메뉴 건너뛰기




Volumn 289, Issue 43, 2014, Pages 29836-29858

Protein/protein interactions in the mammalian heme degradation pathway: Heme oxygenase-2, cytochrome P450 reductase, and biliverdin reductase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSIS; EXPERIMENTS; FLUORESCENCE; MAMMALS; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PIGMENTS; QUENCHING; SURFACE PLASMON RESONANCE;

EID: 84908428449     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.582783     Document Type: Article
Times cited : (30)

References (64)
  • 1
    • 4544220638 scopus 로고    scopus 로고
    • Why heme needs to be degraded to iron, biliverdin IXα, and carbon monoxide?
    • Sassa, S. (2004) Why heme needs to be degraded to iron, biliverdin IXα, and carbon monoxide? Antioxid. Redox Signal. 6, 819-824
    • (2004) Antioxid. Redox Signal. , vol.6 , pp. 819-824
    • Sassa, S.1
  • 2
    • 34948858043 scopus 로고    scopus 로고
    • Heme as a magnificent molecule with multiple missions: Heme determines its own fate and governs cellular homeostasis
    • Furuyama, K., Kaneko, K., and Vargas, P. D. (2007) Heme as a magnificent molecule with multiple missions: heme determines its own fate and governs cellular homeostasis. Tohoku J. Exp. Med. 213, 1-16
    • (2007) Tohoku J. Exp. Med. , vol.213 , pp. 1-16
    • Furuyama, K.1    Kaneko, K.2    Vargas, P.D.3
  • 3
    • 4544272023 scopus 로고    scopus 로고
    • The heme oxygenase system: Past, present, and future
    • Maines, M. D. (2004) The heme oxygenase system: past, present, and future. Antioxid. Redox Signal. 6, 797-801
    • (2004) Antioxid. Redox Signal. , vol.6 , pp. 797-801
    • Maines, M.D.1
  • 4
    • 28844432578 scopus 로고    scopus 로고
    • The heme oxygenase system: Update 2005
    • Maines, M. D. (2005) The heme oxygenase system: update 2005. Antioxid. Redox. Signal. 7, 1761-1766
    • (2005) Antioxid. Redox. Signal. , vol.7 , pp. 1761-1766
    • Maines, M.D.1
  • 5
    • 0027423904 scopus 로고
    • Carbon monoxide: An emerging regulator of cGMP in the brain
    • Maines, M. D. (1993) Carbon monoxide: an emerging regulator of cGMP in the brain. Mol. Cell. Neurosci. 4, 389-397
    • (1993) Mol. Cell. Neurosci. , vol.4 , pp. 389-397
    • Maines, M.D.1
  • 7
    • 84876732556 scopus 로고    scopus 로고
    • Carbon monoxide and the brain: Time to rethink the dogma
    • Hanafy, K. A., Oh, J., and Otterbein, L. E. (2013) Carbon monoxide and the brain: time to rethink the dogma. Curr. Pharm. Des. 19, 2771-2775
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 2771-2775
    • Hanafy, K.A.1    Oh, J.2    Otterbein, L.E.3
  • 9
    • 77953704443 scopus 로고    scopus 로고
    • Conversion of biliverdin to bilirubin by biliverdin reductase contributes to endothelial cell protection by heme oxygenase-1-evidence for direct and indirect antioxidant actions of bilirubin
    • Jansen, T., Hortmann, M., Oelze, M., Opitz, B., Steven, S., Schell, R., Knorr, M., Karbach, S., Schuhmacher, S., Wenzel, P., Münzel, T., and Daiber, A. (2010) Conversion of biliverdin to bilirubin by biliverdin reductase contributes to endothelial cell protection by heme oxygenase-1-evidence for direct and indirect antioxidant actions of bilirubin. J. Mol. Cell. Cardiol. 49, 186-195
    • (2010) J. Mol. Cell. Cardiol. , vol.49 , pp. 186-195
    • Jansen, T.1    Hortmann, M.2    Oelze, M.3    Opitz, B.4    Steven, S.5    Schell, R.6    Knorr, M.7    Karbach, S.8    Schuhmacher, S.9    Wenzel, P.10    Münzel, T.11    Daiber, A.12
  • 12
    • 8544246393 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3
    • McCoubrey, W. K., Jr., Huang, T. J., and Maines, M. D. (1997) Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3. Eur. J. Biochem. 247, 725-732
