메뉴 건너뛰기




Volumn 50, Issue 1, 2013, Pages 8-19

The oxidative denitrosylation mechanism and nitric oxide release from human fetal and adult hemoglobin, an experimentally based model simulation study

Author keywords

Fetal hemoglobin; Nitric oxide; Nitrite; Sickle cell disease; Vasodilation

Indexed keywords

DEOXYHEMOGLOBIN; HEMOGLOBIN F; NITRIC OXIDE; NITRITE; OXYHEMOGLOBIN;

EID: 84869870660     PISSN: 10799796     EISSN: 10960961     Source Type: Journal    
DOI: 10.1016/j.bcmd.2012.08.006     Document Type: Article
Times cited : (19)

References (33)
  • 1
    • 0032789444 scopus 로고    scopus 로고
    • Nitric oxide: a unique endogenous signaling molecule in vascular biology
    • Ignarro L.J. Nitric oxide: a unique endogenous signaling molecule in vascular biology. Biosci. Rep. 1999, 19:51-71.
    • (1999) Biosci. Rep. , vol.19 , pp. 51-71
    • Ignarro, L.J.1
  • 4
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: a plausible model
    • Monod J., Wyman J., Changeux J.-P. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 1965, 12:88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 5
    • 0029875840 scopus 로고    scopus 로고
    • S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
    • Jia L., Bonaventura C., Bonaventura J., Stamler J.S. S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature 1996, 380:221-226.
    • (1996) Nature , vol.380 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 7
    • 0016192332 scopus 로고
    • Ligand-dependent conformational changes in isolated subunits and intact tetramers of human adult and fetal hemoglobin
    • McDonald M.J., Noble R.W. Ligand-dependent conformational changes in isolated subunits and intact tetramers of human adult and fetal hemoglobin. J. Biol. Chem. 1974, 249:3161-3165.
    • (1974) J. Biol. Chem. , vol.249 , pp. 3161-3165
    • McDonald, M.J.1    Noble, R.W.2
  • 10
    • 0344443777 scopus 로고    scopus 로고
    • Active nitric oxide produced in the red cell under hypoxic conditions by deoxy hemoglobin mediated nitrite reduction
    • Nagababu E., Ramasamy S., Abernethy D.R., Rifkind J.M. Active nitric oxide produced in the red cell under hypoxic conditions by deoxy hemoglobin mediated nitrite reduction. J. Biol. Chem. 2003, 278:46349-46356.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46349-46356
    • Nagababu, E.1    Ramasamy, S.2    Abernethy, D.R.3    Rifkind, J.M.4
  • 11
    • 0017112413 scopus 로고
    • Cooperativity in the dissociation of nitric oxide from hemoglobin
    • Moore E.G., Gibson Q.H. Cooperativity in the dissociation of nitric oxide from hemoglobin. J. Biol. Chem. 1976, 251:2788-2794.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2788-2794
    • Moore, E.G.1    Gibson, Q.H.2
  • 12
    • 0016276724 scopus 로고
    • Spectral-kinetic heterogeneity in reactions of nitrosyl hemoglobin
    • Salhany J.M., Ogawa S., Shulman R.G. Spectral-kinetic heterogeneity in reactions of nitrosyl hemoglobin. Proc. Natl. Acad. Sci. U.S.A. 1974, 71:3359-3362.
    • (1974) Proc. Natl. Acad. Sci. U.S.A. , vol.71 , pp. 3359-3362
    • Salhany, J.M.1    Ogawa, S.2    Shulman, R.G.3
  • 14
    • 74849119101 scopus 로고    scopus 로고
    • Reaction of nitrite with human fetal oxyhemoglobin: a model simulation study with implications for blood flow regulation in sickle cell disease (SCD)
