메뉴 건너뛰기




Volumn 98, Issue 4, 1998, Pages 1357-1373

The molecular mechanism of autoxidation for myoglobin and hemoglobin: A venerable puzzle

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0001023291     PISSN: 00092665     EISSN: None     Source Type: Journal    
DOI: 10.1021/cr970042e     Document Type: Article
Times cited : (241)

References (83)
  • 1
    • 0021893230 scopus 로고
    • 2 bonding in myoglobin: An overview from physical to clinical biochemistry
    • 2 bonding in myoglobin: An overview from physical to clinical biochemistry. Experientia 1985, 41, 701-706.
    • (1985) Experientia , vol.41 , pp. 701-706
    • Shikama, K.1
  • 2
    • 0014250481 scopus 로고
    • Substituted deuteroporphyrins. IV. on the kinetics and mechanism of reactions of iron(II) porphyrins with oxygen
    • Cohen, I. A.; Caughey, W. S. Substituted deuteroporphyrins. IV. On the kinetics and mechanism of reactions of iron(II) porphyrins with oxygen. Biochemistry 1968, 7, 636-641.
    • (1968) Biochemistry , vol.7 , pp. 636-641
    • Cohen, I.A.1    Caughey, W.S.2
  • 3
    • 0010860465 scopus 로고
    • Oxidation of iron(II) chloride in nonaqueous solvents
    • Hammond, G. S.; Wu, C.-H. S. Oxidation of iron(II) chloride in nonaqueous solvents. Adv. Chem. Ser. 1968, 77, 186-207.
    • (1968) Adv. Chem. Ser. , vol.77 , pp. 186-207
    • Hammond, G.S.1    Wu, C.-H.S.2
  • 4
    • 0015513712 scopus 로고
    • The crystal structure and molecular stereochemistry of μ-oxo-bis[α,β,γ,δ-tetraphenylporphinatoiron(III)]
    • Huffman, A. B.; Collins, D. M.; Day, V. W.; Fleischer, E. B.; Srivastava, T. S.; Hoard, J. L. The crystal structure and molecular stereochemistry of μ-oxo-bis[α,β,γ,δ-tetraphenylporphinatoiron(III)]. J. Am. Chem. Soc. 1972, 94, 3620-3626.
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 3620-3626
    • Huffman, A.B.1    Collins, D.M.2    Day, V.W.3    Fleischer, E.B.4    Srivastava, T.S.5    Hoard, J.L.6
  • 5
    • 0015932856 scopus 로고
    • Binding of dioxygen to iron(II). Reversible behavior in solution
    • Baldwin, J. E.; Huff, J. Binding of dioxygen to iron(II). Reversible behavior in solution. J. Am. Chem. Soc. 1973, 95, 5757-5759.
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 5757-5759
    • Baldwin, J.E.1    Huff, J.2
  • 6
    • 0000182959 scopus 로고
    • Reversible oxygenation and autoxidation of a "capped" porphyrin iron(II) complex
    • Almog, J.; Baldwin, J. E.; Huff, J. Reversible oxygenation and autoxidation of a "capped" porphyrin iron(II) complex. J. Am. Chem. Soc. 1975, 97, 227-228.
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 227-228
    • Almog, J.1    Baldwin, J.E.2    Huff, J.3
  • 7
    • 33847800685 scopus 로고
    • Synthetic oxygen carriers of biological interest
    • Basolo, F.; Hoffman, B. M.; Ibers, J. A. Synthetic oxygen carriers of biological interest. Acc. Chem. Res. 1975, 8, 384-392.
    • (1975) Acc. Chem. Res. , vol.8 , pp. 384-392
    • Basolo, F.1    Hoffman, B.M.2    Ibers, J.A.3
  • 8
    • 33847088870 scopus 로고
    • Synthetic models for the oxygen-binding hemoproteins
    • Collman, J. P. Synthetic models for the oxygen-binding hemoproteins. Acc. Chem. Res. 1977, 10, 265-272.
    • (1977) Acc. Chem. Res. , vol.10 , pp. 265-272
    • Collman, J.P.1
  • 9
    • 0021503754 scopus 로고
    • A controversy on the mechanism of autoxidation of oxymyoglobin and oxyhaemoglobin: Oxidation, dissociation, or displacement?
