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Volumn 107, Issue 3, 2009, Pages 325-333

Oximetry with the NMR signals of hemoglobin Val E11 and Tyr C7

Author keywords

Bioenergetics; Muscle; Myoglobin; Oxygen; Oxygen transport

Indexed keywords

BIOLOGICAL MARKER; HEMOGLOBIN; TYROSINE; VALINE;

EID: 70349742374     PISSN: 14396319     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00421-009-1125-3     Document Type: Article
Times cited : (2)

References (45)
  • 3
    • 0018215404 scopus 로고
    • Sequence of oxygen binding by hemoglobin
    • Asakura T, Lau P (1978) Sequence of oxygen binding by hemoglobin. Proc Natl Acad Sci USA 75:5462-5465
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 5462-5465
    • Asakura, T.1    Lau, P.2
  • 4
    • 0014250343 scopus 로고
    • Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin
    • Benesch R, Benesch RE, Yu CI (1967) Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin. Biochemistry 59:526-532
    • (1967) Biochemistry , vol.59 , pp. 526-532
    • Benesch, R.1    Benesch, R.E.2    Yu, C.I.3
  • 6
    • 0037197658 scopus 로고    scopus 로고
    • Effects of amino acid substitutions at beta 131 on the structure and properties of hemoglobin: Evidence for communication between alpha 1 beta 1- and alpha 1 beta 2-subunit interfaces
    • Chang CK, Simplaceanu V, Ho C (2002) Effects of amino acid substitutions at beta 131 on the structure and properties of hemoglobin: Evidence for communication between alpha 1 beta 1- and alpha 1 beta 2-subunit interfaces. Biochemistry 41:5655
    • (2002) Biochemistry , vol.41 , pp. 5655
    • Chang, C.K.1    Simplaceanu, V.2    Ho, C.3
  • 8
    • 0021845968 scopus 로고
    • Proton nuclear overhauser effect investigation of the heme pockets in ligated forms hemoglobin conformational differences between oxy and carbonmonoxy form
    • Dalvitt C, Ho C (1985) Proton nuclear overhauser effect investigation of the heme pockets in ligated forms hemoglobin conformational differences between oxy and carbonmonoxy form. Biochemistry 24:3398-3407
    • (1985) Biochemistry , vol.24 , pp. 3398-3407
    • Dalvitt, C.1    Ho, C.2
  • 10
    • 0028982491 scopus 로고
    • 1H NMR investigation of the oxygenation of hemoglobin in intact human red blood cells
    • 1H NMR investigation of the oxygenation of hemoglobin in intact human red blood cells. Biophys J 68:681-693
    • (1995) Biophys J , vol.68 , pp. 681-693
    • Fetler, B.K.1    Simplaceanu, V.2    Ho, C.3
  • 11
    • 33645978391 scopus 로고    scopus 로고
    • Quaternary structure of carbonmonoxyhemoglobins in solution: Structural changes induced by the allosteric effector inositol hexaphosphate
    • Gong Q, Simplaceanu V, Lukin JA, Giovannelli JL, Ho NT, Ho C (2006) Quaternary structure of carbonmonoxyhemoglobins in solution: Structural changes induced by the allosteric effector inositol hexaphosphate. Biochemistry 45:5140-5148
    • (2006) Biochemistry , vol.45 , pp. 5140-5148
    • Gong, Q.1    Simplaceanu, V.2    Lukin, J.A.3    Giovannelli, J.L.4    Ho, N.T.5    Ho, C.6
  • 12
    • 0019753768 scopus 로고
    • Proton nuclear magnetic resonance investigation of hemoglobins
    • Academic, New York
    • Ho C, Russu I (1981), Proton nuclear magnetic resonance investigation of hemoglobins. Methods in Enzymology, Academic, New York
    • (1981) Methods in Enzymology
    • Ho, C.1    Russu, I.2
  • 13
    • 0242267149 scopus 로고    scopus 로고
    • A modeling investigation to the possible role of myoglobin in human muscle in near infrared spectroscopy (NIRS) measurements