    • Salhany J.M. Reaction of nitrite with human fetal oxyhemoglobin: a model simulation study with implications for blood flow regulation in sickle cell disease (SCD). Blood Cells, Molecules and Diseases 2010, 44:111-114.
    • (2010) Blood Cells, Molecules and Diseases , vol.44 , pp. 111-114
    • Salhany, J.M.1
  • 15
    • 0345104387 scopus 로고
    • Oxydation menschlicher und tierischer oxyhamoglobine durch natrium nitrit
    • Betke K., Greinacher I., Tietze O. Oxydation menschlicher und tierischer oxyhamoglobine durch natrium nitrit. Arch. Exp. Path. Pharmakol. 1956, 229:220-226.
    • (1956) Arch. Exp. Path. Pharmakol. , vol.229 , pp. 220-226
    • Betke, K.1    Greinacher, I.2    Tietze, O.3
  • 16
    • 0021796890 scopus 로고
    • Kinetics of amyl nitrite-induced hemoglobin oxidation in cord and adult blood
    • Tarburton J.P., Metclaf W.K. Kinetics of amyl nitrite-induced hemoglobin oxidation in cord and adult blood. Toxicology 1985, 36:15-21.
    • (1985) Toxicology , vol.36 , pp. 15-21
    • Tarburton, J.P.1    Metclaf, W.K.2
  • 17
    • 0242415895 scopus 로고
    • Formation of ferrihaemoglobin of isolated human haemoglobin types by sodium nitrite
    • Martin H., Huisman T.H.J. Formation of ferrihaemoglobin of isolated human haemoglobin types by sodium nitrite. Nature 1963, 200:898-899.
    • (1963) Nature , vol.200 , pp. 898-899
    • Martin, H.1    Huisman, T.H.J.2
  • 19
    • 0015501410 scopus 로고
    • The effect of pH on the rates of ligand replacement reactions of human adult and fetal hemoglobin's and their subunits
    • McDonald M.J., Noble R.W. The effect of pH on the rates of ligand replacement reactions of human adult and fetal hemoglobin's and their subunits. J. Biol. Chem. 1972, 247:4282-4287.
    • (1972) J. Biol. Chem. , vol.247 , pp. 4282-4287
    • McDonald, M.J.1    Noble, R.W.2
  • 20
    • 0015217741 scopus 로고
    • The effect of p-hydroxymercuribenzoate on the reactions of isolated chains of human hemoglobin with ligands
    • Noble R.W. The effect of p-hydroxymercuribenzoate on the reactions of isolated chains of human hemoglobin with ligands. J. Biol. Chem. 1971, 246:2972-2976.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2972-2976
    • Noble, R.W.1
  • 21
    • 0015209636 scopus 로고
    • The deoxygenation kinetic properties of human fetal hemoglobin: effect of 2,3-diphosphoglycerate
    • Salhany J.M., Mizukami H., Eliot R.S. The deoxygenation kinetic properties of human fetal hemoglobin: effect of 2,3-diphosphoglycerate. Biochem. Biophys. Res. Commun. 1971, 45:1350-1356.
    • (1971) Biochem. Biophys. Res. Commun. , vol.45 , pp. 1350-1356
    • Salhany, J.M.1    Mizukami, H.2    Eliot, R.S.3
  • 22
    • 0017145758 scopus 로고
    • Relative stabilities of the two quaternary conformational states of human fetal hemoglobin
    • Wind M., Stern A., Law L., Simon S. Relative stabilities of the two quaternary conformational states of human fetal hemoglobin. Biochemistry 1976, 15:5161-5167.
    • (1976) Biochemistry , vol.15 , pp. 5161-5167
    • Wind, M.1    Stern, A.2    Law, L.3    Simon, S.4
  • 24
    • 44349096391 scopus 로고    scopus 로고
    • The reaction between nitrite and oxyhemoglobin. A mechanistic study
