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Volumn 39, Issue 2, 2005, Pages 145-151

Rates of nitric oxide dissociation from hemoglobin

Author keywords

Dissociation kinetics; Electron paramagnetic resonance; Hemoglobin; Nitric oxide

Indexed keywords

DITHIOCARBAMIC ACID; HEME; HEMOGLOBIN; HEMOGLOBIN S; HISTIDINE; IRON; NITRIC OXIDE; PROLINE;

EID: 20444453680     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2005.03.001     Document Type: Article
Times cited : (45)

References (49)
  • 1
    • 0000707453 scopus 로고
    • Nitric-oxide activates guanylate cyclase and increases guanosine 3′-5′-cyclic monophosphate levels in various tissue preparations
    • W.P. Arnold, C.K. Mittal, S. Katsuki, and F. Murad Nitric-oxide activates guanylate cyclase and increases guanosine 3′-5′-cyclic monophosphate levels in various tissue preparations Proc. Natl. Acad. Sci. USA 74 1977 3203 3207
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3203-3207
    • Arnold, W.P.1    Mittal, C.K.2    Katsuki, S.3    Murad, F.4
  • 2
    • 0019195506 scopus 로고
    • The obligatory role of endothelial-cells in the relaxation of arterial smooth-muscle by acetylcholine
    • R.F. Furchgott, and J.V. Zawadzki The obligatory role of endothelial-cells in the relaxation of arterial smooth-muscle by acetylcholine Nature 288 1980 373 376
    • (1980) Nature , vol.288 , pp. 373-376
    • Furchgott, R.F.1    Zawadzki, J.V.2
  • 3
    • 0023518452 scopus 로고
    • Endothelium-derived relaxing factor from pulmonary-artery and vein possesses pharmacological and chemical-properties identical to those of nitric-oxide radical
    • L.J. Ignarro, R.E. Byrns, G.M. Buga, and K.S. Wood Endothelium-derived relaxing factor from pulmonary-artery and vein possesses pharmacological and chemical-properties identical to those of nitric-oxide radical Circ. Res. 61 1987 866 879
    • (1987) Circ. Res. , vol.61 , pp. 866-879
    • Ignarro, L.J.1    Byrns, R.E.2    Buga, G.M.3    Wood, K.S.4
  • 4
    • 0023505509 scopus 로고
    • Endothelium-derived relaxing factor produced and released from artery and vein is nitric-oxide
    • L.J. Ignarro, G.M. Buga, K.S. Wood, R.E. Byrns, and G. Chaudhuri Endothelium-derived relaxing factor produced and released from artery and vein is nitric-oxide Proc. Natl. Acad. Sci. USA 84 1987 9265 9269
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 9265-9269
    • Ignarro, L.J.1    Buga, G.M.2    Wood, K.S.3    Byrns, R.E.4    Chaudhuri, G.5
  • 5
    • 0001676319 scopus 로고
    • Biochemical and pharmacological properties of endothelium-derived relaxing factor and its similarity to nitric oxide radical
    • P.M. Vanhoutte Raven New York
    • L.J. Ignarro, R.E. Byrns, and K.S. Wood Biochemical and pharmacological properties of endothelium-derived relaxing factor and its similarity to nitric oxide radical P.M. Vanhoutte Vasodilatation: vascular smooth muscle, peptides, autonomic nerves, and endothelium 1988 Raven New York 427 435
    • (1988) Vasodilatation: Vascular Smooth Muscle, Peptides, Autonomic Nerves, and Endothelium , pp. 427-435
    • Ignarro, L.J.1    Byrns, R.E.2    Wood, K.S.3
  • 6
    • 0023198721 scopus 로고
    • Nitric-oxide release accounts for the biological-activity of endothelium-derived relaxing factor