    • Hoofd L, Colier W, Oeseburg B (2009) A modeling investigation to the possible role of myoglobin in human muscle in near infrared spectroscopy (NIRS) measurements. Adv Exp Med Biol 530:637-643
    • (2009) Adv Exp Med Biol , vol.530 , pp. 637-643
    • Hoofd, L.1    Colier, W.2    Oeseburg, B.3
  • 14
    • 0001512518 scopus 로고
    • A new method for water suppression in the proton NMR spectra of aqueous solutions
    • Hore PJ (1983) A new method for water suppression in the proton NMR spectra of aqueous solutions. J Magn Reson 54:539-542
    • (1983) J Magn Reson , vol.54 , pp. 539-542
    • Hore, P.J.1
  • 15
    • 0019738497 scopus 로고
    • Measurement of accurate oxygen equilibrium curves by an automatic oxygenation apparatus
    • Imai K (1981) Measurement of accurate oxygen equilibrium curves by an automatic oxygenation apparatus. Methods Enzymol 76:438-449
    • (1981) Methods Enzymol , vol.76 , pp. 438-449
    • Imai, K.1
  • 16
    • 0017571334 scopus 로고
    • Noninvasive, infrared monitoring of cerebral and myocardial oxygen sufficiency and circulatory parameters
    • Jobsis FF (1977) Noninvasive, infrared monitoring of cerebral and myocardial oxygen sufficiency and circulatory parameters. Science 198:1264-1267
    • (1977) Science , vol.198 , pp. 1264-1267
    • Jobsis, F.F.1
  • 17
    • 0003604662 scopus 로고
    • Measuring tissue oxygenation with the 1 H NMR signals of myoglobin
    • In: Gillies RJ (ed) Academic Press, New York
    • Jue T (1994) Measuring tissue oxygenation with the 1 H NMR signals of myoglobin. In: Gillies RJ (ed) NMR in physiology and biomedicine. Academic Press, New York
    • (1994) NMR in Physiology and Biomedicine
    • Jue, T.1
  • 18
    • 0026266227 scopus 로고
    • 1H nuclear magnetic resonance deoxymyoglobin signal as indicator of intracellular oxygenation in myocardium
    • 1H nuclear magnetic resonance deoxymyoglobin signal as indicator of intracellular oxygenation in myocardium. Am J Physiol 30:H2091-H2097
    • (1991) Am J Physiol , vol.30
    • Kreutzer, U.1    Jue, T.2
  • 19
    • 0026610882 scopus 로고
    • 1H NMR signal of the myoglobin Val-E11 in myocardium: An index of cellular oxygenation
    • 1H NMR signal of the myoglobin Val-E11 in myocardium: An index of cellular oxygenation. Proc Natl Acad Sci USA 89:4731-4733
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4731-4733
    • Kreutzer, U.1    Wang, D.S.2    Jue, T.3
  • 20
    • 0027916672 scopus 로고
    • 1H-NMR characterization of the human myocardium myoglobin and erythrocyte hemoglobin signals
    • 1H-NMR characterization of the human myocardium myoglobin and erythrocyte hemoglobin signals. Biochim Biophys Acta 1161:33-37
    • (1993) Biochim Biophys Acta , vol.1161 , pp. 33-37
    • Kreutzer, U.1    Chung, Y.2    Butler, D.3    Jue, T.4
  • 22
    • 34047230316 scopus 로고    scopus 로고
    • Anisotropy and temperature dependence of myoglobin translational diffusion in myocardium: Implication on oxygen transport and cellular architecture
    • Lin PC, Kreutzer U, Jue T (2007) Anisotropy and temperature dependence of myoglobin translational diffusion in myocardium: Implication on oxygen transport and cellular architecture. Biophys J 92:2608-2620
    • (2007) Biophys J , vol.92 , pp. 2608-2620
    • Lin, P.C.1    Kreutzer, U.2    Jue, T.3
  • 23
    • 0000010874 scopus 로고
    • Magnetic field-dependent water proton spin lattice relaxation rates of hemoglobin solutions and whole blood
    • Lindstrom TR, Koenig SH (1974) Magnetic field-dependent water proton spin lattice relaxation rates of hemoglobin solutions and whole blood. J Magn Reson 15:344-353
    • (1974) J Magn Reson , vol.15 , pp. 344-353
    • Lindstrom, T.R.1    Koenig, S.H.2