    • Shikama, K. A controversy on the mechanism of autoxidation of oxymyoglobin and oxyhaemoglobin: Oxidation, dissociation, or displacement? Biochem. J. 1984, 223, 279-280.
    • (1984) Biochem. J. , vol.223 , pp. 279-280
    • Shikama, K.1
  • 10
    • 0000564980 scopus 로고
    • The electron-transfer mechanism of autoxidation for hemoglobin, myoglobin, and their iron(II) cyclidene models
    • Dickerson, L. D.; Sauer-Masarwa, A.; Herron, N.; Fendrick, C. M.; Busch, D. H. The electron-transfer mechanism of autoxidation for hemoglobin, myoglobin, and their iron(II) cyclidene models. J. Am. Chem. Soc. 1993, 115, 3623-3626.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3623-3626
    • Dickerson, L.D.1    Sauer-Masarwa, A.2    Herron, N.3    Fendrick, C.M.4    Busch, D.H.5
  • 11
    • 10644277476 scopus 로고
    • Iron and cobalt "lacunar" complexes as dioxygen carriers
    • Busch, D. H.; Alcock, N. W. Iron and cobalt "lacunar" complexes as dioxygen carriers. Chem. Rev. 1994, 94, 585-623.
    • (1994) Chem. Rev. , vol.94 , pp. 585-623
    • Busch, D.H.1    Alcock, N.W.2
  • 12
    • 0019143916 scopus 로고
    • Autoxidation of native oxymyoglobin. Thermodynamic analysis of the pH profile
    • Sugawara, Y.; Shikama, K. Autoxidation of native oxymyoglobin. Thermodynamic analysis of the pH profile. Eur. J. Biochem. 1980, 110, 241-246.
    • (1980) Eur. J. Biochem. , vol.110 , pp. 241-246
    • Sugawara, Y.1    Shikama, K.2
  • 13
    • 0015887378 scopus 로고
    • Nonequivalence of chains in hemoglobin oxidation
    • Mansouri, A.; Winterhalter, K. H. Nonequivalence of chains in hemoglobin oxidation. Biochemistry 1973, 12, 4946-4949.
    • (1973) Biochemistry , vol.12 , pp. 4946-4949
    • Mansouri, A.1    Winterhalter, K.H.2
  • 14
    • 0031552067 scopus 로고    scopus 로고
    • Biphasic nature in the autoxidation reaction of human oxyhemoglobin
    • Tsuruga, M.; Shikama, K. Biphasic nature in the autoxidation reaction of human oxyhemoglobin. Biochim. Biophys. Acta 1997, 1337, 96-104.
    • (1997) Biochim. Biophys. Acta , vol.1337 , pp. 96-104
    • Tsuruga, M.1    Shikama, K.2
  • 15
    • 0022273616 scopus 로고
    • Myoglobin:cytochrome 65 interactions and the kinetic mechanism of metmyoglobin reductase
    • Livingston, D. J.; McLachlan, S. J.; La Mar, G. N.; Brown, W. D. Myoglobin:cytochrome 65 interactions and the kinetic mechanism of metmyoglobin reductase. J. Biol. Chem. 1985, 260, 15699-15707.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15699-15707
    • Livingston, D.J.1    McLachlan, S.J.2    La Mar, G.N.3    Brown, W.D.4
  • 17
    • 3042907629 scopus 로고
    • Synthetic heme dioxygen complexes
    • Momenteau, M.; Reed, C. A. Synthetic heme dioxygen complexes. Chem. Rev. 1994, 94, 659-698.
    • (1994) Chem. Rev. , vol.94 , pp. 659-698
    • Momenteau, M.1    Reed, C.A.2
  • 18
    • 0000675667 scopus 로고
    • The oxidation of haemoglobin to methaemoglobin by oxygen. II. The relation between the rate of oxidation and the partial pressure of oxygen
    • Brooks, J. The oxidation of haemoglobin to methaemoglobin by oxygen. II. The relation between the rate of oxidation and the partial pressure of oxygen. Proc. R. Soc. London, Ser. B. 1935, 118, 560-577.
    • (1935) Proc. R. Soc. London, Ser. B , vol.118 , pp. 560-577
    • Brooks, J.1
  • 19
    • 0000448117 scopus 로고
    • The oxidation of myoglobin to metmyoglobin by oxygen. 2. The relation between the first-order rate constant and the partial pressure of oxygen
    • George, P.; Stratmann, C. J. The oxidation of myoglobin to metmyoglobin by oxygen. 2. The relation between the first-order rate constant and the partial pressure of oxygen. Biochem. J. 1952, 51, 418-425.
