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Volumn 46, Issue 41, 2007, Pages 11650-11659

Intermediates detected by visible spectroscopy during the reaction of nitrite with deoxyhemoglobin: The effect of nitrite concentration and diphosphoglycerate

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN; PHOSPHATES; RATE CONSTANTS; SPECTROSCOPIC ANALYSIS;

EID: 35348877494     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700364e     Document Type: Article
Times cited : (33)

References (51)
  • 1
    • 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. (1996) S-Nitrosohaemoglobin: a dynamic activity of blood involved in vascular control, Nature 380, 221-226.
    • (1996) Nature , vol.380 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 2
    • 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. (2003) Active nitric oxide produced in the red cell under hypoxic conditions by deoxyhemoglobin-mediated nitrite reduction, J. Biol. Chem. 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
  • 6
    • 0019807744 scopus 로고    scopus 로고
    • Doyle, M. P., Pickering, R. A., DeWeert, T. M., Hoekst.ra, J. W., and Pater, D. (1981) Kinetics and mechanism of the oxidation of human deoxyhemoglobin by nitrites, J. Biol. Chem. 256, 12393-12398.
    • Doyle, M. P., Pickering, R. A., DeWeert, T. M., Hoekst.ra, J. W., and Pater, D. (1981) Kinetics and mechanism of the oxidation of human deoxyhemoglobin by nitrites, J. Biol. Chem. 256, 12393-12398.
  • 7
    • 0028540281 scopus 로고
    • The nitric oxide cycle in mammals and nitrite reducing activity of heme-containing proteins]
    • Reutov, V. P., Sorokina, E. G., and Kaiushin, L. P. (1994) [The nitric oxide cycle in mammals and nitrite reducing activity of heme-containing proteins], Vopr. Med. Khim. 40, 31-35.
    • (1994) Vopr. Med. Khim , vol.40 , pp. 31-35
    • Reutov, V.P.1    Sorokina, E.G.2    Kaiushin, L.P.3
  • 8
    • 0036519252 scopus 로고    scopus 로고
    • Nitric oxide cycle in mammals and the cyclicity principle
    • Reutov, V. P. (2002) Nitric oxide cycle in mammals and the cyclicity principle, Biochemistry (Moscow) 67, 293-311.
    • (2002) Biochemistry (Moscow) , vol.67 , pp. 293-311
    • Reutov, V.P.1
  • 10
    • 0030004767 scopus 로고
    • Direct Observation by FTIR Spectroscopy of the Ferrous Heme-NO+ Intermediate in Reduction of Nitrite by a Dissimilatory Heme cd1 Nitrite Reductas
    • Wang, Y., and Averill, B. A. (1960) Direct Observation by FTIR Spectroscopy of the Ferrous Heme-NO+ Intermediate in Reduction of Nitrite by a Dissimilatory Heme cd1 Nitrite Reductas, J. Am. Chem. Soc 118, 3972-3973.
    • (1960) J. Am. Chem. Soc , vol.118 , pp. 3972-3973
    • Wang, Y.1    Averill, B.A.2
  • 12
    • 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. (2005) The reaction between nitrite and hemoglobin: the role of nitrite in hemoglobin-mediated hypoxic vasodilation, J. Inorg. Biochem. 99, 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
  • 13
    • 23644459872 scopus 로고    scopus 로고
    • The reaction between nitrite and deoxyhemoglobin. Reassessment of reaction kinetics and stoichiometry
    • Huang, K. T., Keszler, A., Patel, N., Patel, R. P., Gladwin, M. T., Kim-Shapiro, D. B., and Hogg, N. (2005) The reaction between nitrite and deoxyhemoglobin. Reassessment of reaction kinetics and stoichiometry, J. Biol. Chem. 280, 31126-31131.
    • (2005) J. Biol. Chem , vol.280 , pp. 31126-31131
    • Huang, K.T.1    Keszler, A.2    Patel, N.3    Patel, R.P.4    Gladwin, M.T.5    Kim-Shapiro, D.B.6    Hogg, N.7
  • 14
    • 16244401683 scopus 로고    scopus 로고
    • Assessments of the chemistry and vasodilatory activity of nitrite with hemoglobin under physiologically relevant conditions
    • Luchsinger, B. P., Rich, E. N., Yan, Y., Williams, E. M., Stamler, J. S., and Singel, D. J. (2005) Assessments of the chemistry and vasodilatory activity of nitrite with hemoglobin under physiologically relevant conditions, J. Inorg. Biochem. 99, 912-921.