    • R.M.J. Palmer, A.G. Ferrige, and S. Moncada Nitric-oxide release accounts for the biological-activity of endothelium-derived relaxing factor Nature 327 1987 524 526
    • (1987) Nature , vol.327 , pp. 524-526
    • Palmer, R.M.J.1    Ferrige, A.G.2    Moncada, S.3
  • 7
    • 0000014429 scopus 로고
    • Studies on relaxation of rabbit aorta by sodium nitrite: The basis for the proposal that the acid-activatable factor from bovine retractor penis is inorganic nitrite and the endothelium-derived relaxing factor is nitric oxide
    • P.M. Vanhoutte Raven New York
    • R.F. Furchgott Studies on relaxation of rabbit aorta by sodium nitrite: the basis for the proposal that the acid-activatable factor from bovine retractor penis is inorganic nitrite and the endothelium-derived relaxing factor is nitric oxide P.M. Vanhoutte Vasodilatation: vascular smooth muscle, peptides, autonomic nerves, and endothelium 1988 Raven New York 401 414
    • (1988) Vasodilatation: Vascular Smooth Muscle, Peptides, Autonomic Nerves, and Endothelium , pp. 401-414
    • Furchgott, R.F.1
  • 9
    • 1342328188 scopus 로고    scopus 로고
    • The biochemistry of nitric oxide, nitrite, and hemoglobin: Role in blood flow regulation
    • M.T. Gladwin, J.H. Crawford, and R.P. Patel The biochemistry of nitric oxide, nitrite, and hemoglobin: role in blood flow regulation Free Radic. Biol. Med. 36 2004 707 717
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 707-717
    • Gladwin, M.T.1    Crawford, J.H.2    Patel, R.P.3
  • 10
    • 0034778939 scopus 로고    scopus 로고
    • Nitric oxide therapy in sickle cell disease
    • M.T. Gladwin, and A.N. Schechter Nitric oxide therapy in sickle cell disease Semin. Hematol. 38 2001 333 342
    • (2001) Semin. Hematol. , vol.38 , pp. 333-342
    • Gladwin, M.T.1    Schechter, A.N.2
  • 11
    • 0037372314 scopus 로고    scopus 로고
    • An emerging role for nitric oxide in sickle cell disease vascular homeostasis and therapy
    • C.D. Reiter, and M.T. Gladwin An emerging role for nitric oxide in sickle cell disease vascular homeostasis and therapy Curr. Opin. Hematol. 10 2003 99 107
    • (2003) Curr. Opin. Hematol. , vol.10 , pp. 99-107
    • Reiter, C.D.1    Gladwin, M.T.2
  • 13
    • 1242351237 scopus 로고    scopus 로고
    • Hemoglobin-nitric oxide cooperativity: Is no the third respiratory ligand?
    • D.B. Kim-Shapiro Hemoglobin-nitric oxide cooperativity: Is no the third respiratory ligand? Free Radic. Biol. Med. 36 2004 402 412
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 402-412
    • Kim-Shapiro, D.B.1
  • 18
    • 0035252076 scopus 로고    scopus 로고
    • Export by red blood cells of nitric oxide bioactivity
    • J.R. Pawloski, D.T. Hess, and J.S. Stamler Export by red blood cells of nitric oxide bioactivity Nature 409 2001 622 626
    • (2001) Nature , vol.409 , pp. 622-626
    • Pawloski, J.R.1    Hess, D.T.2    Stamler, J.S.3
  • 20
    • 0029875840 scopus 로고    scopus 로고
    • S-Nitrosohaemoglobin: A dynamic activity of blood involved in vascular control
    • L. Jia, C. Bonaventura, J. Bonaventura, and J.S. Stamler S-Nitrosohaemoglobin: a dynamic activity of blood involved in vascular control Nature 380 1996 221 226
    • (1996) Nature , vol.380 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 23
    • 0344443777 scopus 로고    scopus 로고
    • Active nitric oxide produced in the red cell under hypoxic conditions by deoxyhemoglobin-mediated nitrite reduction