    • (1952) Biochem. J. , vol.51 , pp. 418-425
    • George, P.1    Stratmann, C.J.2
  • 20
    • 0028243148 scopus 로고
    • Aplysia myoglobin with unusual properties: Another prototype in myoglobin and hemoglobin biochemistry
    • Shikama, K.; Matsuoka, A. Aplysia myoglobin with unusual properties: Another prototype in myoglobin and hemoglobin biochemistry. Biol. Rev. (Cambridge) 1994, 69, 233-251.
    • (1994) Biol. Rev. (Cambridge) , vol.69 , pp. 233-251
    • Shikama, K.1    Matsuoka, A.2
  • 21
    • 0028824271 scopus 로고
    • The unique structures of protozoan myoglobin and yeast hemoglobin: An evolutionary diversity
    • Shikama, K.; Matsuoka, A.; Iwaasa, H. The unique structures of protozoan myoglobin and yeast hemoglobin: An evolutionary diversity. Int. J. Biochem. Cell Biol. 1995, 27, 1107-1115.
    • (1995) Int. J. Biochem. Cell Biol. , vol.27 , pp. 1107-1115
    • Shikama, K.1    Matsuoka, A.2    Iwaasa, H.3
  • 22
    • 0025186280 scopus 로고
    • Protozoan myoglobin from Paramecium caudatum: Its autoxidation reaction and hemichrome formation
    • Tsubamoto, Y.; Matsuoka, A.; Yusa, K.; Shikama, K. Protozoan myoglobin from Paramecium caudatum: Its autoxidation reaction and hemichrome formation. Eur. J. Biochem. 1990, 193, 55-59.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 55-59
    • Tsubamoto, Y.1    Matsuoka, A.2    Yusa, K.3    Shikama, K.4
  • 23
    • 0029144157 scopus 로고
    • Role of globin moiety in the autoxidation reaction of oxymyoglobin: Effect of 8 M urea
    • Sugawara, Y.; Matsuoka, A.; Kaino, A.; Shikama, K. Role of globin moiety in the autoxidation reaction of oxymyoglobin: Effect of 8 M urea. Biophys. J. 1995, 69, 583-592.
    • (1995) Biophys. J. , vol.69 , pp. 583-592
    • Sugawara, Y.1    Matsuoka, A.2    Kaino, A.3    Shikama, K.4
  • 24
    • 0001902954 scopus 로고
    • The oxidation of haemoglobin to methaemoglobin by oxygen
    • Brooks, J. The oxidation of haemoglobin to methaemoglobin by oxygen. Proc. R. Soc. London, Ser. B. 1931, 109, 35-50.
    • (1931) Proc. R. Soc. London, Ser. B , vol.109 , pp. 35-50
    • Brooks, J.1
  • 25
    • 0009695370 scopus 로고
    • The oxidation of myoglobin to metmyoglobin by oxygen. 3. Kinetic studies in the presence of carbon monoxide, and at different hydrogen-ion concentrations with considerations regarding the stability of oxymyoglobin
    • George, P.; Stratmann, C. J. The oxidation of myoglobin to metmyoglobin by oxygen. 3. Kinetic studies in the presence of carbon monoxide, and at different hydrogen-ion concentrations with considerations regarding the stability of oxymyoglobin. Biochem. J. 1954, 57, 568-573.
    • (1954) Biochem. J. , vol.57 , pp. 568-573
    • George, P.1    Stratmann, C.J.2
  • 26
    • 0014691369 scopus 로고
    • Autoxidation of oxymyoglobins
    • Brown, W. C.; Mebine, L. B. Autoxidation of oxymyoglobins. J. Biol. Chem. 1969, 244, 6696-6701.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6696-6701
    • Brown, W.C.1    Mebine, L.B.2
  • 27
    • 0019995366 scopus 로고
    • Mechanism of autoxidation for hemoglobins and myoglobins. Promotion of superoxide production by protons and anions
    • Wallace, W. J.; Houtchens, R. A.; Maxwell, J. C.; Caughey, W. S. Mechanism of autoxidation for hemoglobins and myoglobins. Promotion of superoxide production by protons and anions. J. Biol. Chem. 1982, 257, 4966-4977.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4966-4977
    • Wallace, W.J.1    Houtchens, R.A.2    Maxwell, J.C.3    Caughey, W.S.4
  • 29
    • 0007040080 scopus 로고
    • Studies on the oxidation - Reduction potentials of heme proteins. IV. The kinetics of oxidation of hemoglobin and myoglobin by ferricyanide
    • Antonini, E.; Brunori, M.; Wyman, J. Studies on the oxidation - reduction potentials of heme proteins. IV. The kinetics of oxidation of hemoglobin and myoglobin by ferricyanide. Biochemistry 1965, 4, 545-551.
