ρ ΡΠΈΠ°Π½ΠΈΠ΄ΠΎΠΌ. ΠΠ΅ΡΠΎΠ΄Π°ΠΌΠΈ ΡΠ»Π΅ΠΊΡΡΠΎΠ½Π½ΠΎΠΉ ΡΠΏΠ΅ΠΊΡΡΠΎΡΠΊΠΎΠΏΠΈΠΈ ΠΈ ΡΠ»Π΅ΠΊΡΡΠΎΠ½Π½ΠΎΠ³ΠΎ ΠΏΠ°ΡΠ°ΠΌΠ°Π³Π½ΠΈΡΠ½ΠΎΠ³ΠΎ ΡΠ΅Π·ΠΎΠ½Π°Π½ΡΠ° Π΄ΠΎΠΊΠ°Π·Π°Π½ΠΎ ΠΎΠ±ΡΠ°Π·ΠΎΠ²Π°Π½ΠΈΠ΅ Π³Π΅ΠΊΡΠ°ΠΊΠΎΠΎΡΠ΄ΠΈΠ½Π°ΡΠΈΠΎΠ½Π½ΠΎΠ³ΠΎ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠ°… Π§ΠΈΡΠ°ΡΡ Π΅ΡΡ >
Π‘ΠΏΠΈΡΠΎΠΊ Π»ΠΈΡΠ΅ΡΠ°ΡΡΡΡ
- Matthews, R.G. Cobalamin- and Corrinoid-Dependent Enzymes/ R.G. Matthews // Met. Ions Life Sci. 2009. — V. 6. — P. 53−114.
- Vitamin Bi2 and Redox Homeostasis: Cob (II)alamin Reacts with Superoxide at Rates Approaching Superoxide Dismutase (SOD)/ E. Suarez-Moreira, J. Yun, C.S. Birch, J.H. Williams, A. McCaddon, N.E. Brasch // J. Am. Chem. Soc. 2009. — V. 131.-P. 15 078−15 079.
- Kinetics and Mechanism of the Reversible Binding of Nitric Oxide to Reduced Cobalamin Bi2r (Cob (II)alamin)/ M. Wolak, A. Zahl, T. Schneppensieper, G. Stochel, R. van Eldik// J. Am. Chem. Soc.-2001.-V. 123.-P. 9780−9791.
- Mukherjee, R. Kinetic Studies on the Reaction between Cob (I)alamin and Peroxynitrite: Rapid Oxidation of Cob (I)alamin to Cob (II)alamin by Peroxynitrous Acid/ R. Mukherjee, N.E. Brasch // Chem. Eur. J. 2011. — V. 17. — P. 1 172 311 727.
- Kinetic and Mechanistic Studies on the Reactions of the Reduced Vitamin Bi2 Complex Cob (I)alamin with Nitrite and Nitrate/ N.T. Plymale, R.S. Dassanayake, H.A. Hassanin, N.E. Brasch // Eur. J. Inorg. Chem. 2012. — P. 913−921.
- A novel role for vitamin B12: Cobalamins are intracellular antioxidants in vitro/ C.S. Birch, N.E. Brasch, A. McCaddon, J.H. Williams // Free Radic. Biol. Med. 2009. -V. 47.-P. 184−188.
- Cobinamide is superior to other treatments in a mouse model of cyanide poisoning/ A. Chan, M. Balasubramanian, W. Blackledge, O.M. Mohammad, L. Alvarez, G.R. Boss, T.D. Bigby // Clin. Toxicol. 2010. — V. 48. — P. 709−717.
- Structure of vitamin Bi2 / D.C. Hodgkin, J. Kamper, M. Mackay, J. Pickworth, K.N. Trueblood, J.G. White // Nature. 1956. — V. 178. — P. 64−66.
- Accurate assessment and identification of naturally occurring cellular cobalamins/ L. Hannibal, A. Axhemi, A.V. Glushchenko, E.S. Moreira, N.E. Brasch, D.W. Jacobsen // Clin. Chem. Lab. Med. 2008. — V. 46. — P. 1739−1746.
- Brown, K.L. Chemistry and Enzymology of Vitamin Bi2 / K.L. Brown // Chem. Rev. 2005. -V. 105. — P. 2075−2149.
- Burke, S.A. Clustered Genes Encoding the Methyltransferases of Methanogenesis from Monomethylamine/ S.A. Burke, S.L. Lo, J.A. Krzycki // J. Bacteriol. 1998. -V. 180.-P. 3432−3440.
- Olteanu, H. Human Methionine Synthase Reductase, a Soluble P-450 Reductase-like Dual Flavoprotein, Is Sufficient for NADPH-dependent Methionine Synthase Activation/ H. Olteanu, R. Banerjee // J. Biol. Chem. 2001. — V. 276. — P. 3 555 835 563.
- Brown, K.L. The enzymatic activation of coenzyme B.2/ K.L. Brown // Dalton Trans. 2006. — P. 1123−1133.
- Spectroscopic and Computational Studies on the Adenosylcobalamin-Dependent
- Methylmalonyl-CoA Mutase: Evaluation of Enzymatic Contributions to Co-C Bondl i
- Activation in the Co Ground State/ A.J. Brooks, M. Vlasie, R. Banerjee, T.C. Brunold// J. Am. Chem. Soc. -2004. V. 126.-P. 8167−8180.
