메뉴 건너뛰기




Volumn 50, Issue 39, 2011, Pages 8323-8332

Crystallographic trapping of heme loss intermediates during the nitrite-induced degradation of human hemoglobin

Author keywords

[No Author keywords available]

Indexed keywords

COFACTORS; EXOGENOUS LIGANDS; LARGE PARTS; REGIOSPECIFIC; SMALL-MOLECULE BINDINGS; STRUCTURAL INSIGHTS;

EID: 80053390286     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2009322     Document Type: Article
Times cited : (26)

References (59)
  • 1
    • 53149126899 scopus 로고    scopus 로고
    • Protein Dynamics Explain the Allosteric Behaviors of Hemoglobin
    • Yonetani, T. and Laberge, M. (2008) Protein Dynamics Explain the Allosteric Behaviors of Hemoglobin Biochim. Biophys. Acta 1784, 1146-1158
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1146-1158
    • Yonetani, T.1    Laberge, M.2
  • 2
    • 16244376841 scopus 로고    scopus 로고
    • Ligand specificity of H-NOX domains: From sGC to bacterial NO sensors
    • DOI 10.1016/j.jinorgbio.2004.12.016, Heme-Diatomic Interactions, Part 2
    • Boon, E. M. and Marletta, M. A. (2005) Ligand Specificity of H-NOX Domains: From sGC to Bacterial NO Sensors J. Inorg. Biochem. 99, 892-902 (Pubitemid 40461919)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.4 , pp. 892-902
    • Boon, E.M.1    Marletta, M.A.2
  • 5
    • 0029737668 scopus 로고    scopus 로고
    • Structural factors governing hemin dissociation from metmyoglobin
    • DOI 10.1021/bi960372d
    • Hargrove, M. S., Wilkinson, A. J., and Olson, J. S. (1996) Structural Factors Governing Hemin Dissociation from Metmyoglobin Biochemistry 35, 11300-11309 (Pubitemid 26299303)
    • (1996) Biochemistry , vol.35 , Issue.35 , pp. 11300-11309
    • Hargrove, M.S.1    Wilkinson, A.J.2    Olson, J.S.3
  • 6
    • 0014408353 scopus 로고
    • Exchange of Heme among Hemoglobins and between Hemoglobin and Albumin
    • Bunn, H. F. and Jandl, J. H. (1968) Exchange of Heme Among Hemoglobins and Between Hemoglobin and Albumin J. Biol. Chem. 243, 465-475
    • (1968) J. Biol. Chem. , vol.243 , pp. 465-475
    • Bunn, H.F.1    Jandl, J.H.2
  • 7
    • 77954828486 scopus 로고    scopus 로고
    • Role of Heme in the Unfolding and Assembly of Myoglobin
    • Culbertson, D. S. and Olson, J. S. (2010) Role of Heme in the Unfolding and Assembly of Myoglobin Biochemistry 49, 6052-6063
    • (2010) Biochemistry , vol.49 , pp. 6052-6063
    • Culbertson, D.S.1    Olson, J.S.2
  • 9
    • 0001023291 scopus 로고    scopus 로고
    • The molecular mechanism of autoxidation for myoglobin and hemoglobin: A venerable puzzle
    • Shikama, K. (1998) The Molecular Mechanism of Autoxidation for Myoglobin and Hemoglobin: A Venerable Puzzle Chem. Rev. 98, 1357-1373 (Pubitemid 128635957)
    • (1998) Chemical Reviews , vol.98 , Issue.4 , pp. 1357-1373
    • Shikama, K.1
  • 10
    • 0034143648 scopus 로고    scopus 로고
    • Decomposition of nitrite under various pH and aeration conditions
    • Braida, W. and Ong, S. K. (2000) Decomposition of Nitrite Under Various pH and Aeration Conditions Water, Air, Soil Pollut. 118, 13-26 (Pubitemid 30104054)
    • (2000) Water, Air, and Soil Pollution , vol.118 , Issue.1-2 , pp. 13-26
    • Braida, W.1    Ong, S.K.2
  • 11
    • 0019807744 scopus 로고
    • Kinetics and mechanism of the oxidation of human deoxyhemoglobin by nitrites
    • Doyle, M. P., Pickering, R. A., DeWeert, T. M., Hoekstra, J. W., and Pater, D. (1981) Kinetics and Mechanism of the Oxidation of Human Deoxyhemoglobin by Nitrites J. Biol. Chem. 256, 12393-12398 (Pubitemid 12141507)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.23 , pp. 12393-12398
    • Doyle, M.P.1    Pickering, R.A.2    DeWeert, T.M.3