    • (1965) Biochemistry , vol.4 , pp. 545-551
    • Antonini, E.1    Brunori, M.2    Wyman, J.3
  • 30
    • 0000456481 scopus 로고
    • Preparation of crystalline oxymyoglobin from horse heart
    • Yamazaki, I.; Yokota, K.; Shikama, K. Preparation of crystalline oxymyoglobin from horse heart. J. Biol. Chem. 1964, 239, 4151-4153.
    • (1964) J. Biol. Chem. , vol.239 , pp. 4151-4153
    • Yamazaki, I.1    Yokota, K.2    Shikama, K.3
  • 32
    • 0023661090 scopus 로고
    • Oxidation of oxymyoglobin to metmyoglobin with hydrogen peroxide: Involvement of ferryl intermediate
    • Yusa, K.; Shikama, K. Oxidation of oxymyoglobin to metmyoglobin with hydrogen peroxide: Involvement of ferryl intermediate. Biochemistry 1987, 26, 6684-6688.
    • (1987) Biochemistry , vol.26 , pp. 6684-6688
    • Yusa, K.1    Shikama, K.2
  • 33
    • 0016156128 scopus 로고
    • The mechanisms of hemoglobin autoxidation. Evidence for proton-assisted nucleophilic displacement of superoxide by anions
    • Wallace, W. J.; Maxwell, J. C.; Caughey, W. S. The mechanisms of hemoglobin autoxidation. Evidence for proton-assisted nucleophilic displacement of superoxide by anions. Biochem. Biophys. Res. Commun. 1974, 57, 1104-1110.
    • (1974) Biochem. Biophys. Res. Commun. , vol.57 , pp. 1104-1110
    • Wallace, W.J.1    Maxwell, J.C.2    Caughey, W.S.3
  • 34
    • 0016184960 scopus 로고
    • A role for chloride in the autoxidation of hemoglobin under conditions similar to those in erythrocytes
    • Wallace, W. J.; Maxwell, J. C.; Caughey, W. S. A role for chloride in the autoxidation of hemoglobin under conditions similar to those in erythrocytes. FEBS Lett. 1974, 43, 33-36.
    • (1974) FEBS Lett. , vol.43 , pp. 33-36
    • Wallace, W.J.1    Maxwell, J.C.2    Caughey, W.S.3
  • 35
    • 1942470767 scopus 로고
    • Kinetic study of the oxidation of ferrohemochrome by molecular oxygen
    • Kao, O. H.; Wang, J. H. Kinetic study of the oxidation of ferrohemochrome by molecular oxygen. Biochemistry 1965, 4, 342-347.
    • (1965) Biochemistry , vol.4 , pp. 342-347
    • Kao, O.H.1    Wang, J.H.2
  • 36
    • 0017870716 scopus 로고
    • Oxidation of lowspin iron(II) porphyrins by molecular oxygen. An outer sphere mechanism
    • Chu, M. M. L.; Castro, C. E.; Hathaway, G. M. Oxidation of lowspin iron(II) porphyrins by molecular oxygen. An outer sphere mechanism. Biochemistry 1978, 17, 481-486.
    • (1978) Biochemistry , vol.17 , pp. 481-486
    • Chu, M.M.L.1    Castro, C.E.2    Hathaway, G.M.3
  • 37
    • 0028061399 scopus 로고
    • Oxidation of hemoglobin and the enhancement produced by nitroblue tetrazolium
    • Abugo, O. O.; Rifkind, J. M. Oxidation of hemoglobin and the enhancement produced by nitroblue tetrazolium. J. Biol. Chem. 1994, 269, 24845-24853.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24845-24853
    • Abugo, O.O.1    Rifkind, J.M.2
  • 38
    • 0002424327 scopus 로고
    • Nature of the iron-oxygen bond in oxyhaemoglobin
    • Weiss, J. J. Nature of the iron-oxygen bond in oxyhaemoglobin. Nature (London) 1964, 202, 83-84.