- Spectroscopic Evidence for the Formation of a Four-Coordinate Co Cobalamin Species upon Binding to the Human ATP: Cobalamin Adenosyltransferase/ T.A. Stich, M. Yamanishi, R. Banerjee, T.C. Brunold // J. Am. Chem. Soc. 2005. — V. 127.-P. 7660−7661.
- Thompson, J.P. Hydroxocobalamin in cyanide poisoning/ J.P. Thompson, T.C. Marrs // Clin. Toxicol. 2012. — V. 50. — P. 875−885.
- Cyanide Detoxification by the Cobalamin Precursor Cobinamide/ K.E. Broderick, P. Potluri, S. Zhuang, I.E. Scheffler, V.S. Sharma, R.B. Pilz, G.R. Boss // Exp. Biol. Med. 2006. — V. 231. — P. 641−649.
- Broderick, K.E. Nitric Oxide Scavenging by the Cobalamin Precursor Cobinamide/ K.E. Broderick, V. Singh, S. Zhuang, A. Kambo, J.C. Chen, V.S. Sharma, R.B. Pilz, G.R. Boss // J. Biol. Chem. 2005. — V. 280. — P. 8678−8685.
- George, P. The Influence of Chelation in Determining thet Reactivity of the Iron in Hemoproteins, and the Cobalt in Vitamin Bi2 Derivatives/ P. George, D.H. Irvine, S.C. Glauser // Ann. N. Y. Acad. Sci. 1960. -V. 88. -P. 393−415.
- Mannel-Croise, C. A Straightforward Method for the Colorimetric Detection of Endogenous Biological Cyanide/ C. Mannel-Croise, B. Probst, F. Zelder // Anal. Chem. 2009. — V. 81. — P. 9493−9498.
- A disposable blood cyanide sensor/ Y. Tian, P.K. Dasgupta, S.B. Mahon, J. Ma, M. Brenner, J.-H. Wang, G.R. Boss // Anal. Chim. Acta. 2013. — V. 768. — P. 129−135.
- Mannel-Croise, C. Rapid visual detection of blood cyanide/ C. Mannel-Croise, F. Zelder // Anal. Methods. 2012. — V. 4. — P. 2632−2634.
- Mannel-Croise, C. Complex Samples Cyanide Detection with Immobilized Corrinoids/ C. Mannel-Croise, F. Zelder // ACS Appl. Mater. Interfaces. 2012. -V. 4. — P. 725−729.
- Cobinamide chemistries for photometric cyanide determination. A merging zone liquid core waveguide cyanide analyzer using cyanoaquacobinamide/ J. Ma, P.K. Dasgupta, F.H. Zelder, G.R. Boss // Anal. Chim. Acta. 2012. — V. 736. — P. 78−84.
- Reaction of Nitric Oxide with Vitamin Bi2 and Its Precursor, Cobinamide/ V.S. Sharma, R.B. Pilz, G.R. Boss, D. Magde // Biochemistry. 2003. — V. 42. — P. 89 008 908.
- Five-Coordination and Adduct Formation in Com-Corrinoids Dissecting Ligand Substitution into Its Component Steps/ M.S.A. Hamza, R. van Eldik, P.L.S. Harper, J.M. Pratt, E.A. Betterton // Eur. J. Inorg. Chem. 2002. — P. 580−583.
- Meier, M. Ligand-Substitution Reactions of Aquacobalamin (Vitamin Bi2a) Revisited. Conclusive Evidence for the Operation of a Dissociative Interchange Mechanism/ M. Meier, R. van Eldik // Inorg. Chem. 1993. — V. 32. — P. 26 352 639.
- Marques, H.M. Factors affecting the rate of ligand substitution reactions of aquacobalamin (vitamin Bi2a)/ H.M. Marques, L. Knapton // J. Chem. Soc., Dalton Trans. 1997. — P. 3827−3833.
- Detailed kinetic and thermodynamic studies on the cyanation of alkylcobalamins. A generalized mechanistic description/ M.S.A. Hamza, X. Zou, K.L. Brown, R. van Eldik // J. Chem. Soc., Dalton Trans. 2002. — P. 3832−3839.
- The Ligand-substitution Reactions of Aquahydroxocobinamide Proceed Through a Dissociative Interchange Mechdnism/ H.M. Marques, J.C. Bradley, K.L. Brown, H. Brooks // J. Chem. Soc., Dalton Trans. 1993. — P. 3475−3478.
- Trans and cis influences and effects in cobalamins and in their simple models/ M. De March, N. Demitri, S. Geremia, N. Hickey, L. Randaccio // J. Inorg. Biochem. -2012.-V. 116.-P. 215−227.
- Mechanistic Studies on the Reaction between R2N-NONOates and Aquacobalamin: Evidence for Direct Transfer of a Nitroxyl Group from R2N-NONOates to
- Cobalt (III) Centers/ H.A. Hassanin, L. Hannibal, D.W. Jacobsen, M.F. El-Shahat, M.S.A. Hamza, N.E. Brasch // Angew. Chem. Int. Ed. 2009. — V. 48. — P. 89 098 913.
- Perry, C.B. Probing the eis and trans Influence in Cobalamin Chemistry by Electronic Spectroscopy/ C.B. Perry, H.M. Marques // S. Afr. J. Chem. 2005. — V.58.-P. 9−15.
- Linn, D.E. Jr. Electron Transfer. 92. Reductions of Vitamin Bi2a (Hydroxocobalamin) with Formate and Related Formyl Species/ D.E. Linn, Jr., E.S. Gould//Inorg. Chem. 1988. -V. 27. — P. 1625−1628.