  • 12
  • 13
    • 25444529461 scopus 로고    scopus 로고
    • Proposed mechanism of nitrite-induced methemoglobinemia
    • DOI 10.1007/s10541-005-0139-7
    • Titov, V. Y. and Petrenko, Y. M. (2005) Proposed Mechanism of Nitrite-Induced Methemoglobinemia Biochemistry (Moscow, Russ. Fed.) 70, 473-483 (Pubitemid 40878794)
    • (2005) Biochemistry (Moscow) , vol.70 , Issue.4 , pp. 473-483
    • Titov, V.Yu.1    Petrenko, Yu.M.2
  • 16
    • 80053420281 scopus 로고
    • Nitrite Methaemoglobin and Related Pigments
    • Hartridge, H. (1920) Nitrite Methaemoglobin and Related Pigments J. Physiol. 54, 253-259
    • (1920) J. Physiol. , vol.54 , pp. 253-259
    • Hartridge, H.1
  • 17
    • 0014670534 scopus 로고
    • The Reaction of Methemoglobin with Some Ligands
    • Gibson, Q. H., Parkhurst, L. J., and Gerachi, G. (1969) The Reaction of Methemoglobin with Some Ligands J. Biol. Chem. 244, 4668-4676
    • (1969) J. Biol. Chem. , vol.244 , pp. 4668-4676
    • Gibson, Q.H.1    Parkhurst, L.J.2    Gerachi, G.3
  • 18
    • 49449116592 scopus 로고    scopus 로고
    • The Nitrite Anion Binds to Human Hemoglobin via the Uncommon O -Nitrito Mode
    • Yi, J., Safo, M. K., and Richter-Addo, G. B. (2008) The Nitrite Anion Binds to Human Hemoglobin via the Uncommon O -Nitrito Mode Biochemistry 47, 8247-8249
    • (2008) Biochemistry , vol.47 , pp. 8247-8249
    • Yi, J.1    Safo, M.K.2    Richter-Addo, G.B.3
  • 19
    • 0001006465 scopus 로고
    • Formation of Bovine Nitrosylmyoglobin. I. pH 4.5-6.5
    • Fox, J. B. and Thomson, J. S. (1963) Formation of Bovine Nitrosylmyoglobin. I. pH 4.5-6.5 Biochemistry 2, 465-470
    • (1963) Biochemistry , vol.2 , pp. 465-470
    • Fox, J.B.1    Thomson, J.S.2
  • 20
    • 33947487901 scopus 로고
    • The Formation of Green Heme Pigments from Metmyoglobin and Methemoglobin by the Action of Nitrite
    • Fox, J. B. and Thomson, J. S. (1964) The Formation of Green Heme Pigments from Metmyoglobin and Methemoglobin by the Action of Nitrite Biochemistry 3, 1323-1328
    • (1964) Biochemistry , vol.3 , pp. 1323-1328
    • Fox, J.B.1    Thomson, J.S.2
  • 21
    • 78649264106 scopus 로고    scopus 로고
    • Covelent Modifications of Hemoglobin by Nitrite Anions: Formation Kinetics and Properties of Nitrihemoglobin
    • Otsuka, M., Marks, S. A., Winnica, D. A., Amoscato, A. A., Pearce, L. L., and Peterson, J. (2010) Covelent Modifications of Hemoglobin by Nitrite Anions: Formation Kinetics and Properties of Nitrihemoglobin Chem. Res. Toxicol. 23, 1786-1795
    • (2010) Chem. Res. Toxicol. , vol.23 , pp. 1786-1795
    • Otsuka, M.1    Marks, S.A.2    Winnica, D.A.3    Amoscato, A.A.4    Pearce, L.L.5    Peterson, J.6
  • 22
    • 0024573682 scopus 로고
    • Structural characterization of nitrimyoglobin
    • Bondoc, L. L. and Timkovich, R. (1989) Structural Characterization of Nitrimyoglobin J. Biol. Chem. 264, 6134-6145 (Pubitemid 19106682)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.11 , pp. 6134-6145
    • Bondoc, L.L.1    Timkovich, R.2
  • 25
    • 0028364885 scopus 로고
    • Detection, formation, and relevance of hemichromes and hemochromes
    • DOI 10.1016/0076-6879(94)31030-0
    • Rifkind, J. M., Abugo, O., Levy, A., and Heim, J. (1994) Detection, Formation, and Relevance of Hemichromes and Hemochromes Methods Enzymol. 231, 449-480 (Pubitemid 24169858)
    • (1994) Methods in Enzymology , vol.231 , pp. 449-480
    • Rifkind, J.M.1    Abugo, O.2    Levy, A.3    Heim, J.4
  • 26
    • 0000758608 scopus 로고
    • Low-Spin Compounds of Heme Proteins
    • Blumberg, W. E. and Peisach, J. (1971) Low-Spin Compounds of Heme Proteins Adv. Chem. Ser. 100, 271-291