    • (1964) Nature (London) , vol.202 , pp. 83-84
    • Weiss, J.J.1
  • 39
    • 0015502066 scopus 로고
    • The generation of superoxide radical during the autoxidation of hemoglobin
    • Misra, H. P.; Fridovich, I. The generation of superoxide radical during the autoxidation of hemoglobin. J. Biol. Chem. 1972, 247, 6960-6962.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6960-6962
    • Misra, H.P.1    Fridovich, I.2
  • 40
    • 0001540685 scopus 로고
    • Generation of superoxide radicals during the autoxidation of mammalian oxyhemoglobin
    • Wever, R.; Oudega, B.; Van Gelder, B. F. Generation of superoxide radicals during the autoxidation of mammalian oxyhemoglobin. Biochim. Biophys. Acta 1973, 302, 475-478.
    • (1973) Biochim. Biophys. Acta , vol.302 , pp. 475-478
    • Wever, R.1    Oudega, B.2    Van Gelder, B.F.3
  • 41
    • 0016660866 scopus 로고
    • Formation of superoxide in the autoxidation of the isolated α and β chains of human hemoglobin and its involvement in hemichrome precipitation
    • Brunori, M.; Falcioni, G.; Fioretti, E.; Giardina, B.; Rotilio, G. Formation of superoxide in the autoxidation of the isolated α and β chains of human hemoglobin and its involvement in hemichrome precipitation. Eur. J. Biochem. 1975, 53, 99-104.
    • (1975) Eur. J. Biochem. , vol.53 , pp. 99-104
    • Brunori, M.1    Falcioni, G.2    Fioretti, E.3    Giardina, B.4    Rotilio, G.5
  • 42
    • 0017137387 scopus 로고
    • Generation of the superoxide radical during autoxidation of oxymyoglobin
    • Gotoh, T.; Shikama, K. Generation of the superoxide radical during autoxidation of oxymyoglobin. J. Biochem. (Tokyo) 1976, 80, 397-399.
    • (1976) J. Biochem. (Tokyo) , vol.80 , pp. 397-399
    • Gotoh, T.1    Shikama, K.2
  • 43
    • 37049049612 scopus 로고
    • Nature of the iron-oxygen bond in oxyhaemoglobin
    • Pauling, L. Nature of the iron-oxygen bond in oxyhaemoglobin. Nature (London) 1964, 203, 182-183.
    • (1964) Nature (London) , vol.203 , pp. 182-183
    • Pauling, L.1
  • 44
    • 0013925081 scopus 로고
    • Mössbauer effect in some haemoglobin compounds
    • Lang, G.; Marshall, W. Mössbauer effect in some haemoglobin compounds. J. Mol. Biol. 1966, 18, 385-404.
    • (1966) J. Mol. Biol. , vol.18 , pp. 385-404
    • Lang, G.1    Marshall, W.2
  • 45
    • 0016146116 scopus 로고
    • Infrared evidence for the mode of binding of oxygen to iron of myoglobin from heart muscle
    • Maxwell, J. C.; Volpe, J. A.; Barlow, C. H.; Caughey, W. S. Infrared evidence for the mode of binding of oxygen to iron of myoglobin from heart muscle. Biochem. Biophys. Res. Commun. 1974, 58, 166-171.
    • (1974) Biochem. Biophys. Res. Commun. , vol.58 , pp. 166-171
    • Maxwell, J.C.1    Volpe, J.A.2    Barlow, C.H.3    Caughey, W.S.4
  • 47
    • 0016819379 scopus 로고
    • Relation between redox potentials and rate constants in reactions coupled with the system oxygen-superoxide
    • Sawada, Y.; Iyanagi, T.; Yamazaki, I. Relation between redox potentials and rate constants in reactions coupled with the system oxygen-superoxide. Biochemistry 1975, 14, 3761-3764.
    • (1975) Biochemistry , vol.14 , pp. 3761-3764
    • Sawada, Y.1    Iyanagi, T.2    Yamazaki, I.3
  • 48
    • 0025173627 scopus 로고
    • Autoxidation of oxymyoglobin: A meeting point of the stabilization and the activation of molecular oxygen
    • Shikama, K. Autoxidation of oxymyoglobin: A meeting point of the stabilization and the activation of molecular oxygen. Biol. Rev. (Cambridge) 1990, 65, 517-527.