- Lexa, D. The Elecrochemistry of Vitamin Bi2/ D. Lexa, J.-M. Saveant // Acc. Chem. Res. 1983. — V. 16. — P. 235−243.
- Electroreduction of a Series of Alkylcobalamins: Mechanism of Stepwise Reductive Cleavage of the Co-C Bond/ R.L. Birke, Q. Huang, T. Spataru, D.K. Gosser, Jr. // J. Am. Chem. Soc. 2006. — 128. — P. 1922−1936.
- Kumar, M. Computational Modeling of Standard Reduction Potentials of BJ2 Cofactors // M. Kumar, W. Galezowski, P.M. Kozlowski // Int. J. Quantum Chem. -2013.-V. 113.-P. 479−488.
- Krautler, B. Coenzyme B12 Chemistry: The Crystal and Molecular Structure of Cob (II)alamin/ B. Krautler, W. Keller, C. Kratky // J. Am. Chem. Soc. 1989. — V. 111.-P. 8936−8938.
- Axial Solvent Coordination in «Base-Off' Cob (II)alamin and Related Co (II)-Corrinates Revealed by 2D-EPR/ S. Van Doorslaer, G. Jeschke, B. Epel, D.
- Goldfarb, R.-A. Eichel, B. Krautler, A. Schweiger // J. Am. Chem. Soc. 2003. — V. 125.-P. 5915−5927.
- In situ X-ray absorption spectroelectrochemical study of hydroxocobalamin/ M. Giorgetti, I. Ascone, M. Berrettoni, P. Conti, S. Zamponi, R. Marassi // J. Biol. Inorg. Chem. 2000. — V. 5 — P. 156−166.
- Electron Paramagnetic Resonance Studies of Cob (II)alamin and Cob (II)inamides/ J.H. Bayston, F.D. Looney, J.R. Pilbrow, M.E. Winfield // Biochemistry. 1970. -V. 9.-P. 2164−2172.
- The Chemistry of Vitamin B12. Part XVI. Binding of Thiols to the Cobalt (II) Corrins/ S. Cockle, H.A.O. Hill, S. Ridsdale, RJ.P. Williams // J. Chem. Soc., Dalton Trans. 1972. — P. 297−302.
- Cobalamin reduction by dithionite. Evidence for the formation of a six-coordinate cobalamin (II) complex/ D.S. Salnikov, R. Silaghi-Dumitrescu, S.V. Makarov, R. van Eldik, G.R. Boss // Dalton Trans. 2011. — V. 40. — P. 9831 — 9834.
- Acid-Base Properties of a-Ribazole and the Thermodynamics of Dimethylbenzimidazole Association in Alkylcobalamins/ K.L. Brown, J.M. Hakimi, D.M. Nuss, Y.D. Montejano, D.W. Jacobsen // Inorg. Chem. 1984. — V. 23. -1463−1471.
- Nitroxylcob (III)alamin: Synthesis and X-ray Structural Characterization/ L. Hannibal, C.A. Smith, D.W. Jacobsen, N.E. Brasch // Angew. Chem. Int. Ed. 2007. -V. 46.-P. 5140−5143.
- Nitric Oxide Inhibits Mammalian Methylmalonyl-CoA Mutase/ A. Kambo, V.S. Sharma, D.E. Casteel, V. L. Woods, Jr., R.B. Pilz, G.R. Boss // J. Biol. Chem. -2005.-V. 280.-P. 10 073−10 082.
- Nitric oxide interactions with cobalamins: biochemical and functional consequences/ M. Brouwer, W. Chamulitrat, G. Ferruzzi, D.L. Sauls, J.B. Weinberg/ Blood. 1996. -V. 88.-P. 1857−1864.
- Jiang, F. Effect of hydroxocobalamin on vasodilatations to nitrergic transmitter, nitric oxide and endothelium-derived relaxing factor in guinea-pig basilar artery/ F. Jiang, C.G. Li, M. J. Rand // Eur. J. Pharmacol. 1997. — V. 340. — P. 181−186.
- Folic acid rescues nitric oxide-induced neural tube closure defects/ M. Weil, R. Abeles, A. Nachmany, V. Gold, E. Michael // Cell Death Differ. 2004. -V. 11. — P. 361−363.
- Wolak, M. Reactivity of Aquacobalamin and Reduced Cobalamin toward S-Nitrosoglutathione and S-Nitroso-N-acetylpenicillamine/ M. Wolak, G. Stochel, R. vanEldik// Inorg. Chem. 2006.-V. 45.-P. 1367−1379.
- Liptak, M.D. Spectroscopic and Computational Studies of Co1+Cobalamin: Spectral and Electronic Properties of the „Superreduced“ B.2 Cofactor / M.D. Liptak, T.C. Brunold // J.Am.Chem.Soc. 2006. — V. 128. — P. 9144−9156.
