메뉴 건너뛰기




Volumn 15, Issue 1, 2006, Pages 20-29

S-Nitrosohemoglobin: A mechanism for its formation in conjunction with nitrite reduction by deoxyhemoglobin

Author keywords

Hemoglobin; Hypoxia; Iron nitrosyl hemoglobin; Nitric oxide; Nitrite; S Nitrosohemoglobin

Indexed keywords

ASCORBIC ACID; COPPER COMPLEX; CYSTEINE; DEOXYHEMOGLOBIN; HEME; HEMOGLOBIN DERIVATIVE; NITRIC OXIDE; NITRITE; NITROSO DERIVATIVE; S NITROSOHEMOGLOBIN; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 33745497365     PISSN: 10898603     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.niox.2006.01.012     Document Type: Article
Times cited : (73)

References (60)
  • 1
    • 0031425115 scopus 로고    scopus 로고
    • A tutorial on the diffusibility and reactivity of free nitric oxide
    • Lancaster Jr. J.R. A tutorial on the diffusibility and reactivity of free nitric oxide. Nitric Oxide 1 (1997) 18-30
    • (1997) Nitric Oxide , vol.1 , pp. 18-30
    • Lancaster Jr., J.R.1
  • 2
    • 0032707717 scopus 로고    scopus 로고
    • Nitric oxide as a signaling molecule in the vascular system: an overview
    • Ignarro L.J., Cirino G., Casini A., and Napoli C. Nitric oxide as a signaling molecule in the vascular system: an overview. J. Cardiovasc. Pharmacol. 34 (1999) 879-886
    • (1999) J. Cardiovasc. Pharmacol. , vol.34 , pp. 879-886
    • Ignarro, L.J.1    Cirino, G.2    Casini, A.3    Napoli, C.4
  • 3
    • 0029875840 scopus 로고    scopus 로고
    • S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
    • Jia L., Bonaventura C., Bonaventura J., and Stamler J.S. 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
  • 6
    • 0035252076 scopus 로고    scopus 로고
    • Export by red blood cells of nitric oxide bioactivity
    • Pawloski J.R., Hess D.T., and Stamler J.S. 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
  • 8
    • 0344443777 scopus 로고    scopus 로고
    • Active nitric oxide produced in the red cell under hypoxic conditions by deoxyhemoglobin-mediated nitrite reduction
    • Nagababu E., Ramasamy S., Abernethy D.R., and Rifkind J.M. 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
  • 10
    • 0033638564 scopus 로고    scopus 로고
    • Nitrite uptake and metabolism and oxidant stress in human erythrocytes
    • May J.M., Qu Z.C., Xia L., and Cobb C.E. Nitrite uptake and metabolism and oxidant stress in human erythrocytes. Am. J. Physiol. Cell Physiol. 279 (2000) 1946-1954
    • (2000) Am. J. Physiol. Cell Physiol. , vol.279 , pp. 1946-1954
    • May, J.M.1    Qu, Z.C.2    Xia, L.3    Cobb, C.E.4
  • 12
    • 0030036756 scopus 로고    scopus 로고
    • Studies on the reaction mechanism for reductive nitrosylation of ferrihemoproteins in buffer solutions
    • Hoshino M., Maeda M., Konishi R., Seki H., and Ford P.C. Studies on the reaction mechanism for reductive nitrosylation of ferrihemoproteins in buffer solutions. J. Am. Chem. Soc. 118 (1996) 5702-5707
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 5702-5707
    • Hoshino, M.1    Maeda, M.2    Konishi, R.3    Seki, H.4    Ford, P.C.5
  • 13
    • 0002621915 scopus 로고    scopus 로고
    • Interactions of nitric oxide with heme proteins using UV-vis spectroscopy
    • stamler J.S., and Feelisch M. (Eds), Wiley, Chichester, UK
    • Kharnitov V.G., Bonaventura C., and Sharma V.S. Interactions of nitric oxide with heme proteins using UV-vis spectroscopy. In: stamler J.S., and Feelisch M. (Eds). Methods in Nitric Oxide Research (1996), Wiley, Chichester, UK 39-45
    • (1996) Methods in Nitric Oxide Research , pp. 39-45
    • Kharnitov, V.G.1    Bonaventura, C.2    Sharma, V.S.3
  • 14
    • 0032902721 scopus 로고    scopus 로고