    • Keszler A., Piknova B., Schechter A.N., Hogg N. The reaction between nitrite and oxyhemoglobin. A mechanistic study. J. Biol. Chem. 2008, 283:9615-9622.
    • (2008) J. Biol. Chem. , vol.283 , pp. 9615-9622
    • Keszler, A.1    Piknova, B.2    Schechter, A.N.3    Hogg, N.4
  • 25
    • 61849150615 scopus 로고    scopus 로고
    • The new chemical biology of nitrite reactions with hemoglobin: R-state catalysis, oxidative denitrosylation and nitrite reduction/ anhydrase
    • Gladwin M.T., Grubina R., Doyle M.P. The new chemical biology of nitrite reactions with hemoglobin: R-state catalysis, oxidative denitrosylation and nitrite reduction/ anhydrase. Acc. Chem. Res. 2009, 42:157-167.
    • (2009) Acc. Chem. Res. , vol.42 , pp. 157-167
    • Gladwin, M.T.1    Grubina, R.2    Doyle, M.P.3
  • 26
    • 44449098314 scopus 로고    scopus 로고
    • Kinetics of reaction of nitrite with deoxy hemoglobin after rapid deoxygenation or predeoxygenation by dithionite measured in solution and bound to the cytoplasmic domain of band 3
    • Salhany J.M. Kinetics of reaction of nitrite with deoxy hemoglobin after rapid deoxygenation or predeoxygenation by dithionite measured in solution and bound to the cytoplasmic domain of band 3. Biochemistry 2008, 47:6059-6072.
    • (2008) Biochemistry , vol.47 , pp. 6059-6072
    • Salhany, J.M.1
  • 27
    • 0018716776 scopus 로고
    • Stoichiometry of the reaction of oxyhemoglobin with nitrite
    • Kosaka H., Imaizumi K., Imai K., Tyuma I. Stoichiometry of the reaction of oxyhemoglobin with nitrite. Biochim. Biophys. Acta 1979, 581:184-188.
    • (1979) Biochim. Biophys. Acta , vol.581 , pp. 184-188
    • Kosaka, H.1    Imaizumi, K.2    Imai, K.3    Tyuma, I.4
  • 28
    • 0019807744 scopus 로고
    • Kinetics and mechanism of the oxidation of human deoxy hemoglobin by nitrites
    • Doyle M.P., Pickering R.A., DeWeert T.M., Hoekstra J.W., Pater D. Kinetics and mechanism of the oxidation of human deoxy hemoglobin by nitrites. J. Biol. Chem. 1981, 256:12393-12398.
    • (1981) J. Biol. Chem. , vol.256 , pp. 12393-12398
    • Doyle, M.P.1    Pickering, R.A.2    DeWeert, T.M.3    Hoekstra, J.W.4    Pater, D.5
  • 29
    • 0001457172 scopus 로고
    • The kinetics of dissociation of the first oxygen molecule from fully saturated oxyhemoglobin in sheep blood solution
    • Gibson Q.H., Roughton F.J.W. The kinetics of dissociation of the first oxygen molecule from fully saturated oxyhemoglobin in sheep blood solution. Proc. R. Soc. Lond. B Biol. Sci. 1955, 143:310-334.
    • (1955) Proc. R. Soc. Lond. B Biol. Sci. , vol.143 , pp. 310-334
    • Gibson, Q.H.1    Roughton, F.J.W.2
  • 30
    • 77949845947 scopus 로고    scopus 로고
    • Comparative analysis of nitrite uptake and hemoglobin nitrite reactions in erythrocytes: sorting out uptake mechanisms and oxygenation dependencies
    • Jensen F.B., Rohde S. Comparative analysis of nitrite uptake and hemoglobin nitrite reactions in erythrocytes: sorting out uptake mechanisms and oxygenation dependencies. Am. J. Physiol. Regul. Comp. Physiol. 2010, 298:R297-R982.
    • (2010) Am. J. Physiol. Regul. Comp. Physiol. , vol.298
    • Jensen, F.B.1    Rohde, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.