- ΠΠ³Π΅Π΅Π²Π°, E.C. ΠΠ·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ Π½ΠΈΡΡΠΈΡΠ° Ρ ΡΠ΅ΡΠΎΡΠΎΠ΄Π΅ΡΠΆΠ°ΡΠΈΠΌΠΈ Π²ΠΎΡΡΡΠ°Π½ΠΎΠ²ΠΈΡΠ΅Π»ΡΠΌΠΈ Π²ΠΏΡΠΈΡΡΡΡΡΠ²ΠΈΠΈ ΠΌΠ΅ΡΠ°Π»Π»ΠΎΡΡΠ°Π»ΠΎΡΠΈΠ°Π½ΠΈΠ½ΠΎΠ² ΠΈ Π³ΠΈΠ΄ΡΠΎΠΊΡΠΎΠΊΠΎΠ±Π°Π»Π°ΠΌΠΈΠ½Π°: Π΄ΠΈΡΡ.ΠΊΠ°Π½Π΄.Ρ ΠΈΠΌ. Π½Π°ΡΠΊ: 00.02.04: Π·Π°ΡΠΈΡΠ΅Π½Π° 2010: ΡΡΠ². 2012. / ΠΠ³Π΅Π΅Π²Π° ΠΠ»Π΅Π½Π° Π‘Π΅ΡΠ³Π΅Π΅Π²Π½Π°. -ΠΠ²Π°Π½ΠΎΠ²ΠΎ, 2010.-109 Ρ.
- Kinetic and Thermodynamic Characterization of the Common Polymorphic Variants of Human Methionine Synthase Reductase/ H. Olteanu, K.R. Wolthers, A.W. Munro, N.S. Scrutton, R. Banerjee // Biochemistry. 2004. — V. 43. — P. 1988−1997.
- Co /Co Redox Tuning in Methyltransferases Induced by a Conformational Change at the Axial Ligand/ M. Kumar, N. Kumar, H. Hirao, P.M. Kozlowski // Inorg. Chem. 2012. — V. 51. — P. 5533−5538.
- Kumar, M. A Biologically Relevant Co1+—H Bond: Possible Implications in the Protein-Induced Redox Tuning of Co2+/Co,+ Reduction/ M. Kumar, P.M. Kozlowski // Angew. Chem. Int. Ed. 2011. — V. 50. — P. 8702−8705.
- Hydrogen bonds involving transition metal centres a brief review/ L. Brammer, D. Zhao, F.T. Ladipo, J. Braddock-Wilking // Acta Cryst. B. — 1995. — V. 51. — P. 632 640.
- Dispersion-Driven Hydrogen Bonding: Predicted Hydrogen Bond between Water and Platinum (II) Identified by Neutron Diffraction/ S. Rizzato, J. Berges, S.A. Mason, A. Albinati, J. Kozelka // Angew. Chem. Int. Ed. 2010. — V. 49. — P. 74 407 443.
- Structural and solution study on binary peptide and ternary peptide-nucleobase complexes of palladium (II)/ M. Wienken, E. Zangrando, L. Randaccio, S. Menzer, B. Lippert // J. Chem. Soc., Dalton Trans. 1993. -P. 3349−3357.
- Hydrogen Bonding in Organometallic Crystals. 6. X-H—M Hydrogen Bonds and M—(H-X) Pseudo-Agostic Bonds D. Braga, F. Grepioni, E. Tedesco, K. Biradha, G.R. Desiraju // Organometallics. 1997. -V. 16. — P. 1846−1856.
- Jensen, K.P. Electronic Structure of Cob (I)alamin: The Story of an Unusual Nucleophile/K.P. Jensen//J. Phys. Chem. B.-2005.-V. 109.-P. 10 505−10 512.
- Porro, C.S. Electronic properties of pentacoordinated heme complexes in cytochrome P450 enzymes: search for an Fe (I) oxidation state/ C.S. Porro, D. Kumar, S.P. de Visser // Phys. Chem. Chem. Phys. 2009. — V. 11. — P. 1 021 910 226.
- Silaghi-Dumitrescu, R. A computational analysis of electromerism in hemoprotein Fe (I) models/ R. Silaghi-Dumitrescu, S.V. Makarov // J. Biol. Inorg. Chem. 2010. -V. 15.-P. 977−986.
- Kis, Z. The Electronic Structure of Biologically Relevant Fe (0) Systems/ Z. Kis, R. Silaghi-Dumitrescu // Int. J. Quantum Chem. 2010. — V. 110. — P. 1848−1856.
- Schrauzer, G.N. The Nucleophilicity of Vitamin B12s/ G.N. Schrauzer, E. Deutsch, R.J. Windgassen // J. Am. Chem. Soc. 1968. — V. 90. — P. 2441−2442.
- Schrauzer, G.N. Reactions of Cobalt (I) Supernucleophiles. The Alkylation of Vitamin Bi2s, Cobaloximes (I), and Related Compounds/ G.N. Schrauzer, E. Deutsch //J. Am. Chem. Soc. 1969. -V. 91. — P. 3341−3350.
- Pearson, R.G. Nucleophilic reactivity constants toward methyl iodide and trans-dichlorodi (pyridine)platinum (II)/ R.G. Pearson, H. Sobel, J. Songstad // J. Am. Chem. Soc. 1968. -V. 90. — P. 319−326.
- Swain, C.G. Quantitative Correlation of Relative Rates. Comparison of Hydroxide Ion with Other Nucleophilic Reagents toward Alkyl Halides, Esters, Epoxides and Acyl Halides/ C.G. Swain, C.B. Scott // J. Am. Chem. Soc. 1953. -V. 75. — P. 141 147.
- Chemaly, S.M. The Chemistry of Vitamin B12. Part 23. Decomposition of the Cobalt (I) Cobalamin Bi2s in Aqueous Solution- a Novel Oscillating Reaction/ S.M. Chemaly, R.A. Hasty, J.M. Pratt // J. Chem. Soc. Dalton Trans. 1983. — P. 22 232 227.