    • (2005) J. Inorg. Biochem , vol.99 , pp. 912-921
    • Luchsinger, B.P.1    Rich, E.N.2    Yan, Y.3    Williams, E.M.4    Stamler, J.S.5    Singel, D.J.6
  • 15
    • 33744832041 scopus 로고    scopus 로고
    • An S-nitrosothiol (SNO) synthase function of hemoglobin that utilizes nitrite as a substrate
    • Angelo, M., Singel, D. J., and Stamler, J. S. (2006) An S-nitrosothiol (SNO) synthase function of hemoglobin that utilizes nitrite as a substrate, Proc. Natl. Acad. Sci. U.S.A. 103, 8366-8371.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 8366-8371
    • Angelo, M.1    Singel, D.J.2    Stamler, J.S.3
  • 17
    • 0030338271 scopus 로고    scopus 로고
    • Simultaneous measurement of total hemoglobin and its derivatives in blood using CO-oximeters: Analytical principles; their application in selecting analytical wavelengths and reference methods; a comparison of the results of the choices made
    • Brunelle, J. A., Degtiarov, A. M., Moran, R. F., and Race, L. A. (1996) Simultaneous measurement of total hemoglobin and its derivatives in blood using CO-oximeters: analytical principles; their application in selecting analytical wavelengths and reference methods; a comparison of the results of the choices made, Scand. J. Clin. Lab. Invest. Suppl. 224, 47-69.
    • (1996) Scand. J. Clin. Lab. Invest. Suppl , vol.224 , pp. 47-69
    • Brunelle, J.A.1    Degtiarov, A.M.2    Moran, R.F.3    Race, L.A.4
  • 18
    • 0025088854 scopus 로고
    • Multiple heme pocket subconformations of methemoglobin associated with distal histidine interactions
    • Levy, A., Kuppusamy, P., and Rifkind, J. M. (1990) Multiple heme pocket subconformations of methemoglobin associated with distal histidine interactions, Biochemistry 29, 9311-9316.
    • (1990) Biochemistry , vol.29 , pp. 9311-9316
    • Levy, A.1    Kuppusamy, P.2    Rifkind, J.M.3
  • 19
    • 0022523277 scopus 로고
    • Nitrosyliron(III) hemoglobin: Autoreduction and spectroscopy
    • Addison, A. W., and Stephanos, J. J. (1986) Nitrosyliron(III) hemoglobin: autoreduction and spectroscopy, Biochemistry 25, 4104-4113.
    • (1986) Biochemistry , vol.25 , pp. 4104-4113
    • Addison, A.W.1    Stephanos, J.J.2
  • 20
    • 33745497365 scopus 로고    scopus 로고
    • S-nitrosohemoglobin: A mechanism for its formation in conjunction with nitrite reduction by deoxyhemoglobin
    • Nagababu, E., Ramasamy, S., and Rifkind, J. M. (2006) S-nitrosohemoglobin: a mechanism for its formation in conjunction with nitrite reduction by deoxyhemoglobin, Nitric Oxide 15, 20-29.
    • (2006) Nitric Oxide , vol.15 , pp. 20-29
    • Nagababu, E.1    Ramasamy, S.2    Rifkind, J.M.3
  • 21
    • 35348844597 scopus 로고    scopus 로고
    • Rifkind, J. M. (2005) S-Nitrosohemoglobin formation: a mechanism involving electron derealization in the heme pocket, Biophys. J. 88, 391A-part 392 suppl.
    • Rifkind, J. M. (2005) S-Nitrosohemoglobin formation: a mechanism involving electron derealization in the heme pocket, Biophys. J. 88, 391A-part 392 suppl.