    • (1990) Biol. Rev. (Cambridge) , vol.65 , pp. 517-527
    • Shikama, K.1
  • 49
    • 0002950246 scopus 로고
    • Oxidation - Reduction potentials of the metmyoglobin-myoglobin system
    • Taylor, J. F.; Morgan, V. E. Oxidation - reduction potentials of the metmyoglobin-myoglobin system. J. Biol. Chem. 1942, 144, 15-20.
    • (1942) J. Biol. Chem. , vol.144 , pp. 15-20
    • Taylor, J.F.1    Morgan, V.E.2
  • 50
  • 51
    • 0018071017 scopus 로고
    • Autoxidation of native oxymyoglobin. Kinetic analysis of the pH profile
    • Shikama, K.; Sugawara, Y. Autoxidation of native oxymyoglobin. Kinetic analysis of the pH profile. Eur. J. Biochem. 1978, 91, 407-413.
    • (1978) Eur. J. Biochem. , vol.91 , pp. 407-413
    • Shikama, K.1    Sugawara, Y.2
  • 52
    • 0001388027 scopus 로고
    • Aplysia oxymyoglobin with an unusual stability property: Kinetic analysis of the pH dependence
    • Shikama, K.; Matsuoka, A. Aplysia oxymyoglobin with an unusual stability property: Kinetic analysis of the pH dependence. Biochemistry 1986, 25, 3898-3903.
    • (1986) Biochemistry , vol.25 , pp. 3898-3903
    • Shikama, K.1    Matsuoka, A.2
  • 55
    • 0026517416 scopus 로고
    • Stability properties of Aplysia oxymyoglobin: Effect of esterification of the heme propionates
    • Matsuoka, A.; Shikama, K. Stability properties of Aplysia oxymyoglobin: Effect of esterification of the heme propionates. Biochim. Biophys. Acta 1992, 1118, 123-129.
    • (1992) Biochim. Biophys. Acta , vol.1118 , pp. 123-129
    • Matsuoka, A.1    Shikama, K.2
  • 56
    • 0002609608 scopus 로고    scopus 로고
    • A myoglobin-like protein from Tetrahymena pyriformis: Isolation and characterization
    • Korenaga, S.; Miki, K.; Shikama, K. A myoglobin-like protein from Tetrahymena pyriformis: Isolation and characterization. Eur. J. Protistol. 1996, 32, Suppl. I, 73-78.
    • (1996) Eur. J. Protistol. , vol.32 , Issue.1 SUPPL. , pp. 73-78
    • Korenaga, S.1    Miki, K.2    Shikama, K.3
  • 57
    • 0002400397 scopus 로고
    • The mode of attachment of the azide ion to sperm whale metmyoglobin
    • Stryer, L.; Kendrew, J. C.; Watson, H. C. The mode of attachment of the azide ion to sperm whale metmyoglobin. J. Mol. Biol. 1964, 8, 96-104.
    • (1964) J. Mol. Biol. , vol.8 , pp. 96-104
    • Stryer, L.1    Kendrew, J.C.2    Watson, H.C.3
  • 58
    • 0019827532 scopus 로고
    • Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin
    • Phillips, S. E. V.; Schoenborn, B. P. Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin. Nature (London) 1981, 292, 81-82.
    • (1981) Nature (London) , vol.292 , pp. 81-82
    • Phillips, S.E.V.1    Schoenborn, B.P.2
  • 59
    • 0002564269 scopus 로고
    • Stability properties of dioxygen - Iron(II) porphyrins: An overview from simple complexes to myoglobin
    • Shikama, K. Stability properties of dioxygen - iron(II) porphyrins: An overview from simple complexes to myoglobin. Coord. Chem. Rev. 1988, 83, 73-91.
    • (1988) Coord. Chem. Rev. , vol.83 , pp. 73-91
    • Shikama, K.1
  • 60
    • 0024293920 scopus 로고
    • Aplysia oxymyoglobin with an unusual stability property: Involvement of two kinds of carboxyl groups
    • Matsuoka, A.; Shikama, K. Aplysia oxymyoglobin with an unusual stability property: involvement of two kinds of carboxyl groups. Biochim. Biophys. Acta 1988, 956, 127-132.