- Cob (I)alamin reacts with sucralose to afford an alkylcobalamin: Relevance to in vivo cobalamin and sucralose interaction/ H.V. Motwani, S. Qui, B.T. Golding, H. Kylin, M. Tornqvist // Food Chem. Toxicol. 2011. — V. 49. — P. 750−757.
- Watson, W.P. A New Role for Glutathione: Protection of Vitamin B12 from Depletion by Xenobiotics/ W.P. Watson, T. Munter, B.T. Golding // Chem. Res. Toxicol.-2004.-V. 17.-P. 1562−1567.
- Motwani, H.V. Cob (I)alamin for Trapping Butadiene Epoxides in Metabolism with Rat S9 and for Determining Associated Kinetic Parameters/ H.V. Motwani, C. Fred, J. Haglund, B.T. Golding, M. Tornqvist // Chem. Res. Toxicol. 2009. — V. 22. — P. 1509−1516.
- Balasubramanian, P.N. Electron Transfer. 67. Reductions of Hydroxylamine Derivatives by Vitamin Bi2s (Cob (I)alamin)/ P.N. Balasubramanian, E.S. Gould // Inorg. Chem. 1984. — V. 23. — P. 824−828.
- Balasubramanian, P.N. Electron Transfer. 64. Reduction of Nitrate by Vitamin Bi2S (Cob (I)alamin)/ P.N. Balasubramanian, E.S. Gould // Inorg. Chem. 1983. — V. 22.-P. 2635−2637.
- Banks, R.G.S. Reactions of Gases in Solution. Part III. Some Reactions of Nitrous Oxide with Transition-metal Complexes/ R.G.S. Banks, RJ. Henderson, J.M. Pratt // J. Chem. Soc. (A). 1968. — P. 2886−2889.
- Blackburn, R. Reaction of Cob (I)alamin with Nitrous Oxide and Cob (III)alamin/ R. Blackburn, M. Kyaw, A J. Swallow // J. Chem. Soc., Faraday Trans. 1. 1977. -V. 73.-P. 250−255.
- Zheng, D. Electrochemical and Spectral Studies of the Reactions of Aquocobalamin with Nitric Oxide and Nitrite Ion / D. Zheng, L. Yan, R.L. Birke // Inorg.Chem. 2002. — V. 41. — P. 2548−2555.
- Chithambarathanu Pillai, G. Electron Transfer. 79. Reductions of Organic Disulfides by Vitamin Bi2s (Cob (I)alamin)/ G. Chithambarathanu Pillai, E.S. Gould // Inorg. Chem. 1986. — V. 25. — P. 3353−3356.
- Tahara, Π. Eco-friendly molecular transformations catalyzed by a vitamin Π12 derivative with a visible-light-driven system/ K. Tahara, Y. Hisaeda // Green Chem. -2011.-V. 13.-P. 558−561.
- Dechlorination of DDT catalyzed by visible-light-driven system composed of vitamin Π12 derivative and Rhodamin Π/ K. Tahara, K. Mikuriya, T. Masuko, J. Kikuchi, Y. Hisaeda // J. Porphyrins Phthalocyanines. 2013. — V. 17. — P. 135−141.
- Grodkowski, J. Cobalt Corrin Catalyzed Photoreduction of C02/ J. Grodkowski, P. Neta // J. Phys. Chem. A. 2000. — V. 104. — P. 1848−1853.
- Microwave Detection of Sulfoxylic Acid (HOSOH)/ K.N. Crabtree, O. Martinez, L. Barreau, S. Thorwirth, M.C. McCarthy // J. Phys. Chem. Π., ΡΡΠ°ΡΡΡ Π² ΠΏΠ΅ΡΠ°ΡΠΈ. -DOI: 10.102 l/jp400742q.
- Reactions of methyl viologen and nitrite with thiourea dioxide/ S.V. Makarov, E.V. Kudrik, R. van Eldik, E.V. Naidenko // J. Chem. Soc., Dalton Trans. 2002. -P. 4074−4076.
- Makarov, S.V. Acid-Base Properties of Sulfoxylate Ion/ S.V. Makarov, E.V. Kudrik, E.V. Naidenko // Russ. J. Phys. Chem. 2006. — V. 51. — P. 1149−1152.
- Makarov, S.V. Acid-Base Properties and Stability of Sulfoxylic Acid in Aqueous Solutions/ S.V. Makarov, D.S. Sal’nikov, A.S. Pogorelova // Russ. J. Inorg. Chem. -2010.-V. 55.-P. 301−304.
- A new route to carbon monoxide adducts of heme proteins/ S.V. Makarov, D.S. Salnikov, A.S. Pogorelova, Z. Kis, R. Silaghi-Dumitrescu // J. Porphyrins Phthalocyanines. 2008. — V. 12. — P. 1096−1099.
- Kinetics and Mechanism of the Iron Phthalocyanine Catalyzed Reduction of Nitrite by Dithionite and Sulfoxylate in Aqueous Solution/ E.V. Kudrik, S.V. Makarov, A. Zahl, R. van Eldik // Inorg. Chem. 2005. — V. 44. — P. 6470−6475.