    • (1971) Adv. Chem. Ser. , vol.100 , pp. 271-291
    • Blumberg, W.E.1    Peisach, J.2
  • 27
    • 0042324524 scopus 로고    scopus 로고
    • A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin
    • DOI 10.1021/bi030059t
    • Robinson, V. L., Smith, B. B., and Arnone, A. (2003) A pH-Dependent Aquomet-to-Hemichrome Transition in Crystalline Horse Methemoglobin Biochemistry 42, 10113-10125 (Pubitemid 37052031)
    • (2003) Biochemistry , vol.42 , Issue.34 , pp. 10113-10125
    • Robinson, V.L.1    Smith, B.B.2    Arnone, A.3
  • 28
    • 61849150615 scopus 로고    scopus 로고
    • The New Chemical Biology of Nitrite Reactions with Hemoglobin: R -State Catalysis, Oxidative Denitrosylation, and Nitrite Reductase/Anhydrase
    • Gladwin, M. T., Grubina, R., and Doyle, M. P. (2009) The New Chemical Biology of Nitrite Reactions with Hemoglobin: R -State Catalysis, Oxidative Denitrosylation, and Nitrite Reductase/Anhydrase Acc. Chem. Res. 42, 157-167
    • (2009) Acc. Chem. Res. , vol.42 , pp. 157-167
    • Gladwin, M.T.1    Grubina, R.2    Doyle, M.P.3
  • 29
    • 33846027866 scopus 로고    scopus 로고
    • Nitrite reductase activity of sol-gel-encapsulated deoxyhemoglobin: Influence of quaternary and tertiary structure
    • DOI 10.1074/jbc.M603914200
    • Roche, C. J., Dantsker, D., Samuni, U., and Friedman, J. M. (2006) Nitrite Reductase Activity of Sol-Gel-encapsulated Deoxyhemoglobin: Influence of Quatenary and Tertiary Structure J. Biol. Chem. 281, 36874-36882 (Pubitemid 46042155)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.48 , pp. 36874-36882
    • Roche, C.J.1    Dantsker, D.2    Samuni, U.3    Friedman, J.M.4
  • 30
    • 35348877494 scopus 로고    scopus 로고
    • Intermediates detected by visible spectroscopy during the reaction of nitrite with deoxyhemoglobin: The effect of nitrite concentration and diphosphoglycerate
    • DOI 10.1021/bi700364e
    • Nagababu, E., Ramasamy, S., and Rifkind, J. M. (2007) Intermediates Detected by Visible Spectroscopy During the Reaction of Nitrite with Deoxyhemoglobin: The Effect of Nitrite Concentration and Diphosphoglycerate Biochemistry 46, 11650-11659 (Pubitemid 47585511)
    • (2007) Biochemistry , vol.46 , Issue.41 , pp. 11650-11659
    • Nagababu, E.1    Ramasamy, S.2    Rifkind, J.M.3
  • 31
    • 0036266780 scopus 로고    scopus 로고
    • Pharmacokinetics of sodium nitrite-induced methemoglobinemia in the rat
    • DOI 10.1124/dmd.30.6.676
    • Kohn, M. C., Melnick, R. L., Ye, F., and Portier, C. J. (2002) Pharmacokinetics of Sodium Nitrite-Induced Methemoglobinemia in the Rat Drug Metab. Dispos. 30, 676-683 (Pubitemid 34579102)
    • (2002) Drug Metabolism and Disposition , vol.30 , Issue.6 , pp. 676-683
    • Kohn, M.C.1    Melnick, R.L.2    Ye, F.3    Portier, C.J.4
  • 33
    • 0142228328 scopus 로고    scopus 로고
    • X-ray Crystallography of Hemoglobins
    • Safo, M. K. and Abraham, D. J. (2003) X-ray Crystallography of Hemoglobins Methods Mol. Med. 82, 1-19
    • (2003) Methods Mol. Med. , vol.82 , pp. 1-19
    • Safo, M.K.1    Abraham, D.J.2
  • 35
    • 79958099097 scopus 로고    scopus 로고
    • Crystal Structure of Human R -State Aquomethemoglobin at 2.0 Å Resolution
    • Yi, J., Thomas, L. M., and Richter-Addo, G. B. (2011) Crystal Structure of Human R -State Aquomethemoglobin at 2.0 Å Resolution Acta Crystallogr. F67, 647-651
    • (2011) Acta Crystallogr. , vol.67 , pp. 647-651
    • Yi, J.1    Thomas, L.M.2    Richter-Addo, G.B.3
  • 44
    • 0000122597 scopus 로고    scopus 로고
    • Binding and Activation of Nitric Oxide by Metalloporphyrins and Heme
    • (Guilard, R. Smith, K. and Kadish, K. M. Eds.) Academic Press, New York.