    • (1988) Biochim. Biophys. Acta , vol.956 , pp. 127-132
    • Matsuoka, A.1    Shikama, K.2
  • 61
    • 0024961706 scopus 로고
    • Aplysia limacina myoglobin: Crystallographic analysis at 1.6 a resolution
    • Bolognesi, M.; Onesti, S.; Gatti, G.; Coda, A.; Ascenzi, P.; Brunori, M. Aplysia limacina myoglobin: crystallographic analysis at 1.6 A resolution. J. Mol. Biol. 1989, 205, 529-544.
    • (1989) J. Mol. Biol. , vol.205 , pp. 529-544
    • Bolognesi, M.1    Onesti, S.2    Gatti, G.3    Coda, A.4    Ascenzi, P.5    Brunori, M.6
  • 62
    • 0024962496 scopus 로고
    • Spectral properties unique to the myoglobins lacking the usual distal histidine residue
    • Shikama, K.; Matsuoka, A. Spectral properties unique to the myoglobins lacking the usual distal histidine residue. J. Mol. Biol. 1989, 209, 489-491.
    • (1989) J. Mol. Biol. , vol.209 , pp. 489-491
    • Shikama, K.1    Matsuoka, A.2
  • 63
    • 0026478810 scopus 로고
    • The Soret magnetic circular dichroism of ferric high-spin myoglobins. A probe for the distal histidine residue
    • Matsuoka, A.; Kobayashi, N.; Shikama, K. The Soret magnetic circular dichroism of ferric high-spin myoglobins. A probe for the distal histidine residue. Eur. J. Biochem. 1992, 210, 337-341.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 337-341
    • Matsuoka, A.1    Kobayashi, N.2    Shikama, K.3
  • 65
    • 0019811330 scopus 로고
    • Autoxidation of oxymyoglobin. A nucleophilic displacement mechanism
    • Satoh, Y.; Shikama, K. Autoxidation of oxymyoglobin. A nucleophilic displacement mechanism. J. Biol. Chem. 1981, 256, 10272-10275.
    • (1981) J. Biol. Chem. , vol.256 , pp. 10272-10275
    • Satoh, Y.1    Shikama, K.2
  • 66
    • 0001290315 scopus 로고
    • Polarizability, basicity and nucleophilic character
    • Edwards, J. O. Polarizability, basicity and nucleophilic character. J. Am. Chem. Soc. 1956, 78, 1819-1820.
    • (1956) J. Am. Chem. Soc. , vol.78 , pp. 1819-1820
    • Edwards, J.O.1
  • 68
    • 33947298622 scopus 로고
    • 2 in aqueous solutions by pulse radiolysis
    • 2 in aqueous solutions by pulse radiolysis. J. Phys. Chem. 1969, 73, 3736-3744.
    • (1969) J. Phys. Chem. , vol.73 , pp. 3736-3744
    • Rabani, J.1    Nielsen, S.O.2
  • 69
    • 0016414528 scopus 로고
    • Superoxide dismutases
    • Fridovich, I. Superoxide dismutases. Annu. Rev. Biochem. 1975, 44, 147-159.
    • (1975) Annu. Rev. Biochem. , vol.44 , pp. 147-159
    • Fridovich, I.1
  • 70
    • 0023656226 scopus 로고
    • Autoxidation of oxymyoglobin. An overall stoichiometry including subsequent side reactions
    • Tajima, G.; Shikama, K. Autoxidation of oxymyoglobin. An overall stoichiometry including subsequent side reactions. J. Biol. Chem. 1987, 262, 12603-12606.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12603-12606
    • Tajima, G.1    Shikama, K.2
  • 71
    • 0027471930 scopus 로고
    • Decomposition of hydrogen peroxide by metmyoglobin: A cyclic formation of the ferryl intermediate
    • Tajima, G.; Shikama, K. Decomposition of hydrogen peroxide by metmyoglobin: A cyclic formation of the ferryl intermediate. Int. J. Biochem. 1993, 25, 101-105.
    • (1993) Int. J. Biochem. , vol.25 , pp. 101-105
    • Tajima, G.1    Shikama, K.2
  • 72
    • 0022434098 scopus 로고
    • IV=O stretching vibration of ferryl myoglobin by resonance Raman spectroscopy
    • IV=O stretching vibration of ferryl myoglobin by resonance Raman spectroscopy. Biochim. Biophys. Acta 1985, 828, 229-235.