    • (1997) Eur. J. Biochem. , vol.247 , pp. 725-732
    • McCoubrey, W.K.1    Huang, T.J.2    Maines, M.D.3
  • 13
    • 3042799349 scopus 로고    scopus 로고
    • Characterization of rat heme oxygenase-3 gene. Implication of processed pseudogenes derived from heme oxygenase-2 gene
    • Hayashi, S., Omata, Y., Sakamoto, H., Higashimoto, Y., Hara, T., Sagara, Y., and Noguchi, M. (2004) Characterization of rat heme oxygenase-3 gene. Implication of processed pseudogenes derived from heme oxygenase-2 gene. Gene 336, 241-250
    • (2004) Gene , vol.336 , pp. 241-250
    • Hayashi, S.1    Omata, Y.2    Sakamoto, H.3    Higashimoto, Y.4    Hara, T.5    Sagara, Y.6    Noguchi, M.7
  • 15
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: A regulator of second messenger gases
    • Maines, M. D. (1997) The heme oxygenase system: a regulator of second messenger gases. Annu. Rev. Pharmacol. Toxicol. 37, 517-554
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 16
    • 0034871085 scopus 로고    scopus 로고
    • Heme oxygenase-2 interaction with metalloporphyrins: Function of heme regulatory motifs
    • Huang, T. J., McCoubrey, W. K., Jr., and Maines, M. D. (2001) Heme oxygenase-2 interaction with metalloporphyrins: function of heme regulatory motifs. Antioxid. Redox Signal. 3, 685-696
    • (2001) Antioxid. Redox Signal. , vol.3 , pp. 685-696
    • Huang, T.J.1    McCoubrey, W.K.2    Maines, M.D.3
  • 17
    • 34547121697 scopus 로고    scopus 로고
    • Evidence that the heme regulatory motifs in heme oxygenase-2 serve as a thiol/disulfide redox switch regulating heme binding
    • Yi, L., and Ragsdale, S. W. (2007) Evidence that the heme regulatory motifs in heme oxygenase-2 serve as a thiol/disulfide redox switch regulating heme binding. J. Biol. Chem. 282, 21056-21067
    • (2007) J. Biol. Chem. , vol.282 , pp. 21056-21067
    • Yi, L.1    Ragsdale, S.W.2
  • 18
    • 68949122857 scopus 로고    scopus 로고
    • Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state
    • Yi, L., Jenkins, P. M., Leichert, L. I., Jakob, U., Martens, J. R., and Ragsdale, S. W. (2009) Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state. J. Biol. Chem. 284, 20556-20561
    • (2009) J. Biol. Chem. , vol.284 , pp. 20556-20561
    • Yi, L.1    Jenkins, P.M.2    Leichert, L.I.3    Jakob, U.4    Martens, J.R.5    Ragsdale, S.W.6
  • 19
    • 84867406948 scopus 로고    scopus 로고
    • Role of cysteine residues in heme binding to human heme oxygenase-2 elucidated by two-dimensional NMR spectroscopy
    • Varfaj, F., Lampe, J. N., and Ortiz de Montellano, P. R. (2012) Role of cysteine residues in heme binding to human heme oxygenase-2 elucidated by two-dimensional NMR spectroscopy. J. Biol. Chem. 287, 35181-35191
    • (2012) J. Biol. Chem. , vol.287 , pp. 35181-35191
    • Varfaj, F.1    Lampe, J.N.2    Ortiz De Montellano, P.R.3
  • 20
    • 0002473529 scopus 로고
    • (Ortiz de Montellano, P. R., ed) Springer-Verlag Inc., New York
    • Strobel, H. W., Hodgson, A. V., and Shen., S. (1995) in Cytochrome P450 (Ortiz de Montellano, P. R., ed) pp. 225-244, Springer-Verlag Inc., New York
    • (1995) Cytochrome P450 , pp. 225-244
    • Strobel, H.W.1    Hodgson, A.V.2    Shen, S.3
  • 21
    • 0014670945 scopus 로고
    • Microsomal heme oxygenase. Characterization of the enzyme
    • Tenhunen, R., Marver, H. S., and Schmid, R. (1969) Microsomal heme oxygenase. Characterization of the enzyme. J. Biol. Chem. 244, 6388-6394
    • (1969) J. Biol. Chem. , vol.244 , pp. 6388-6394
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 22
    • 0019335801 scopus 로고