    • Cheng, L. and Richter-Addo, G. B. (2000) Binding and Activation of Nitric Oxide by Metalloporphyrins and Heme. In The Porphyrin Handbook (Guilard, R., Smith, K., and Kadish, K. M., Eds.) Vol. 4, pp 219-291, Academic Press, New York.
    • (2000) The Porphyrin Handbook , vol.4 , pp. 219-291
    • Cheng, L.1    Richter-Addo, G.B.2
  • 45
    • 0013945984 scopus 로고
    • Exchange of Heme among Hemoglobin Molecules
    • (Addendum, p 1926)
    • Bunn, H. F. and Jandl, J. H. (1966) Exchange of Heme Among Hemoglobin Molecules Proc. Natl. Acad. Sci. U.S.A. 56, 974-978 (Addendum, p 1926)
    • (1966) Proc. Natl. Acad. Sci. U.S.A. , vol.56 , pp. 974-978
    • Bunn, H.F.1    Jandl, J.H.2
  • 46
    • 0027242099 scopus 로고
    • The porphyrin-iron hybrid hemoglobins. Absence of the Fe-His bonds in one type of subunits favors a deoxy-like structure with low oxygen affinity
    • Fujii, M., Hori, H., Miyazaki, G., Morimoto, H., and Yonetani, T. (1993) The Porphyrin-Iron Hybrid Hemoglobins: Absence of the Fe-His Bonds in One Type of Subunits Favors a Deoxy-Like Structure with Low-Oxygen Affinity J. Biol. Chem. 268, 15386-15393 (Pubitemid 23222026)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.21 , pp. 15386-15393
    • Fujii, M.1    Hori, H.2    Miyazaki, G.3    Morimoto, H.4    Yonetani, T.5
  • 47
    • 0014685779 scopus 로고
    • Formation of Hemichromes from Oxidized Hemoglobin Subunits
    • Rachmilewitz, E. A. (1969) Formation of Hemichromes From Oxidized Hemoglobin Subunits Ann. N.Y. Acad. Sci. 165, 171-184
    • (1969) Ann. N.Y. Acad. Sci. , vol.165 , pp. 171-184
    • Rachmilewitz, E.A.1
  • 48
    • 37049113745 scopus 로고
    • Nitrosation and Nitrosylation of Haemoproteins and Related Compounds. Part 1. Porphyrins and Metalloporphyrins
    • Bonnett, R., Charalambides, A. A., and Martin, R. A. (1978) Nitrosation and Nitrosylation of Haemoproteins and Related Compounds. Part 1. Porphyrins and Metalloporphyrins J. Chem. Soc., Perkin Trans. 1, 974-980
    • (1978) J. Chem. Soc., Perkin Trans. , vol.1 , pp. 974-980
    • Bonnett, R.1    Charalambides, A.A.2    Martin, R.A.3
  • 50
    • 0014665650 scopus 로고
    • Nitration of the Vinyl Groups of Ferriheme
    • Atassi, M. Z. (1969) Nitration of the Vinyl Groups of Ferriheme Biochim. Biophys. Acta 177, 663-665
    • (1969) Biochim. Biophys. Acta , vol.177 , pp. 663-665
    • Atassi, M.Z.1
  • 51
    • 37249051057 scopus 로고    scopus 로고
    • Peroxynitrite inactivation of human cytochrome P450s 2B6 and 2E1: Heme modification and site-specific nitrotyrosine formation
    • DOI 10.1021/tx700220e
    • Lin, H. L., Myshkin, E., Waskell, L., and Hollenberg, P. F. (2007) Peroxynitrite Inactivation of Human Cytochrome P450s 2B6 and 2E1: Heme Modification and Site-Specific Nitrotyrosine Formation Chem. Res. Toxicol. 20, 1612-1622 (Pubitemid 350275606)
    • (2007) Chemical Research in Toxicology , vol.20 , Issue.11 , pp. 1612-1622
    • Lin, H.-L.1    Myshkin, E.2    Waskell, L.3    Hollenberg, P.F.4
  • 52
    • 37049093269 scopus 로고