    • Relationships between nitric oxide, nitroxyl ion, nitrosonium cation and peroxynitrite
    • Hughes M.N. Relationships between nitric oxide, nitroxyl ion, nitrosonium cation and peroxynitrite. Biochim. Biophys. Acta 1411 (1999) 263-272
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 263-272
    • Hughes, M.N.1
  • 15
    • 0036174890 scopus 로고    scopus 로고
    • The biochemistry and physiology of S-nitrosothiols
    • Hogg N. The biochemistry and physiology of S-nitrosothiols. Annu. Rev. Pharmacol. Toxicol. 42 (2002) 585-600
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 585-600
    • Hogg, N.1
  • 19
    • 0031740405 scopus 로고    scopus 로고
    • Concerted nitric oxide/oxygen delivery by hemoglobin
    • McMahon T.J., and Stamler J.S. Concerted nitric oxide/oxygen delivery by hemoglobin. Methods Enzymol. 301 (1999) 99-114
    • (1999) Methods Enzymol. , vol.301 , pp. 99-114
    • McMahon, T.J.1    Stamler, J.S.2
  • 20
    • 0029780524 scopus 로고    scopus 로고
    • Mechanism of nitric oxide release from S-nitrosothiols
    • Singh R.J., Hogg N., Joseph J., and Kalyanaraman B. Mechanism of nitric oxide release from S-nitrosothiols. J. Biol. Chem. 271 (1996) 18596-18603
    • (1996) J. Biol. Chem. , vol.271 , pp. 18596-18603
    • Singh, R.J.1    Hogg, N.2    Joseph, J.3    Kalyanaraman, B.4
  • 21
    • 0000741366 scopus 로고    scopus 로고
    • Preparation and detection of S-nitrosothiols
    • Stamler J.S., and Feelisch M. (Eds), Wiley, Chichester, UK
    • Stamler J.S., and Feelisch M. Preparation and detection of S-nitrosothiols. In: Stamler J.S., and Feelisch M. (Eds). Methods in Nitric Oxide Research (2005), Wiley, Chichester, UK 521-539
    • (2005) Methods in Nitric Oxide Research , pp. 521-539
    • Stamler, J.S.1    Feelisch, M.2
  • 22
    • 0027762128 scopus 로고
    • Biological activity of S-nitrosothiols: the role of nitric oxide
    • Mathews W.R., and Kerr S.W. Biological activity of S-nitrosothiols: the role of nitric oxide. J. Pharmacol. Exp. Ther. 267 (1993) 1529-1537
    • (1993) J. Pharmacol. Exp. Ther. , vol.267 , pp. 1529-1537
    • Mathews, W.R.1    Kerr, S.W.2
  • 25
    • 0033988226 scopus 로고    scopus 로고
    • A chemiluminescense-based assay for S-nitrosoalbumin and other plasma S-nitrosothiols
    • Marley R., Feelisch M., Holt S., and Moore K. A chemiluminescense-based assay for S-nitrosoalbumin and other plasma S-nitrosothiols. Free. Radic. Res. 32 (2000) 1-9
    • (2000) Free. Radic. Res. , vol.32 , pp. 1-9
    • Marley, R.1    Feelisch, M.2    Holt, S.3    Moore, K.4
  • 26
    • 0036846736 scopus 로고    scopus 로고
    • Concomitant S-, N-, and heme-nitros(yl)ation in biological tissues and fluids: implications for the fate of NO in vivo
    • Feelisch M., Rassaf T., Mnaimneh S., Singh N., Bryan N.S., Jourd'heuil D., and Kelm M. Concomitant S-, N-, and heme-nitros(yl)ation in biological tissues and fluids: implications for the fate of NO in vivo. FASEB J. 16 (2002) 1775-1785
    • (2002) FASEB J. , vol.16 , pp. 1775-1785
    • Feelisch, M.1    Rassaf, T.2    Mnaimneh, S.3    Singh, N.4    Bryan, N.S.5    Jourd'heuil, D.6    Kelm, M.7
  • 27
    • 0037251861 scopus 로고    scopus 로고
    • Methodologies for the sensitive and specific measurement of S-nitrosothiols, iron-nitrosyls, and nitrite in biological samples
    • Yang B.K., Vivas E.X., Reiter C.D., and Gladwin M.T. Methodologies for the sensitive and specific measurement of S-nitrosothiols, iron-nitrosyls, and nitrite in biological samples. Free. Radic. Res. 37 (2003) 1-10
    • (2003) Free. Radic. Res. , vol.37 , pp. 1-10
    • Yang, B.K.1    Vivas, E.X.2    Reiter, C.D.3    Gladwin, M.T.4
  • 28
    • 1542373633 scopus 로고    scopus 로고