- Π’Π΅ΡΡΠ°ΡΡΠ»ΡΡΠΎΡΡΠ°Π»ΠΎΡΠΈΠ°Π½ΠΈΠ½ ΠΊΠΎΠ±Π°Π»ΡΡΠ° ΠΊΠ°ΡΠ°Π»ΠΈΠ·Π°ΡΠΎΡ Π²ΠΎΡΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½ΠΈΡ Π½ΠΈΡΡΠΈΡΠ° Π΄ΠΈΠΎΠΊΡΠΈΠ΄ΠΎΠΌ ΡΠΈΠΎΠΌΠΎΡΠ΅Π²ΠΈΠ½Ρ/ Π. Π‘. ΠΠΎΠ³ΠΎΡΠ΅Π»ΠΎΠ²Π°, Π‘. Π. ΠΠ°ΠΊΠ°ΡΠΎΠ², Π. Π‘. ΠΠ³Π΅Π΅Π²Π°, Π . Π‘ΠΈΠ»Π°Π³ΠΈ-ΠΡΠΌΠΈΡΡΠ΅ΡΠΊΡ // ΠΡΡΠ½. ΡΠΈΠ·. Ρ ΠΈΠΌΠΈΠΈ. — 2009. — Π’. 83. — Π‘. 2250−2254.
- ΠΠ°ΠΊΠ°ΡΠΎΠ², Π‘.Π. ΠΠΎΠ²ΡΠ΅ Π½Π°ΠΏΡΠ°Π²Π»Π΅Π½ΠΈΡ Π² Ρ ΠΈΠΌΠΈΠΈ ΡΠ΅ΡΠΎΡΠΎΠ΄Π΅ΡΠΆΠ°ΡΠΈΡ Π²ΠΎΡΡΡΠ°Π½ΠΎΠ²ΠΈΡΠ΅Π»Π΅ΠΉ/ Π‘. Π. ΠΠ°ΠΊΠ°ΡΠΎΠ² // Π£ΡΠΏ. Ρ ΠΈΠΌΠΈΠΈ. — 2001. Π’. 70. — Π‘. 996−1007.
- ΠΡΠ΄Π°Π½ΠΎΠ², Π.Π. Π₯ΠΈΠΌΠΈΡ ΡΠ΅ΡΠΎΡΠΎΠ΄Π΅ΡΠΆΠ°ΡΠΈΡ Π²ΠΎΡΡΡΠ°Π½ΠΎΠ²ΠΈΡΠ΅Π»Π΅ΠΉ (ΡΠΎΠ½Π³Π°Π»ΠΈΡ, Π΄ΠΈΡΠΈΠΎΠ½ΠΈΡ, Π΄ΠΈΠΎΠΊΡΠΈΠ΄ ΡΠΈΠΎΠΌΠΎΡΠ΅Π²ΠΈΠ½Ρ)/ Π. Π. ΠΡΠ΄Π°Π½ΠΎΠ², Π‘. Π. ΠΠ°ΠΊΠ°ΡΠΎΠ² // Π.: Π₯ΠΈΠΌΠΈΡ. — 1994.-Π‘. 140.
- Reactive Oxygen Species in the Aerobic Decomposition of Sodium Hydroxymethanesulfinate/ S.V. Makarov, C. Mundoma, S.A. Svarovsky, X. Shi, P.M. Gannet, R.H. Simoyi // Arch. Biochem. Biophys. 1999. — V. 367. — P. 289 296.
- ΠΠΎΡΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½ΠΈΠ΅ Π½ΠΈΡΡΠΈΡΠ° Π³ΠΈΠ΄ΡΠΎΠΊΡΠΈΠΌΠ΅ΡΠ°Π½ΡΡΠ»ΡΡΠΈΠ½Π°ΡΠΎΠΌ Π½Π°ΡΡΠΈΡ Π² ΠΏΡΠΈΡΡΡΡΡΠ²ΠΈΠΈ ΡΠ΅ΡΡΠ°ΡΡΠ»ΡΡΠΎΡΡΠ°Π»ΠΎΡΠΈΠ°Π½ΠΈΠ½ΠΎΠ² ΠΊΠΎΠ±Π°Π»ΡΡΠ° ΠΈ ΠΆΠ΅Π»Π΅Π·Π°/ Π. Π‘. ΠΠ³Π΅Π΅Π²Π°, Π. Π. ΠΠ»Π°ΡΠΎΠ²Π°, Π‘. Π. ΠΠ°ΠΊΠ°ΡΠΎΠ², Π. Π‘. ΠΠ°ΠΊΠ°ΡΠΎΠ²Π° // ΠΠ·Π². Π²ΡΠ·ΠΎΠ². Π₯ΠΈΠΌΠΈΡ ΠΈ Ρ ΠΈΠΌ. ΡΠ΅Ρ Π½ΠΎΠ»ΠΎΠ³ΠΈΡ. 2010. — Π’. 53.-Π‘. 74−78.
- Pratt, J.M. Inorganic Chemistry of Vitamin B12/ J.M. Pratt. London: Academic Press, 1972.-335 p.
- Lambeth, D.O. The Kinetics and Mechanism of Reduction of Electron Transfer Proteins and Other Compounds of Biological Interest by Dithionite/ D.O. Lambeth, G. Palmer // J. Biol. Chem. 1973. — V. 248. — P. 6095−6103.
- Blackburn, R.S. Green Chemistry Methods in Sulfur Dyeing: Application of
- Various Reducing d-Sugars and Analysis of the Importance of Optimum Redox Potential/ R.S. Blackburn, A. Harvey // Environ. Sci. Technol. 2004. — V. 38. — P. 4034−4039.