    • S -Nitrosation and the Reactions of S -Nitroso Compounds
    • Williams, D. L. H. (1985) S -Nitrosation and the Reactions of S -Nitroso Compounds Chem. Soc. Rev. 14, 171-196
    • (1985) Chem. Soc. Rev. , vol.14 , pp. 171-196
    • Williams, D.L.H.1
  • 53
    • 3543110157 scopus 로고    scopus 로고
    • Preparations of C -Nitroso Compounds
    • Gowenlock, B. G. and Richter-Addo, G. B. (2004) Preparations of C -Nitroso Compounds Chem. Rev. 104, 3315-3340
    • (2004) Chem. Rev. , vol.104 , pp. 3315-3340
    • Gowenlock, B.G.1    Richter-Addo, G.B.2
  • 54
    • 0007316074 scopus 로고
    • A Convenient Preparation of Conjugated Nitro Olefins by Electrochemical Methods
    • Kunai, A., Yanagi, Y., and Sasaki, K. (1983) A Convenient Preparation of Conjugated Nitro Olefins by Electrochemical Methods Tetrahedron Lett. 24, 4443-4444
    • (1983) Tetrahedron Lett. , vol.24 , pp. 4443-4444
    • Kunai, A.1    Yanagi, Y.2    Sasaki, K.3
  • 55
    • 0007311931 scopus 로고
    • Formation of Nitro-Compounds during Nitrosation of Olefins by Alkylnitrites
    • Yandovskii, V. N., Ryabinkin, I. I., and Tselinskii, I. V. (1980) Formation of Nitro-Compounds during Nitrosation of Olefins by Alkylnitrites Zh. Org. Khim. 16, 2084-2086
    • (1980) Zh. Org. Khim. , vol.16 , pp. 2084-2086
    • Yandovskii, V.N.1    Ryabinkin, I.I.2    Tselinskii, I.V.3
  • 56
    • 0014755113 scopus 로고
    • Unstable Hemoglobins: Role of Heme Loss in Heinz Body Formation
    • Jacob, H. and Winterhalter, K. H. (1970) Unstable Hemoglobins: Role of Heme Loss in Heinz Body Formation Proc. Natl. Acad. Sci. U.S.A. 65, 697-701
    • (1970) Proc. Natl. Acad. Sci. U.S.A. , vol.65 , pp. 697-701
    • Jacob, H.1    Winterhalter, K.H.2
  • 57
    • 0014882126 scopus 로고
    • Role of Hemoglobin Heme Loss in Heinz Body Formation: Studies with a Partially Heme-Deficient Hemoglobin and with Genetically Unstable Hemoglobins
    • Jacob, H. S. and Winterhalter, K. H. (1970) Role of Hemoglobin Heme Loss in Heinz Body Formation: Studies with a Partially Heme-Deficient Hemoglobin and with Genetically Unstable Hemoglobins J. Clin. Invest. 49, 2008-2016
    • (1970) J. Clin. Invest. , vol.49 , pp. 2008-2016
    • Jacob, H.S.1    Winterhalter, K.H.2
  • 58
    • 0038440472 scopus 로고
    • Heme Deficiency of β Chains: A Cause of Hemoglobin Precipitation in Congential Heinz Body Hemolytic Anemia (CHBHA)
    • (Abstract 286)
    • Winterhalter, K. H. and Jacob, H. S. (1969) Heme Deficiency of β Chains: A Cause of Hemoglobin Precipitation in Congential Heinz Body Hemolytic Anemia (CHBHA) J. Clin. Invest 48, A89 (Abstract 286)
    • (1969) J. Clin. Invest , vol.48 , pp. 89
    • Winterhalter, K.H.1    Jacob, H.S.2
  • 59
    • 79952608525 scopus 로고
    • Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement
    • Engh, R. A. and Huber, R. (1991) Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement Acta Crystallogr. A47, 392-400
    • (1991) Acta Crystallogr. , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.