    • S-nitrosothiols in the blood: roles, amounts, and methods of analysis
    • Stamler J.S. S-nitrosothiols in the blood: roles, amounts, and methods of analysis. Circ. Res. 94 (2004) 414-417
    • (2004) Circ. Res. , vol.94 , pp. 414-417
    • Stamler, J.S.1
  • 30
    • 0030010784 scopus 로고    scopus 로고
    • Decomposition of S-nitrosoglutathione in the presence of copper ions and glutathione
    • Gorren A.C., Schrammel A., Schmidt K., and Mayer B. Decomposition of S-nitrosoglutathione in the presence of copper ions and glutathione. Arch. Biochem. Biophys. 330 (1996) 219-228
    • (1996) Arch. Biochem. Biophys. , vol.330 , pp. 219-228
    • Gorren, A.C.1    Schrammel, A.2    Schmidt, K.3    Mayer, B.4
  • 31
    • 0023274482 scopus 로고
    • Reaction of nitric oxide with heme proteins and model compounds of hemoglobin
    • Sharma V.S., Traylor T.G., Gardiner R., and Mizukami H. Reaction of nitric oxide with heme proteins and model compounds of hemoglobin. Biochemistry 26 (1987) 3837-3843
    • (1987) Biochemistry , vol.26 , pp. 3837-3843
    • Sharma, V.S.1    Traylor, T.G.2    Gardiner, R.3    Mizukami, H.4
  • 33
    • 0031015162 scopus 로고    scopus 로고
    • Characterisation of S-nitrosohaemoglobin by mass spectrometry
    • Ferranti P., Malorni A., Mamone G., Sannolo N., and Marino G. Characterisation of S-nitrosohaemoglobin by mass spectrometry. FEBS Lett. 400 (1997) 19-24
    • (1997) FEBS Lett. , vol.400 , pp. 19-24
    • Ferranti, P.1    Malorni, A.2    Mamone, G.3    Sannolo, N.4    Marino, G.5
  • 34
    • 0031590450 scopus 로고    scopus 로고
    • S-nitrosohemoglobin in the fetal circulation may represent a cycle for blood pressure regulation
    • Funai E.F., Davidson A., Seligman S.P., and Finlay T.H. S-nitrosohemoglobin in the fetal circulation may represent a cycle for blood pressure regulation. Biochem. Biophys. Res. Commun. 239 (1997) 875-877
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 875-877
    • Funai, E.F.1    Davidson, A.2    Seligman, S.P.3    Finlay, T.H.4
  • 37
    • 0028803686 scopus 로고
    • Kinetics of nitrosation of thiols by nitric oxide in the presence of oxygen
    • Kharitonov V.G., Sundquist A.R., and Sharma V.S. Kinetics of nitrosation of thiols by nitric oxide in the presence of oxygen. J. Biol. Chem. 270 (1995) 28158-28164
    • (1995) J. Biol. Chem. , vol.270 , pp. 28158-28164
    • Kharitonov, V.G.1    Sundquist, A.R.2    Sharma, V.S.3
  • 39
    • 0037470250 scopus 로고    scopus 로고
    • Reactions of deoxy-, oxy-, and methemoglobin with nitrogen monoxide. Mechanistic studies of the S-nitrosothiol formation under different mixing conditions
    • Herold S., and Rock G. Reactions of deoxy-, oxy-, and methemoglobin with nitrogen monoxide. Mechanistic studies of the S-nitrosothiol formation under different mixing conditions. J. Biol. Chem. 278 (2003) 6623-6634
    • (2003) J. Biol. Chem. , vol.278 , pp. 6623-6634
    • Herold, S.1    Rock, G.2
  • 40
    • 0025006512 scopus 로고
    • Redox reactivity of iron(III) porphyrins and heme proteins with nitric oxide. Nitrosyl transfer to carbon, oxygen, nitrogen, and sulfur
    • Wade R.S., and Castro C.E. Redox reactivity of iron(III) porphyrins and heme proteins with nitric oxide. Nitrosyl transfer to carbon, oxygen, nitrogen, and sulfur. Chem. Res. Toxicol. 3 (1990) 289-291
    • (1990) Chem. Res. Toxicol. , vol.3 , pp. 289-291
    • Wade, R.S.1    Castro, C.E.2
  • 41
    • 16444362504 scopus 로고    scopus 로고
    • Hemoglobin-mediated, hypoxia-induced vasodilation via nitric oxide: mechanism(s) and physiologic versus pathophysiologic relevance