  • 22
    • 0042856838 scopus 로고    scopus 로고
    • Nitrite catalyzes ferriheme protein reductive nitrosylation
    • Fernandez, B. O., and Ford, P. C. (2003) Nitrite catalyzes ferriheme protein reductive nitrosylation, J. Am. Chem. Soc. 125, 10510-10511.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 10510-10511
    • Fernandez, B.O.1    Ford, P.C.2
  • 26
    • 85117737835 scopus 로고    scopus 로고
    • McMahon, T. J., Pawloski, J. R., Hess, D. T., Piantadosi, C. A., Luchsinger, B. P., Singel, D. J., and Stamler, J. S. (2003) S-nitrosohemoglobin is distinguished from other nitrosovasodilators by unique oxygen-dependent responses that support an allosteric mechanism of action, Blood 102, 410-411; author reply 412-413.
    • McMahon, T. J., Pawloski, J. R., Hess, D. T., Piantadosi, C. A., Luchsinger, B. P., Singel, D. J., and Stamler, J. S. (2003) S-nitrosohemoglobin is distinguished from other nitrosovasodilators by unique oxygen-dependent responses that support an allosteric mechanism of action, Blood 102, 410-411; author reply 412-413.
  • 27
    • 0036886264 scopus 로고    scopus 로고
    • Nitric oxide in RBCs
    • Pawloski, J. R., and Stamler, J. S. (2002) Nitric oxide in RBCs, Transfusion 42, 1603-1609.
    • (2002) Transfusion , vol.42 , pp. 1603-1609
    • Pawloski, J.R.1    Stamler, J.S.2
  • 28
    • 11244316895 scopus 로고    scopus 로고
    • Chemical physiology of blood flow regulation by red blood cells: The role of nitric oxide and S-nitrosohemoglobin
    • Singel, D. J., and Stamler, J. S. (2005) Chemical physiology of blood flow regulation by red blood cells: the role of nitric oxide and S-nitrosohemoglobin, Annu. Rev. Physiol. 67, 99-145.
    • (2005) Annu. Rev. Physiol , vol.67 , pp. 99-145
    • Singel, D.J.1    Stamler, J.S.2
  • 30
    • 0032495529 scopus 로고    scopus 로고
    • Reactions between nitric oxide and haemoglobin under physiological conditions
    • Gow, A. J., and Stamler, J. S. (1998) Reactions between nitric oxide and haemoglobin under physiological conditions, Nature 391, 169-173.
    • (1998) Nature , vol.391 , pp. 169-173
    • Gow, A.J.1    Stamler, J.S.2
  • 32
    • 0031281450 scopus 로고    scopus 로고
    • Contribution of Electron Paramagnetic Resonance to the studies of hemoglobin: The nitrosylhemoglobin system
    • Bemski, G. (1997) Contribution of Electron Paramagnetic Resonance to the studies of hemoglobin: the nitrosylhemoglobin system, Mol. Biol. Rep. 24, 263-269.
    • (1997) Mol. Biol. Rep , vol.24 , pp. 263-269
    • Bemski, G.1
  • 33
    • 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. (1987) Reaction of nitric oxide with heme proteins and model compounds of hemoglobin, Biochemistry 26, 3837-3843.
    • (1987) Biochemistry , vol.26 , pp. 3837-3843
    • Sharma, V.S.1    Traylor, T.G.2    Gardiner, R.3    Mizukami, H.4
  • 34
    • 0015515865 scopus 로고
    • X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin
    • Arnone, A. (1972) X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin, Nature 237, 146-149.
    • (1972) Nature , vol.237 , pp. 146-149
    • Arnone, A.1
  • 35
    • 0005665362 scopus 로고
    • The three-state model: A minimal allosteric description of homotropic and heterotropic effects in the binding of ligands to hemoglobin
    • Minton, A. P., and Imai, K. (1974) The three-state model: a minimal allosteric description of homotropic and heterotropic effects in the binding of ligands to hemoglobin, Proc. Natl. Acad. Sci. U.S.A. 71, 1418-1421.
    • (1974) Proc. Natl. Acad. Sci. U.S.A , vol.71 , pp. 1418-1421
    • Minton, A.P.1    Imai, K.2
  • 36
    • 0037072945 scopus 로고    scopus 로고
    • Global allostery model of hemoglobin. Modulation of O(2) affinity, cooperativity, and Bohr effect by heterotropic allosteric effectors
    • Yonetani, T., Park, S. I., Tsuneshige, A., Imai, K., and Kanaori, K. (2002) Global allostery model of hemoglobin. Modulation of O(2) affinity, cooperativity, and Bohr effect by heterotropic allosteric effectors, J. Biol. Chem. 277, 34508-34520.