  • 24
    • 1842483305 scopus 로고    scopus 로고
    • The structure-function relationship of hemoglobin in solution at atomic resolution
    • Lukin JA, Ho C (2004) The structure-function relationship of hemoglobin in solution at atomic resolution. Chem Rev 104:1219-1230
    • (2004) Chem Rev , vol.104 , pp. 1219-1230
    • Lukin, J.A.1    Ho, C.2
  • 25
    • 0035957144 scopus 로고    scopus 로고
    • A signature of the T → R transition in human hemoglobin
    • Mihailescu MR, Russu IM (2001) A signature of the T → R transition in human hemoglobin. Proc Natl Acad Sci USA 98:3773-3777
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3773-3777
    • Mihailescu, M.R.1    Russu, I.M.2
  • 26
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J, Wyman J, Changeux JP (1965) On the nature of allosteric transitions: A plausible model. J Mol Biol 8:8-118
    • (1965) J Mol Biol , vol.8 , pp. 8-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 27
    • 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 JM, Mazzarella L, Perutz MF (1967) Structure and function of haemoglobin. 3. A three-dimensional Fourier synthesis of human deoxyhaemoglobin at 5.5 Angstrom resolution. J Mol Biol 28:117-156
    • (1967) J Mol Biol , vol.28 , pp. 117-156
    • Muirhead, H.1    Cox, J.M.2    Mazzarella, L.3    Perutz, M.F.4
  • 28
    • 84934441424 scopus 로고    scopus 로고
    • Simulation of Mb/Hb in NIRS and oxygen gradient in the human and canine skeletal muscle using H-NMR and NIRS
    • Nioka S, Wang DJ, Im J, Hamaoka T, Wang ZJ, Leigh JS, Chance B (2009) Simulation of Mb/Hb in NIRS and oxygen gradient in the human and canine skeletal muscle using H-NMR and NIRS. Adv Exp Med Biol 578:223-228
    • (2009) Adv Exp Med Biol , vol.578 , pp. 223-228
    • Nioka, S.1    Wang, D.J.2    Im, J.3    Hamaoka, T.4    Wang, Z.J.5    Leigh, J.S.6    Chance, B.7
  • 29
    • 0034187921 scopus 로고    scopus 로고
    • Characteristics and function of human hemoglobin vesicles as an oxygen carrier
    • Ogata Y (2000) Characteristics and function of human hemoglobin vesicles as an oxygen carrier. Polym Adv Technol 11:205-209
    • (2000) Polym Adv Technol , vol.11 , pp. 205-209
    • Ogata, Y.1
  • 30
    • 0024953088 scopus 로고
    • Mechanisms of cooperativity and allosteric regulation in proteins
    • Perutz MF (1989) Mechanisms of cooperativity and allosteric regulation in proteins. Q Rev Biophys 22:139-236
    • (1989) Q Rev Biophys , vol.22 , pp. 139-236
    • Perutz, M.F.1
  • 31
    • 0014412965 scopus 로고
    • Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A resolution: The atomic model
    • Perutz MF, Muirhead H, Cox JM, Goaman LC (1968) Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A resolution: The atomic model. Nature 219:131-139
    • (1968) Nature , vol.219 , pp. 131-139
    • Perutz, M.F.1    Muirhead, H.2    Cox, J.M.3    Goaman, L.C.4
  • 34
    • 72949146145 scopus 로고
    • Studies on the relations between molecular and functional properties of hemoglobin. II. The effect of salts on the oxygen equilibrium of human hemoglobin
    • Rossi-Fanelli A, Antonini E, Caputo A (1961) Studies on the relations between molecular and functional properties of hemoglobin. II. The effect of salts on the oxygen equilibrium of human hemoglobin. J Biol Chem 236:397-400
    • (1961) J Biol Chem , vol.236 , pp. 397-400
    • Rossi-Fanelli, A.1    Antonini, E.2    Caputo, A.3
  • 35
    • 0023874025 scopus 로고
    • Noninvasive quantitative analysis of blood oxygenation in the rat skeletal muscle
    • Seiyama A, Hazeki O, Tamura M (1988) Noninvasive quantitative analysis of blood oxygenation in the rat skeletal muscle. J Biochem 103:419-424