    • Robinson J.M., and Lancaster Jr. J.R. Hemoglobin-mediated, hypoxia-induced vasodilation via nitric oxide: mechanism(s) and physiologic versus pathophysiologic relevance. Am. J. Repir. Cell. Mol. Biol. 32 (2005) 257-261
    • (2005) Am. J. Repir. Cell. Mol. Biol. , vol.32 , pp. 257-261
    • Robinson, J.M.1    Lancaster Jr., J.R.2
  • 42
    • 10444220188 scopus 로고    scopus 로고
    • The reaction between nitrite and hemoglobin: the role of nitrite in hemoglobin-mediated hypoxic vasodilation
    • Kim-Shapiro D.B., Gladwin M.T., Patel R.P., and Hogg N. The reaction between nitrite and hemoglobin: the role of nitrite in hemoglobin-mediated hypoxic vasodilation. J. Inorg. Biochem. 99 (2005) 237-246
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 237-246
    • Kim-Shapiro, D.B.1    Gladwin, M.T.2    Patel, R.P.3    Hogg, N.4
  • 43
    • 33745491610 scopus 로고    scopus 로고
    • S-nitrosohemoglobin formation: a mechanism involving electron delocalization in the heme pocket
    • Rifkind J.M., Nagababu E., and Ramasamy S. S-nitrosohemoglobin formation: a mechanism involving electron delocalization in the heme pocket. Biophys. J. 88 (2005) 391A
    • (2005) Biophys. J. , vol.88
    • Rifkind, J.M.1    Nagababu, E.2    Ramasamy, S.3
  • 44
    • 58149415056 scopus 로고
    • Structure and function of haemoglobin. 3. A three-dimensional fourier synthesis of human deoxyhaemoglobin at 5.5 Angstrom resolution
    • Muirhead H., Cox J.M., Mazzarella L., and Perutz M.F. Structure and function of haemoglobin. 3. A three-dimensional fourier synthesis of human deoxyhaemoglobin at 5.5 Angstrom resolution. J. Mol. Biol. 28 (1967) 117-156
    • (1967) J. Mol. Biol. , vol.28 , pp. 117-156
    • Muirhead, H.1    Cox, J.M.2    Mazzarella, L.3    Perutz, M.F.4
  • 45
    • 0022523277 scopus 로고
    • Nitrosyliron(III) hemoglobin: autoreduction and spectroscopy
    • Addison A.W., and Stephanos J.J. Nitrosyliron(III) hemoglobin: autoreduction and spectroscopy. Biochemistry 25 (1986) 4104-4113
    • (1986) Biochemistry , vol.25 , pp. 4104-4113
    • Addison, A.W.1    Stephanos, J.J.2
  • 46
    • 0037239903 scopus 로고    scopus 로고
    • Nitrite catalyzes reductive nitrosylation of the water-soluble Ferri-Heme model FeIII(TPPS) to FeII(TPPS)(NO)
    • Fernandez B.O., Lorkovic I.M., and Ford P.C. Nitrite catalyzes reductive nitrosylation of the water-soluble Ferri-Heme model FeIII(TPPS) to FeII(TPPS)(NO). Inorg. Chem. 42 (2003) 2-4
    • (2003) Inorg. Chem. , vol.42 , pp. 2-4
    • Fernandez, B.O.1    Lorkovic, I.M.2    Ford, P.C.3
  • 49
    • 0000093202 scopus 로고    scopus 로고
    • Ellipsoidal delocalization of tunneling electrons in long-range electron transfer proteins
    • Gruschus J.M., and Kuki A. Ellipsoidal delocalization of tunneling electrons in long-range electron transfer proteins. J. Phys. Chem. 103 (1999) 11407-11414
    • (1999) J. Phys. Chem. , vol.103 , pp. 11407-11414
    • Gruschus, J.M.1    Kuki, A.2
  • 50
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunneling in biological oxidation-reduction
    • Page C.C., Moser C.C., Chen X., and Dutton P.L. Natural engineering principles of electron tunneling in biological oxidation-reduction. Nature 402 (1999) 47-52
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 51
    • 0034804272 scopus 로고    scopus 로고
    • Release of nitric oxide from S-nitrosohemoglobin. Electron transfer as a response to deoxygenation
    • Pezacki J.P., Ship N.J., and Kluger R. Release of nitric oxide from S-nitrosohemoglobin. Electron transfer as a response to deoxygenation. J. Am. Chem. Soc. 123 (2001) 4615-4616
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 4615-4616
    • Pezacki, J.P.1    Ship, N.J.2    Kluger, R.3
  • 52
    • 0032558387 scopus 로고    scopus 로고