- ΠΠ·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ ΠΌΠΎΠ½ΠΎΡΠ°Ρ Π°ΡΠΈΠ΄ΠΎΠ² Ρ ΡΠ΅ΡΡΠ°ΡΡΠ»ΡΡΠΎΡΡΠ°Π»ΠΎΡΠΈΠ°Π½ΠΈΠ½ΠΎΠΌ ΠΊΠΎΠ±Π°Π»ΡΡΠ°/ Π. Π. ΠΠ°Π»ΠΈΠ½ΠΊΠΈΠ½Π°, Π. Π‘. ΠΠ°ΠΊΠ°ΡΠΎΠ²Π°, Π‘. Π. ΠΠ°ΠΊΠ°ΡΠΎΠ², Π. Π‘. Π‘Π°Π»ΡΠ½ΠΈΠΊΠΎΠ² // ΠΠ°ΠΊΡΠΎΠ³Π΅ΡΠ΅ΡΠΎΡΠΈΠΊΠ»Ρ. 2011. — Π’. 4. — Π‘. 42−46.
- Gupta, N. Enzymatic mechanism and biochemistry for cyanide degradation: A review/ N. Gupta, C. Balomajumder, V.K. Agarwal // J. Hazard. Mater. 2010. — V. 176.-P. 1−13.
- Ashby, M.T. Hypothiocyanite/ M.T. Ashby // Adv. Inorg. Chem. 2012. — V. 64. -P. 263−303.
- Steady-State Kinetics of Thiocyanate Oxidation Catalyzed by Human Salivary Peroxidase/K.M. Pruitt, B. Mansson-Rahemtulla, D.C. Baldone, F. Rahemtulla // Biochemistry. 1988. — V. 27. — P. 240−245.
- Ashby, M.T. Redox Buffering of Hypochlorous Acid by Thiocyanate in Physiologic Fluids/ M.T. Ashby, A.C. Carlson, M. Jared Scott // J. Am. Chem. Soc. 2004. — V. 126.-P. 15 976−15 977.
- Thiosulfate, polythionates, and elemental sulfur assimilation and reduction in the bacterial world/ A. Le Faou, B.S. Rajagopal, L. Daniels, G. Fauque // FEMS Microbol. Rev. 1990. -V. 75. -P. 351−382.
- Thiosulfate Reduction in Salmonella enterica Is Driven by the Proton Motive Force/ L. Stoffels, M. Krehenbrink, B.C. Berks, G. Unden // J. Bacterid. 2012. -V. 194.-P. 475−485.
- Zhou, K. One-step synthesis of a/|3 cyano-aqua cobinamides from vitamin BI2 with Zn (II) or Cu (II) salts in methanol/ K. Zhou, F. Zelder // J. Porphyrins Phthalocyanines. -2011. V. 15.-P. 555−559.
- Stoll, S. EasySpin, a comprehensive software package for spectral simulation and analysis in EPR/ S. Stoll, A. Schweiger // J. Magn. Reson. 2006. — V. 178. — P. 4255.
- Axial Bonding in Alkylcobalamins: DFT Analysis of the Inverse Versus Normal Trans Influence/ J. Kuta, J. Wuerges, L. Randaccio, P.M. Kozlowski // J. Phys. Chem. A. 2009. — V. 113.-P. 11 604−11 612.
- SPARTAN '06 for Windows, Wavefunction Inc., 18 401 Von Karman Avenue, Suite 370 Irvine, CA 92 612, 2006.
- Hu, T.-M. The Kinetics of Thiol-mediated Decomposition of S-Nitrosothiols/ T.-M. Hu, T.-C. Chou // J. Am. Assoc. Pharm. Sei. 2006. — V. 8. — P. 485−492.
- Redox Chemistry of Fe2(CN)10.4 Part 4. Reaction with L-Cysteine/ F.A. Beckford, D. Bennet, T.P. Dasgupta, G. Stedman // J. Chem. Res. (S). 1998. — P. 98−99.
- The Chemistry of Vitamin BJ2. Part IV. The Thermodynamic trans-Effect. G.C. Hayward, H.A.O. Hill, J.M. Pratt, N.J. Vanston, R.J.O. Williams // J. Chem. Soc. -1965.-P. 6485−6493.
- Baldwin, D.A. The Chemistry of Vitamin B!2. Part 20. Diaquocobinamide: pK Values and Evidence for Conformational Isomers/ D.A. Baldwin, E.A. Betterton, J.M. Pratt // J. Chem. Soc., Dalton Trans. 1983. — P. 217−223.
- Bamford, C.H. Kinetic Studies on Carbohydrates in Alkaline Conditions. III. Interconversion of D-Glucose, D-Fructose and D-Mannose in Feebly Alkaline Solution/ C.H. Bamford, J.R. Collins // Proc. R. Soc. bond. A. 1955. — V. 228. — P. 100−119.
- Christensen, J.J. Thermodynamics of proton dissociation in dilute aqueous solution. Part XV. Proton dissociation from several monosaccharides at 10 and 40 Β°C/ J.J. Christensen, J. Howard Rytting, R.M. Izatt // J. Chem. Soc. B. 1970. -1646−1648.
- Kinetcs and Mechanism of the Cobalt Phthalocyanine Catalyzed Reduction of Nitrite and Nitrate by Ditionite in Aqueous Solution/ E.V. Kudrik, S.V. Makarov, A. Zahl, R. van Eldik // Inorg. Chem. 2003. — V. 42. — P. 618−624.