    • (1985) Biochim. Biophys. Acta , vol.828 , pp. 229-235
    • Sitter, A.J.1    Reczek, C.M.2    Terner, J.3
  • 73
    • 0024297338 scopus 로고
    • 2-mediated crosslinking of sperm whale myoglobin
    • 2-mediated crosslinking of sperm whale myoglobin. J. Biol. Chem. 1988, 263, 17880-17886.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17880-17886
    • Tew, D.1
  • 74
    • 0026063955 scopus 로고
    • Identification of a globin free radical in equine myoglobin treated with peroxides
    • Davies, M. J. Identification of a globin free radical in equine myoglobin treated with peroxides. Biochim. Biophys. Acta 1991, 1077, 86-90.
    • (1991) Biochim. Biophys. Acta , vol.1077 , pp. 86-90
    • Davies, M.J.1
  • 75
    • 0029028275 scopus 로고
    • Self-peroxidation of metmyoglobin results in formation of an oxygen-reactive tryptophan-centered radical
    • Gunther, M. R.; Kelman, D. J.; Corbett, J. T.; Mason, R. P. Self-peroxidation of metmyoglobin results in formation of an oxygen-reactive tryptophan-centered radical. J. Biol. Chem. 1995, 270, 16075-16081.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16075-16081
    • Gunther, M.R.1    Kelman, D.J.2    Corbett, J.T.3    Mason, R.P.4
  • 76
    • 0026701964 scopus 로고
    • Hydrogen peroxide plays a key role in the oxidation reaction of myoglobin by molecular oxygen. A computer simulation
    • Wazawa, T.; Matsuoka, A.; Tajima, G.; Sugawara, Y.; Nakamura, K.; Shikama, K. Hydrogen peroxide plays a key role in the oxidation reaction of myoglobin by molecular oxygen. A computer simulation. Biophys. J. 1992, 63, 544-550.
    • (1992) Biophys. J. , vol.63 , pp. 544-550
    • Wazawa, T.1    Matsuoka, A.2    Tajima, G.3    Sugawara, Y.4    Nakamura, K.5    Shikama, K.6
  • 77
    • 0023051712 scopus 로고
    • Properties of catalase purified from a methanolgrown yeast, Kloeckera sp. 2201
    • Mozaffar, S.; Ueda, M.; Kitatsuji, K.; Shimizu, S.; Osumi, M.; Tanaka, A. Properties of catalase purified from a methanolgrown yeast, Kloeckera sp. 2201. Ear. J. Biochem. 1986, 155, 527-531.
    • (1986) Ear. J. Biochem. , vol.155 , pp. 527-531
    • Mozaffar, S.1    Ueda, M.2    Kitatsuji, K.3    Shimizu, S.4    Osumi, M.5    Tanaka, A.6
  • 79
  • 80
    • 10844276017 scopus 로고
    • Synthetic oxygen carriers related to biological systems
    • Jones, R. D.; Summerville, D. A.; Basolo, F. Synthetic oxygen carriers related to biological systems. Chem. Rev. 1979, 79, 139-179.
    • (1979) Chem. Rev. , vol.79 , pp. 139-179
    • Jones, R.D.1    Summerville, D.A.2    Basolo, F.3
  • 81
    • 0016260026 scopus 로고
    • Autoxidation of native oxymyoglobin from bovine heart muscle
    • Gotoh, T.; Shikama, K. Autoxidation of native oxymyoglobin from bovine heart muscle. Arch. Biochem. Biophys. 1974, 163, 476-481.
    • (1974) Arch. Biochem. Biophys. , vol.163 , pp. 476-481
    • Gotoh, T.1    Shikama, K.2
  • 83
    • 0032502724 scopus 로고    scopus 로고
    • The molecular mechanism of autoxidation for human oxyhemoglobin: Tilting of the distal histidine causes nonequivalent oxidation in the β chain
    • Tsuruga, M.; Matsuoka, A.; Hachimori, A.; Sugawara, Y.; Shikama, K. The molecular mechanism of autoxidation for human oxyhemoglobin: Tilting of the distal histidine causes nonequivalent oxidation in the β chain. J. Biol. Chem. 1998, 273, 8607-8615.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8607-8615
    • Tsuruga, M.1    Matsuoka, A.2    Hachimori, A.3    Sugawara, Y.4    Shikama, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.