References
- Antonini, E. and Brunori, M. (1971) Hemoglobin and myoglobin in their reaction with ligands, North-Holland Publishing Co., Amsterdam.
- Arakawa, T. and Timasheff, S. N. (1982) Stabilization of protein structure by sugars. Biochemistry 21, 6534-6544.
- Baldwin, J. N. and Ye, R. P. (1988) Catalytic reduction of myoglobin and hemoglobin at chemically modified electrodes containing methylene blue. Anal. Chem. 60, 2263-2268. https://doi.org/10.1021/ac00171a021
- Banerjee, R. and Cassoly, R. (1969) Preparation and properties of the isolated alpha and beta chains of human hemoglobin in the ferri state. Investigation of oxidation-reduction equilibria. J Mol. Biol. 42, 337-349. https://doi.org/10.1016/0022-2836(69)90047-3
- Benesch, R. E. Benesch, R. and Yung, S. (1973) Equations for the spectrophotometric analysis of hemoglobin mixtures. Anal. Biochem. 55, 245-248. https://doi.org/10.1016/0003-2697(73)90309-6
- Berman, M. Benesch, R. and Benesch, R. E. (1971) The removal of organic phosphates from hemoglobin. Arch. Biochem. Biophys. 145, 236-239. https://doi.org/10.1016/0003-9861(71)90031-2
-
Bonaventura, C. Tesh, S. Faulkner, K. M. Kraiter, D. and Crumbliss, A. L. (1998) Conformational fluctuations in deoxy hemoglobin revealed as a major contributor to anionic modulation of function through studies of the oxygenation and oxidation of hemoglobin
$A_{0}$ and Hemoglobin Deer Lodge b2(NA2) His$\rightarrow$ Arg). Biochemistry 35, 496-506. - Bordbar, A. K. Moosavi-MovalIedi, A. A. and Saboury, A. A. (1996) Comparative thermodynamical stability of bovine and pigeon hemoglobin by interaction with sodium n-dodecyl sulphate. Thermochimica Acta 287, 343-349. https://doi.org/10.1016/S0040-6031(96)03000-6
- Boyiri, T. Safo, M. K. Danso-DangualI, R. E. Kister, J. Poyart, C. and AbralIam, D. J. (1995) Bisaldehyde allosteric effectors as molecular ratchets and probes. Biochemistry 34, 15021-15036. https://doi.org/10.1021/bi00046a008
- Brabec, V (1996) Experimental Techniques in Bioelectrochem. Vol. 3 Birkhauser Verlag, Germany.
- Brantley, R. E. Jr. Semerdon, S. J. Wilkinson, A. J. Singleton, E. W. and Olson, J. S. (1993) The mechanism of autoxidation of myoglobin. J. Biol. Chem. 268, 6995-7010.
- Bunn, H. F. and Forget, B. G. (1986) Hemoglobin: Molecular Genetic and Clinical Aspects, Saunders Company, Philadelphia, PA.
- Coletta, M. Ascenzi, P. Santucci, R. Bertollini, A. and Amconi, G. (1993) Interaction of inositol hexakisphosphate with liganded ferrous human hemoglobin, direct evidence for two functionally operative binding site. Biochem. Biophys. Acta 1162, 309-314. https://doi.org/10.1016/0167-4838(93)90295-3
- Desbois, A. and Bangerjee, R. (1975) Effects of polyvalent anion binding to hemoglobin on oxygen and oxidation-reduction equilibria and their relevance to allosteric transition. J Mol.Biol. 92, 479-493. https://doi.org/10.1016/0022-2836(75)90293-4
-
Dickerson, L. D. Sauer-Masarwa, A. Herron, N. Fendrick, C. M. and Busch, D.H. (1993) The electron-transfer mechanism of autoxidation for hemoglobin, myoglobin, and their iron (
$\Pi$ ) cyclidene models. J. Am. Chem. Soc. 115, 3623-3626. https://doi.org/10.1021/ja00062a028 - Dickinson, L. C. and Chien, J. C. (1975) Electron transfer between hemoglobin and coboglobin mediated by methylene blue. J. Am. Chem. Soc. 97, 2620-2625. https://doi.org/10.1021/ja00843a005
- Dong, A. Huang, P. Caughey, B. and Caughey, W. S. (1995) Infrared analysis of ligand and oxidation induced conformational changes in hemoglobins and myoglobins. Arch. Biochem. Biophys. 316, 893-898. https://doi.org/10.1006/abbi.1995.1120
- Fauikner, K. M. Bonaventura, C. and Crumbliss, A. L. (1995) A spectroelectrochemical method for differentiation of steric and electronic effects in hemoglobin and myoglobins. J. Biol. Chem. 270, 13404-13412.
- Freifelder, D. (1982) Physical Biochemistry: Applications to Biology, W. H. Freeman and Company, New York, New York.
-
Gary, R. D. and Gibson, Q. H. (1971) The effect of inositol hexaphosphate on the kinetics of CO and
$O_{2}$ binding by human hemoglobin. J. Biol. Chem. 246, 7158-7174. - Geraci, S. and Sada, A. (1972) Reactivity of the 93 sulphydryls of human hemoglobin A: influence of the C-terminal residues. J. Mol. Biol. 70, 729-734. https://doi.org/10.1016/0022-2836(72)90571-2
- Ho, C. Eaton, W. A. Collman, J. P. Gibson, Q. H. Leigh, J. S. Jr. Margoliash, E. Moffat, K. and Scheidt, W. R. (1982) Hemoglobin and Oxygen Binding, Macmillan Press. Ltd. London.