    • E. Nagababu, S. Ramasamy, D.R. Abernethy, and J.M. Rifkind Active nitric oxide produced in the red cell under hypoxic conditions by deoxyhemoglobin- mediated nitrite reduction J. Biol. Chem. 278 2003 46349 46356
    • (2003) J. Biol. Chem. , vol.278 , pp. 46349-46356
    • Nagababu, E.1    Ramasamy, S.2    Abernethy, D.R.3    Rifkind, J.M.4
  • 24
    • 0034730133 scopus 로고    scopus 로고
    • Relative role of heme nitrosylation and beta-cysteine 93 nitrosation in the transport and metabolism of nitric oxide by hemoglobin in the human circulation
    • M.T. Gladwin, F.P. Ognibene, L.K. Pannell, J.S. Nichols, M.E. Pease-Fye, J.H. Shelhamer, and A.N. Schechter Relative role of heme nitrosylation and beta-cysteine 93 nitrosation in the transport and metabolism of nitric oxide by hemoglobin in the human circulation Proc. Natl. Acad. Sci. USA 97 2000 9943 9948
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9943-9948
    • Gladwin, M.T.1    Ognibene, F.P.2    Pannell, L.K.3    Nichols, J.S.4    Pease-Fye, M.E.5    Shelhamer, J.H.6    Schechter, A.N.7
  • 25
    • 0017112413 scopus 로고
    • Cooperativity in dissociation of nitric-oxide from hemoglobin
    • E.G. Moore, and Q.H. Gibson Cooperativity in dissociation of nitric-oxide from hemoglobin J. Biol. Chem. 251 1976 2788 2794
    • (1976) J. Biol. Chem. , vol.251 , pp. 2788-2794
    • Moore, E.G.1    Gibson, Q.H.2
  • 26
    • 0018087302 scopus 로고
    • Dissociation of NO from nitrosylhemoglobin
    • V.S. Sharma, and H.M. Ranney Dissociation of NO from nitrosylhemoglobin J. Biol. Chem. 253 1978 6467 6472
    • (1978) J. Biol. Chem. , vol.253 , pp. 6467-6472
    • Sharma, V.S.1    Ranney, H.M.2
  • 27
    • 0014429937 scopus 로고
    • Paramagnetic resonance study of nitric oxide hemoglobin
    • H. Kon Paramagnetic resonance study of nitric oxide hemoglobin J. Biol. Chem. 243 1968 4350 4357
    • (1968) J. Biol. Chem. , vol.243 , pp. 4350-4357
    • Kon, H.1
  • 28
    • 0017193799 scopus 로고
    • Equilibrium between 6-coordinated and 5-coordinated hemes in nitrosylhemoglobin - Interpretation of electron-spin resonance-spectra
    • A. Szabo, and M.F. Perutz Equilibrium between 6-coordinated and 5-coordinated hemes in nitrosylhemoglobin - interpretation of electron-spin resonance-spectra Biochemistry-US 15 1976 4427 4428
    • (1976) Biochemistry-US , vol.15 , pp. 4427-4428
    • Szabo, A.1    Perutz, M.F.2
  • 29
    • 0018575001 scopus 로고
    • Nmr-studies of the quaternary structure and heterogeneity of nitrosylhemoglobin and methemoglobin
    • T.H. Huang Nmr-studies of the quaternary structure and heterogeneity of nitrosylhemoglobin and methemoglobin J. Biol. Chem. 254 1979 1467 1474
    • (1979) J. Biol. Chem. , vol.254 , pp. 1467-1474
    • Huang, T.H.1
  • 30
    • 0018596293 scopus 로고
    • Spectral transitions of nitrosyl hemes during ligand-binding to hemoglobin
    • R. Hille, J.S. Olson, and G. Palmer Spectral transitions of nitrosyl hemes during ligand-binding to hemoglobin J. Biol. Chem. 254 1979 2110 2120
    • (1979) J. Biol. Chem. , vol.254 , pp. 2110-2120
    • Hille, R.1    Olson, J.S.2    Palmer, G.3
  • 31
    • 0032493731 scopus 로고    scopus 로고
    • Electron paramagnetic resonance and oxygen binding studies of alpha-nitrosyl hemoglobin - A novel oxygen carrier having no-assisted allosteric functions