- ΠΠ»Π°ΡΠΎΠ²Π°, E.A. ΠΠΈΠ½Π΅ΡΠΈΠΊΠ° Π²ΠΎΡΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½ΠΈΡ Π½ΠΈΡΡΠΈΡΠ° Π΄ΠΈΠΎΠΊΡΠΈΠ΄ΠΎΠΌ ΡΠΈΠΎΠΌΠΎΡΠ΅Π²ΠΈΠ½Ρ Π² ΠΏΡΠΈΡΡΡΡΡΠ²ΠΈΠΈ ΠΎΠΊΡΠ°ΡΡΠ»ΡΡΠΎΡΠ΅Π½ΠΈΠ»ΡΠ΅ΡΡΠ°ΠΏΠΈΡΠ°Π·ΠΈΠ½ΠΎΠΏΠΎΡΡΠΈΡΠ°Π·ΠΈΠ½Π° ΠΊΠΎΠ±Π°Π»ΡΡΠ°/ Π.Π.
- ΠΠ»Π°ΡΠΎΠ²Π°, Π‘.Π. ΠΠ°ΠΊΠ°ΡΠΎΠ², Π.Π. ΠΠ°Π»ΠΈΠ½ΠΊΠΈΠ½Π° // ΠΡΡΠ½. ΡΠΈΠ·. Ρ ΠΈΠΌΠΈΠΈ. 2010. — Π’. 84. -Π‘. 655−660.
- Crystal chemistry and binding of N02, SCN and SeCN to Co in cobalamins/ G. Garau, S. Geremia, L.G. Marzilli, G. Nardin, L. Randaccio, G. Tauzher // Acta Crystallogr. Sect. B. -2003. -V. 59. P. 51−59.
- Crowell, T.I. The Hydrolysis of Thiocyanic Acid. I. Dependence of Rate on Acidity Function/ T.I. Crowell, M.G. Hankins // J. Phys. Chem. 1969. — V. 73. -1380−1383.
- Trommel, J.S. Assessment of the Existence of Hyper-Long Axial Co (II)-N Bonds in Cobinamide B.2 Models by Using Electron Paramagnetic Resonance Spectroscopy/ J.S. Trommel, K. Warncke, L.G. Marzilli // J. Am. Chem. Soc. -2001. V. 123. — P. 3358−3366.
- Reig, A.J. Combined Spectroscopic/Computational Studies of Vitamin B12 Precursors: Geometric and Electronic Structures of Cobinamides/ A.J. Reig, K.S. Conrad, T.C. Brunold // Inorg. Chem. 2012. — V. 51. — P. 2867−2879.
- Page, F.M. The Dissociation Constants of Thiosulfiiric Acid/ F.M. Page // J. Chem. Soc. 1953.-P. 1719−1724.
- Steudel, R. Microsolvation of Thiosulfuric Acid and Its Tautomeric Anions HSSO3.» and [SS02(0H)]" Studied by B3LYP-PCM and G3X (MP2) Calulations/ R. Steudel, Y. Steudel // J. Phys. Chem. A. 2009. — V. 113. — P. 9920−9933.
- Kinetics and Mechanism of the Oxidation of Thiosulfate Ion by Hexachloroiridate (IV)/ B. Goyal, S. Solanki, S. Arora, A. Prakash, R.N. Mehrotra // J. Chem. Soc., Dalton Trans. 1995. — P. 3109−3112.
- Electron transfer from thiosulfate to nickel (IV) oxime imine complexes in aqueous solution/ S. Bhattacharya, M. Ali, S. Gangopadhyay, P. Banerjee // J. Chem. Soc., Dalton Trans. 1996. — P. 2645−2651.
- Shvab, N.A. Mechanism of Reduction of Thiosulfate Ions on the Cathode/ N.A. Shvab, V.D. Litovchenko, L.M. Rudkovskaya // Russ. J. Appl. Chem. 2007. — V. 80.-P. 1852−1855.
- Prasad, S.M. Rerefinement of sodium thiosulfate pentahydrate/ S.M. Prasad, A. Rani // Acta Cryst. E. 2001. — V. 57. — P. 67−69.
- Huss, A. Jr. Equilibria and ion activities in aqueous sulfur dioxide solutions/ A. Huss, Jr., C.A. Eckert // J. Phys. Chem. 1977. — V. 81. -P. 2268−2270.
- Hayon, E. Electronic spectra, photochemistry, and autoxidation mechanism of the sulfite-bisulfite-pyrosulfite systems. S02 SO3', SO4″, and S05″ radicals/ E. Hayon, A. Treinin, J. Wilf // J. Am. Chem. Soc. 1972. -V. 94. — P. 47−57.
- Horner, D.A. Equilibrium quotient for the isomerization of bisulfite ion from HSO3' to S03H7 D.A. Horner, R.E. Connick // Inorg. Chem. 1986. — V. 25. — P. 2414−2417.
- Connick, R.E. Equilibrium Constant for the Dimerization of Bisulfite Ion to Form S2052"/ R.E. Connick, T.M. Tam, E. von Deuster // Inorg. Chem. 1982. — V. 21. -P. 103−107.
- Smith, K.W. Mutational Analysis of Sufite Reductase Hemoprotein Reveals the Mechanism for Coordinated Electron and Proton Transfer/ K.W. Smith, M.E. Stroupe // Biochemistry. 2012. — V. 51. — P. 9857−9868.
- Electromerism and linkage isomeristti in biologically-relevant Fe—SO complexes/ M. Surducan, D. Lup, A. Lupan, S.V. Makarov, R. Silaghi-Dumitrescu // J. Inorg. Biochem. -2013. V. 118.-P. 13−20.