    • Superoxide produced in the heme pocket of the beta-chain of hemoglobin reacts with the beta-93 cysteine to produce a thiyl radical
    • Balagopalakrishna C., Abugo O.O., Horsky J., Manoharan P.T., Nagababu E., and Rifkind J.M. Superoxide produced in the heme pocket of the beta-chain of hemoglobin reacts with the beta-93 cysteine to produce a thiyl radical. Biochemistry 37 (1998) 13194-13202
    • (1998) Biochemistry , vol.37 , pp. 13194-13202
    • Balagopalakrishna, C.1    Abugo, O.O.2    Horsky, J.3    Manoharan, P.T.4    Nagababu, E.5    Rifkind, J.M.6
  • 53
    • 3342875505 scopus 로고    scopus 로고
    • Nitroxides scavenge myeloperoxidase-catalyzed thiyl radicals in model systems and in cells
    • Borisenko G.G., Martin I., Zhao Q., Amoscato A.A., and Kagan V.E. Nitroxides scavenge myeloperoxidase-catalyzed thiyl radicals in model systems and in cells. J. Am. Chem. Soc. 126 (2004) 9221-9232
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 9221-9232
    • Borisenko, G.G.1    Martin, I.2    Zhao, Q.3    Amoscato, A.A.4    Kagan, V.E.5
  • 55
    • 0024291092 scopus 로고
    • Spin trapping the cysteine thiyl radical with phenyl-N-t-butylnitrone
    • Graceffa P. Spin trapping the cysteine thiyl radical with phenyl-N-t-butylnitrone. Biochim. Biophys. Acta 954 (1988) 227-230
    • (1988) Biochim. Biophys. Acta , vol.954 , pp. 227-230
    • Graceffa, P.1
  • 56
    • 0033525201 scopus 로고    scopus 로고
    • An electron spin resonance spin-trapping investigation of the free radicals formed by the reaction of mitochondrial cytochrome c oxidase with H2O2
    • Chen Y.R., Gunther M.R., and Mason R.P. An electron spin resonance spin-trapping investigation of the free radicals formed by the reaction of mitochondrial cytochrome c oxidase with H2O2. J. Biol. Chem. 274 (1999) 3308-3314
    • (1999) J. Biol. Chem. , vol.274 , pp. 3308-3314
    • Chen, Y.R.1    Gunther, M.R.2    Mason, R.P.3
  • 57
    • 0021316138 scopus 로고
    • Spin trapping
    • Janzen E.G. Spin trapping. Methods Enzymol. 105 (1984) 188-198
    • (1984) Methods Enzymol. , vol.105 , pp. 188-198
    • Janzen, E.G.1
  • 58
    • 0014679219 scopus 로고
    • Changes in the 4-PDS-reactive -SH groups of hemoglobin associated with the binding of phosphates and ligands
    • Taketa F., and Morell S.A. Changes in the 4-PDS-reactive -SH groups of hemoglobin associated with the binding of phosphates and ligands. Anal. Biochem. 32 (1969) 169-714
    • (1969) Anal. Biochem. , vol.32 , pp. 169-714
    • Taketa, F.1    Morell, S.A.2
  • 59
    • 1842852208 scopus 로고    scopus 로고
    • Vasorelaxation by red blood cells and impairment in diabetes: reduced nitric oxide and oxygen delivery by glycated hemoglobin
    • James P.E., Lang D., Tufnell-Barret T., Milsom A.B., and Frenneaux M.P. Vasorelaxation by red blood cells and impairment in diabetes: reduced nitric oxide and oxygen delivery by glycated hemoglobin. Circ. Res. 94 (2004) 976-983
    • (2004) Circ. Res. , vol.94 , pp. 976-983
    • James, P.E.1    Lang, D.2    Tufnell-Barret, T.3    Milsom, A.B.4    Frenneaux, M.P.5
  • 60
    • 4444248457 scopus 로고    scopus 로고
    • Transduction of NO-bioactivity by the red blood cell in sepsis: novel mechanisms of vasodilation during acute inflammatory disease
    • Crawford J.H., Chacko B.K., Pruitt H.M., Piknova B., Hogg N., and Patel R.P. Transduction of NO-bioactivity by the red blood cell in sepsis: novel mechanisms of vasodilation during acute inflammatory disease. Blood 104 (2004) 1375-1382
    • (2004) Blood , vol.104 , pp. 1375-1382
    • Crawford, J.H.1    Chacko, B.K.2    Pruitt, H.M.3    Piknova, B.4    Hogg, N.5    Patel, R.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.