    • (2002) J. Biol. Chem , vol.277 , pp. 34508-34520
    • Yonetani, T.1    Park, S.I.2    Tsuneshige, A.3    Imai, K.4    Kanaori, K.5
  • 37
    • 10344255690 scopus 로고    scopus 로고
    • Semihemoglobins, high oxygen affinity dimeric forms of human hemoglobin respond efficiently to allosteric effectors without forming tetramers
    • Tsuneshige, A., Kanaori, K., Samuni, U., Danstker, D., Friedman, J. M., Neya, S., Giangiacomo, L., and Yonetani, T. (2004) Semihemoglobins, high oxygen affinity dimeric forms of human hemoglobin respond efficiently to allosteric effectors without forming tetramers, J. Biol. Chem. 279, 48959-48967.
    • (2004) J. Biol. Chem , vol.279 , pp. 48959-48967
    • Tsuneshige, A.1    Kanaori, K.2    Samuni, U.3    Danstker, D.4    Friedman, J.M.5    Neya, S.6    Giangiacomo, L.7    Yonetani, T.8
  • 38
    • 10644243494 scopus 로고    scopus 로고
    • Cross-linking with O-raffinose lowers oxygen affinity and stabilizes haemoglobin in a non-cooperative T-state conformation
    • Jia, Y., Ramasamy, S., Wood, F., Alayash, A. I., and Rifkind, J. M. (2004) Cross-linking with O-raffinose lowers oxygen affinity and stabilizes haemoglobin in a non-cooperative T-state conformation, Biochem. J. 384, 367-375.
    • (2004) Biochem. J , vol.384 , pp. 367-375
    • Jia, Y.1    Ramasamy, S.2    Wood, F.3    Alayash, A.I.4    Rifkind, J.M.5
  • 39
    • 0033061632 scopus 로고    scopus 로고
    • Molecular dynamics of human methemoglobin: The transmission of conformational information between subunits in an alpha beta dimer
    • Ramadas, N., and Rifkind, J. M. (1999) Molecular dynamics of human methemoglobin: the transmission of conformational information between subunits in an alpha beta dimer, Biophys. J. 76, 1796-1811.
    • (1999) Biophys. J , vol.76 , pp. 1796-1811
    • Ramadas, N.1    Rifkind, J.M.2
  • 40
    • 0022389401 scopus 로고
    • Low-temperature formation of a distal histidine complex in hemoglobin: A probe for heme pocket flexibility
    • Levy, A., and Rifkind, J. M. (1985) Low-temperature formation of a distal histidine complex in hemoglobin: a probe for heme pocket flexibility, Biochemistry 24, 6050-6054.
    • (1985) Biochemistry , vol.24 , pp. 6050-6054
    • Levy, A.1    Rifkind, J.M.2
  • 41
    • 0026552930 scopus 로고
    • A new mode for heme-heme interactions in hemoglobin associated with distal perturbations
    • Levy, A., Sharma, V. S., Zhang, L., and Rifkind, J. M. (1992) A new mode for heme-heme interactions in hemoglobin associated with distal perturbations, Biophys. J. 61, 750-755.
    • (1992) Biophys. J , vol.61 , pp. 750-755
    • Levy, A.1    Sharma, V.S.2    Zhang, L.3    Rifkind, J.M.4
  • 42
    • 0021027685 scopus 로고
    • Structure of human oxyhaemoglobin at 2.1 Å resolution
    • Shaanan, B. (1983) Structure of human oxyhaemoglobin at 2.1 Å resolution, J. Mol. Biol. 171, 31-59.
    • (1983) J. Mol. Biol , vol.171 , pp. 31-59
    • Shaanan, B.1
  • 43
    • 0034641754 scopus 로고    scopus 로고
    • NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin
    • Lukin, J. A., Simplaceanu, V., Zou, M., Ho, N. T., and Ho, C. (2000) NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin, Proc. Natl. Acad. Sci. U.S.A. 97, 10354-10358.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 10354-10358
    • Lukin, J.A.1    Simplaceanu, V.2    Zou, M.3    Ho, N.T.4    Ho, C.5
  • 44
    • 0019446263 scopus 로고
    • Resonance Raman and absorption spectroscopic detection of distal histidine - fluoride interactions in human methemoglobin fluoride and sperm whale metmyoglobin fluoride: Measurements of distal histidine ionization constants
    • Asher, S. A., Adams, M. L., and Schuster, T. M. (1981) Resonance Raman and absorption spectroscopic detection of distal histidine - fluoride interactions in human methemoglobin fluoride and sperm whale metmyoglobin fluoride: measurements of distal histidine ionization constants, Biochemistry 20, 3339-3346.