    • (1988) J Biochem , vol.103 , pp. 419-424
    • Seiyama, A.1    Hazeki, O.2    Tamura, M.3
  • 36
    • 0016753485 scopus 로고
    • Allosteric interpretation of hemoglobin properties
    • Shulman R, Hopfield JJ, Ogawa S (1975) Allosteric interpretation of hemoglobin properties. Q Rev Biophys 8:325-420
    • (1975) Q Rev Biophys , vol.8 , pp. 325-420
    • Shulman, R.1    Hopfield, J.J.2    Ogawa, S.3
  • 38
    • 0342955513 scopus 로고
    • Proton nuclear magnetic resonance investigation of structural changes associated with cooperative oxygenation of human adult hemoglobin
    • Viggiano G, Ho C (1979) Proton nuclear magnetic resonance investigation of structural changes associated with cooperative oxygenation of human adult hemoglobin. Proc Natl Acad Sci USA 76:3673-3677
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 3673-3677
    • Viggiano, G.1    Ho, C.2
  • 39
    • 0018707326 scopus 로고
    • Proton nuclear magnetic resonance and biochemical studies of oxygenation of human hemoglobin in deuterium oxide
    • Viggiano G, Ho NT, Ho C (1979) Proton nuclear magnetic resonance and biochemical studies of oxygenation of human hemoglobin in deuterium oxide. Biochemistry 18:5238-5247
    • (1979) Biochemistry , vol.18 , pp. 5238-5247
    • Viggiano, G.1    Ho, N.T.2    Ho, C.3
  • 40
    • 0021934536 scopus 로고
    • A low cost apparatus for the automatic determination of precise oxygen equilibrium curves on red blood cell suspensions
    • Vorger P, Matelin D (1985) A low cost apparatus for the automatic determination of precise oxygen equilibrium curves on red blood cell suspensions. Comp Biochem Physiol 82:355-359
    • (1985) Comp Biochem Physiol , vol.82 , pp. 355-359
    • Vorger, P.1    Matelin, D.2
  • 41
    • 0030782485 scopus 로고    scopus 로고
    • Myoglobin and hemoglobin rotational diffusion in the cell
    • Wang D, Kreutzer U, Chung Y, Jue T (1997) Myoglobin and hemoglobin rotational diffusion in the cell. Biophys J 73:2764-2770
    • (1997) Biophys J , vol.73 , pp. 2764-2770
    • Wang, D.1    Kreutzer, U.2    Chung, Y.3    Jue, T.4
  • 42
    • 34548671665 scopus 로고    scopus 로고
    • High-altitude adaptations in vertebrate hemoglobins
    • Weber RE (2007) High-altitude adaptations in vertebrate hemoglobins. Respir Physiol Neurobiol 158:132-142
    • (2007) Respir Physiol Neurobiol , vol.158 , pp. 132-142
    • Weber, R.E.1
  • 43
    • 70349753910 scopus 로고
    • Cooperativity and electronic properties
    • Weissbluth M (1974) Cooperativity and electronic properties. Mol Biol Biochem Biophys 15:1-175
    • (1974) Mol Biol Biochem Biophys , vol.15 , pp. 1-175
    • Weissbluth, M.1
  • 44
    • 0024821213 scopus 로고
    • Noninvasive detection of skeletal muscle underperfusion with near-infrared spectroscopy in patients with heart failure
    • Wilson JR, Mancini DM, McCully K, Feraro N, Lanoce V, Chance B (1989) Noninvasive detection of skeletal muscle underperfusion with near-infrared spectroscopy in patients with heart failure. Circulation 80:1668-1674
    • (1989) Circulation , vol.80 , pp. 1668-1674
    • Wilson, J.R.1    Mancini, D.M.2    McCully, K.3    Feraro, N.4    Lanoce, V.5    Chance, B.6
  • 45
    • 0037072945 scopus 로고    scopus 로고
    • Global allostery model of hemoglobin. Modulation of O(2) affinity, cooperativity, and Bohr effect by heterotrophic allosteric effectors
    • Yonetani T, Park SI, Tsuneshige A, Imai K, Kanaori K (2002) Global allostery model of hemoglobin. Modulation of O(2) affinity, cooperativity, and Bohr effect by heterotrophic 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.