- Karniyama, T. Sadahide, Y. Nogusa, Y. and Gekko, K. (1999) Polyol induced molten globule of cytochrome C: an evidence for stabilization by hydrophobic interaction. Biochim. Biophys. Acta 1434, 44-57. https://doi.org/10.1016/S0167-4838(99)00159-4
- Kilmartin, J. V. (1973) The interaction of inositol hexaphosphate with methaemoglobin. Biochem. J. 133,725-733. https://doi.org/10.1042/bj1330725
- MacDonald, V. W. and Charache, S. (1982) Comparison of the effects of lower monohydric alcohol and inositol hexaphosphate on the oxidation of hemoglobin by menadion. Biochim. Biophys. Acta 705, 48-54. https://doi.org/10.1016/0167-4838(82)90334-X
- Mansouri, A. and Winterhalter, K. H. (1974) Nonequivalence of chains in hemoglobin oxidation and oxygen binding, effect of organic phosphates. Biochemistry 13, 3311-3314. https://doi.org/10.1021/bi00713a021
- Mizukoshi, H. Itoh, M. Matsakawa, S. Mawatari, K. and Yoneyama, Y. (1982) Tryptophan fluorescence of human hemoglobin. Biochim. Biophys. Acta 700, 143-147. https://doi.org/10.1016/0167-4838(82)90090-5
- Moosavi-Movahedi, A. A. Rabbani, A. Goodarzi, M. and Goliaei, B. (1989) Thermodynamic studies of the interaction of sodium n-dodecyl sulphate with histone H1. Thermochimica Acta 154, 205-212. https://doi.org/10.1016/0040-6031(89)85456-5
- Moosavi-Movahedi, A. A. and Ghobadi, S. (1991) Thermochemical analysis of the interaction between aspergillus niger catalase and sodium n-dodecyl sulphate. Thermochimica Acta 189, 201-207. https://doi.org/10.1016/0040-6031(91)87116-E
- Moosavi-Movahedi, A. A. (1994) lnteraction of aspergillus niger catalase with sodium n-dodecyl sulphate. lUPAC 66, 71-75.
- Moosavi-Movahedi, A. A. Naderi, G. A. and Farzami, B. (1994) Denaturation behavior of calmodulin in guanidine hydrochloride, urea, sodium n-dodecyl sulphate and dodecyl trirnethylammonium bromide. Thermochimica Acta 239, 61-71.
- Moosavi-Movahedi, A. A. Nazari, K. and Saboury, A. A. (1997) Denaturation of horseradish peroxidase with sodium n-dodecyl sulphate and dodecyl trimethyl ammonium bromide. Colloid and Surfaces B: Biointerfaces 9, 123-130. https://doi.org/10.1016/S0927-7765(97)00016-7
- Nazari, K. Saboury, A. A. and Moosavi-Movahedi, A. A. (1997) Enthalpy investigation for elucidation of the transition concentration for the interaction of horseradish peroxidase with surfactants. Themochimica Acta 302, 131-135. https://doi.org/10.1016/S0040-6031(97)00211-6
- Riggs, A. (1981) Preparation of blood hemoglobins of vertebrates. Methods Enzymol. 76, 5-29. https://doi.org/10.1016/0076-6879(81)76111-1
- Safo, M. K. Moure, C. M. Bumett, J. C. Joshi, G. S. and Abraham, D. J. (2001) High-resolution crystal structure of deoxy hemoglobin complexed with a potent allosteric effector. Protein Science 10, 951-957. https://doi.org/10.1110/ps.50601
- Satoh, Y. and Shikama, K. (1981) Autoxidation of oxymyoglobin. A nucleophilic displacement mechanism. J. Biol. Chem. 256, 10272-10275.
- Schlereth, D. D. and Mantele, W. (1992) Redox-induced conformational changes in myoglobin and hemoglobin: electrochemistry and ultraviolet-visible and fourier transform infrared difference spectroscopy at surface-modified gold electrodes in an ultra-thin-Iayer spectroelectrochemical cell. Biochemistry 31, 7494-7502. https://doi.org/10.1021/bi00148a009
- Shikama, K. (1984) A controversy on the mechanism of autoxidation of oxymyoglobin and oxyhaemoglobin: oxidation, dissociation, or displacement? Biochem. J. 223, 279-280. https://doi.org/10.1042/bj2230279
- Skoog, D. A. and Leary, J. J. (1992) Principles of Instrumental Analysis, Saunders College Publishing, 4th ed. New York, New York.
- Stargardt, J. F. Awkridge, F. M. and Lanrum, H. L. (1978) Reversible heterogeneous reduction and oxidation of sperm whale myoglobin at a surface modified gold minigrid electrode. Anal. Chem. 50, 930-932. https://doi.org/10.1021/ac50029a026
- Wallace, W. J. Houtchens, R. A. Maxwell, J. C. and Caughey, W. S. (1982) Mechanism of autoxidation for hemoglobins and myoglobins. promotion of superoxide production by protons and anions. J. Biol. Chem. 257, 4966-4977.
- William, R. C. Jr. and Tsay, K. Y. (1973) A convenient chromatographic method for the preparation of human hemoglobin. Anal. Biochem. 54, 137-145. https://doi.org/10.1016/0003-2697(73)90256-X
- Zavodnik, I. B. Piletskaia T. P. and Stepuro, l. I. (1992) Autoxidation and oxygenation of human hemoglobin. Mol. Biol. (Mosk) 26, 321-327.
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