    • (1981) Biochemistry , vol.20 , pp. 3339-3346
    • Asher, S.A.1    Adams, M.L.2    Schuster, T.M.3
  • 45
    • 0034641673 scopus 로고    scopus 로고
    • Quantum mechanical interpretation of nitrite reduction by cytochrome cd1 nitrite reductase from Paracoccus pantotrophus
    • Ranghino, G., Scorza, E., Sjogren, T., Williams, P. A., Ricci, M., and Hajdu, J. (2000) Quantum mechanical interpretation of nitrite reduction by cytochrome cd1 nitrite reductase from Paracoccus pantotrophus, Biochemistry 39, 10958-10966.
    • (2000) Biochemistry , vol.39 , pp. 10958-10966
    • Ranghino, G.1    Scorza, E.2    Sjogren, T.3    Williams, P.A.4    Ricci, M.5    Hajdu, J.6
  • 46
    • 0029930628 scopus 로고    scopus 로고
    • Production of superoxide from hemoglobin-bound oxygen under hypoxic conditions
    • Balagopalakrishna, C., Manoharan, P. T., Abugo, O. O., and Rifkind, J. M. (1996) Production of superoxide from hemoglobin-bound oxygen under hypoxic conditions, Biochemistry 35, 6393-6398.
    • (1996) Biochemistry , vol.35 , pp. 6393-6398
    • Balagopalakrishna, C.1    Manoharan, P.T.2    Abugo, O.O.3    Rifkind, J.M.4
  • 47
    • 0028061399 scopus 로고
    • Oxidation of hemoglobin and the enhancement produced by nitroblue tetrazolium
    • Abugo, O. O., and Rifkind, J. M. (1994) Oxidation of hemoglobin and the enhancement produced by nitroblue tetrazolium, J. Biol. Chem. 269, 24845-24853.
    • (1994) J. Biol. Chem , vol.269 , pp. 24845-24853
    • Abugo, O.O.1    Rifkind, J.M.2
  • 48
    • 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, J. R., Jr. (2005) Hemoglobin-mediated, hypoxia-induced vasodilation via nitric oxide: mechanism(s) and physiologic versus pathophysiologic relevance, Am. J. Respir. Cell Mol. Biol. 32, 257-261.
    • (2005) Am. J. Respir. Cell Mol. Biol , vol.32 , pp. 257-261
    • Robinson, J.M.1    Lancaster Jr., J.R.2
  • 49
    • 67649823967 scopus 로고    scopus 로고
    • Conformationally regulated uptake of nitrite by deoxyhemoglobin and release of the NO produced
    • Rifkind, J. M., Ramasamy, S., and Nagababu, E. (2007) Conformationally regulated uptake of nitrite by deoxyhemoglobin and release of the NO produced, Biophys. J. 383a-384a.
    • (2007) Biophys. J
    • Rifkind, J.M.1    Ramasamy, S.2    Nagababu, E.3
  • 50
    • 0023099564 scopus 로고
    • The binding of hemoglobin to red cell membrane lowers its oxygen affinity
    • Tsuneshige, A., Imai, K., and Tyuma, I. (1987) The binding of hemoglobin to red cell membrane lowers its oxygen affinity, J. Biochem. (Tokyo) 101, 695-704.
    • (1987) J. Biochem. (Tokyo) , vol.101 , pp. 695-704
    • Tsuneshige, A.1    Imai, K.2    Tyuma, I.3
  • 51
    • 0024261386 scopus 로고
    • The role of hemoglobin in generating oxyradicals
    • Rifkind, J. M., Zhang, L., Heim, J. M., and Levy, A. (1988) The role of hemoglobin in generating oxyradicals, Basic Life Sci. 49, 157-162.
    • (1988) Basic Life Sci , vol.49 , pp. 157-162
    • Rifkind, J.M.1    Zhang, L.2    Heim, J.M.3    Levy, A.4


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