    • T. Yonetani, A. Tsuneshige, Y.X. Zhou, and X.S. Chen Electron paramagnetic resonance and oxygen binding studies of alpha-nitrosyl hemoglobin - a novel oxygen carrier having no-assisted allosteric functions J. Biol. Chem. 273 1998 20323 20333
    • (1998) J. Biol. Chem. , vol.273 , pp. 20323-20333
    • Yonetani, T.1    Tsuneshige, A.2    Zhou, Y.X.3    Chen, X.S.4
  • 33
    • 0027989397 scopus 로고
    • Nitric-oxide production during endotoxic-shock in carbon tetrachloride-treated rats
    • W. Chamulitrat, S.J. Jordan, and R.P. Mason Nitric-oxide production during endotoxic-shock in carbon tetrachloride-treated rats Mol. Pharmacol. 46 1994 391 397
    • (1994) Mol. Pharmacol. , vol.46 , pp. 391-397
    • Chamulitrat, W.1    Jordan, S.J.2    Mason, R.P.3
  • 34
    • 0027074184 scopus 로고
    • Nitric-oxide hemoglobin in patients receiving nitroglycerin as detected by electron-paramagnetic resonance spectroscopy
    • L.R. Cantilena, R.P. Smith, S. Frasur, H. Kruszyna, R. Kruszyna, and D.E. Wilcox Nitric-oxide hemoglobin in patients receiving nitroglycerin as detected by electron-paramagnetic resonance spectroscopy J. Lab. Clin. Med. 120 1992 902 907
    • (1992) J. Lab. Clin. Med. , vol.120 , pp. 902-907
    • Cantilena, L.R.1    Smith, R.P.2    Frasur, S.3    Kruszyna, H.4    Kruszyna, R.5    Wilcox, D.E.6
  • 37
    • 0141448327 scopus 로고    scopus 로고
    • EPR spectroscopy studies on the structural transition of nitrosyl hemoglobin in the arterial-venous cycle of DEANO-treated rats as it relates to the proposed nitrosyl hemoglobin/nitrosothiol hemoglobin exchange
    • A.R. Jaszewski, Y.C. Fann, Y.R. Chen, K. Sato, J. Corbett, and R.P. Mason EPR spectroscopy studies on the structural transition of nitrosyl hemoglobin in the arterial-venous cycle of DEANO-treated rats as it relates to the proposed nitrosyl hemoglobin/nitrosothiol hemoglobin exchange Free Radic. Biol. Med. 35 2003 444 451
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 444-451
    • Jaszewski, A.R.1    Fann, Y.C.2    Chen, Y.R.3    Sato, K.4    Corbett, J.5    Mason, R.P.6
  • 38
    • 0028223401 scopus 로고
    • Esr spectral transition by arteriovenous cycle in nitric-oxide hemoglobin of cytokine-treated rats
    • H. Kosaka, Y. Sawai, H. Sakaguchi, E. Kumura, N. Harada, M. Watanabe, and T. Shiga Esr spectral transition by arteriovenous cycle in nitric-oxide hemoglobin of cytokine-treated rats Am. J. Physiol. 266 1994 C1400 C1405
    • (1994) Am. J. Physiol. , vol.266
    • Kosaka, H.1    Sawai, Y.2    Sakaguchi, H.3    Kumura, E.4    Harada, N.5    Watanabe, M.6    Shiga, T.7
  • 40
    • 0033649852 scopus 로고    scopus 로고
    • Confirmation of a unique intra-dimer cooperativity in the human hemoglobin alpha(1)beta(1) half-oxygenated intermediate supports the symmetry rule model of allosteric regulation
    • G.K. Ackers, J.M. Holt, Y.W. Huang, Y. Grinkova, A.L. Klinger, and I. Denisov Confirmation of a unique intra-dimer cooperativity in the human hemoglobin alpha(1)beta(1) half-oxygenated intermediate supports the symmetry rule model of allosteric regulation Proteins 2000 23 43
    • (2000) Proteins , pp. 23-43
    • Ackers, G.K.1    Holt, J.M.2    Huang, Y.W.3    Grinkova, Y.4    Klinger, A.L.5    Denisov, I.6
  • 42
    • 0037072945 scopus 로고    scopus 로고
    • Global allostery model of hemoglobin - Modulation of O-2 affinity, cooperativity, and Bohr effect by heterotropic allosteric effectors
    • T. Yonetani, S. Park, A. Tsuneshige, K. Imai, and K. Kanaori Global allostery model of hemoglobin - modulation of O-2 affinity, cooperativity, and Bohr effect by heterotropic allosteric effectors J. Biol. Chem. 277 2002 34508 34520
    • (2002) J. Biol. Chem. , vol.277 , pp. 34508-34520
    • Yonetani, T.1    Park, S.2    Tsuneshige, A.3    Imai, K.4    Kanaori, K.5
  • 44
    • 3142606635 scopus 로고    scopus 로고
    • S-Nitrosohemoglobin: An allosteric mediator of NO group function in mammalian vasculature
    • E.J. Frehm, J. Bonaventura, and A.J. Gow S-Nitrosohemoglobin: an allosteric mediator of NO group function in mammalian vasculature Free Radic. Biol. Med. I37 2004 442 453
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 442-453
    • Frehm, E.J.1    Bonaventura, J.2    Gow, A.J.3
  • 45
    • 0030583294 scopus 로고    scopus 로고
    • EPR and laser flash photolysis studies of the reaction of nitric oxide with water soluble NO trap Fe(II)-proline-dithiocarbamate complex
    • S.V. Paschenko, V.V. Khramtsov, M.P. Skatchkov, V.F. Plyusnin, and E. Bassenge EPR and laser flash photolysis studies of the reaction of nitric oxide with water soluble NO trap Fe(II)-proline-dithiocarbamate complex Biochem. Biophys. Res. Commun. 225 1996 577 584
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 577-584
    • Paschenko, S.V.1    Khramtsov, V.V.2    Skatchkov, M.P.3    Plyusnin, V.F.4    Bassenge, E.5
  • 46
    • 0014670514 scopus 로고
    • Preparation and properties of a- and b-chains from human hemoglobin
    • G. Geraci, L.J. Parkhurst, and Q.H. Gibson Preparation and properties of a- and b-chains from human hemoglobin J. Biol. Chem. 17 1969 4664 4667
    • (1969) J. Biol. Chem. , vol.17 , pp. 4664-4667
    • Geraci, G.1    Parkhurst, L.J.2    Gibson, Q.H.3
  • 47
    • 0016589435 scopus 로고
    • Conformation, co-operativity and ligand-binding in human hemoglobin
    • R. Cassoly, and Q.H. Gibson Conformation, co-operativity and ligand-binding in human hemoglobin J. Mol. Biol. 91 1975 301 313
    • (1975) J. Mol. Biol. , vol.91 , pp. 301-313
    • Cassoly, R.1    Gibson, Q.H.2
  • 48
    • 0031006612 scopus 로고    scopus 로고
    • Kinetics of nitric oxide dissociation from five- and six-coordinate nitrosyl hemes and heme proteins, including soluble guanylate cyclase
    • V.G. Kharitonov, V.S. Sharma, D. Magde, and D. Koesling Kinetics of nitric oxide dissociation from five- and six-coordinate nitrosyl hemes and heme proteins, including soluble guanylate cyclase Biochemistry-US 36 1997 6814 6818
    • (1997) Biochemistry-US , vol.36 , pp. 6814-6818
    • Kharitonov, V.G.1    Sharma, V.S.2    Magde, D.3    Koesling, D.4
  • 49
    • 0032400370 scopus 로고    scopus 로고
    • Regeneration of the ferrous heme of soluble guanylate cyclase from the nitric oxide complex: Acceleration by thiols and oxyhemoglobin
    • P.E. Brandish, W. Buechler, and M.A. Marletta Regeneration of the ferrous heme of soluble guanylate cyclase from the nitric oxide complex: acceleration by thiols and oxyhemoglobin Biochemistry-US 37 1998 16898 16907
    • (1998) Biochemistry-US , vol.37 , pp. 16898-16907
    • Brandish, P.E.1    Buechler, W.2    Marletta, M.A.3


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