    • Inability of the NADH-cytochrome b5 reductase system to initiate heme degradation yielding biliverdin IX α from the oxygenated form of heme. heme oxygenase complex
    • Yoshida, T., Noguchi, M., and Kikuchi, G. (1980) Inability of the NADH-cytochrome b5 reductase system to initiate heme degradation yielding biliverdin IX α from the oxygenated form of heme. heme oxygenase complex. FEBS Lett. 115, 278-280
    • (1980) FEBS Lett. , vol.115 , pp. 278-280
    • Yoshida, T.1    Noguchi, M.2    Kikuchi, G.3
  • 23
    • 79955833019 scopus 로고    scopus 로고
    • Uncovering the role of hydrophobic residues in cytochrome P450-cytochrome P450 reductase interactions
    • Kenaan, C., Zhang, H., Shea, E. V., and Hollenberg, P. F. (2011) Uncovering the role of hydrophobic residues in cytochrome P450-cytochrome P450 reductase interactions. Biochemistry 50, 3957-3967
    • (2011) Biochemistry , vol.50 , pp. 3957-3967
    • Kenaan, C.1    Zhang, H.2    Shea, E.V.3    Hollenberg, P.F.4
  • 25
    • 38649111634 scopus 로고    scopus 로고
    • Mass spectrometric identification of lysine residues of heme oxygenase-1 that are involved in its interaction with NADPH-cytochrome P450 reductase
    • Higashimoto, Y., Sugishima, M., Sato, H., Sakamoto, H., Fukuyama, K., Palmer, G., and Noguchi, M. (2008) Mass spectrometric identification of lysine residues of heme oxygenase-1 that are involved in its interaction with NADPH-cytochrome P450 reductase. Biochem. Biophys. Res. Commun. 367, 852-858
    • (2008) Biochem. Biophys. Res. Commun. , vol.367 , pp. 852-858
    • Higashimoto, Y.1    Sugishima, M.2    Sato, H.3    Sakamoto, H.4    Fukuyama, K.5    Palmer, G.6    Noguchi, M.7
  • 26
    • 84894379725 scopus 로고    scopus 로고
    • Structural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenase
    • Sugishima, M., Sato, H., Higashimoto, Y., Harada, J., Wada, K., Fukuyama, K., and Noguchi, M. (2014) Structural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenase. Proc. Natl. Acad. Sci. U.S.A. 111, 2524-2529
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 2524-2529
    • Sugishima, M.1    Sato, H.2    Higashimoto, Y.3    Harada, J.4    Wada, K.5    Fukuyama, K.6    Noguchi, M.7
  • 27
    • 0038165531 scopus 로고    scopus 로고
    • The binding sites on human heme oxygenase-1 for cytochrome p450 reductase and biliverdin reductase
    • Wang, J., and de Montellano, P. R. (2003) The binding sites on human heme oxygenase-1 for cytochrome p450 reductase and biliverdin reductase. J. Biol. Chem. 278, 20069-20076
    • (2003) J. Biol. Chem. , vol.278 , pp. 20069-20076
    • Wang, J.1    De Montellano, P.R.2
  • 28
    • 0036890399 scopus 로고    scopus 로고
    • The cytochrome P450 superfamily: Biochemistry, evolution and drug metabolism in humans
    • Danielson, P. B. (2002) The cytochrome P450 superfamily: biochemistry, evolution and drug metabolism in humans. Curr. Drug Metab. 3, 561-597
    • (2002) Curr. Drug Metab. , vol.3 , pp. 561-597
    • Danielson, P.B.1
  • 29
    • 0018801347 scopus 로고
    • Cytochrome b5 reduction by NADPH-cytochrome P-450 reductase
    • Enoch, H. G., and Strittmatter, P. (1979) Cytochrome b5 reduction by NADPH-cytochrome P-450 reductase. J. Biol. Chem. 254, 8976-8981
    • (1979) J. Biol. Chem. , vol.254 , pp. 8976-8981
    • Enoch, H.G.1    Strittmatter, P.2
  • 30
    • 73649173283 scopus 로고
    • Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver
    • Williams, C. H., Jr., and Kamin, H. (1962) Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver. J. Biol. Chem. 237, 587-595
    • (1962) J. Biol. Chem. , vol.237 , pp. 587-595
    • Williams, C.H.1    Kamin, H.2
  • 31
    • 0016641043 scopus 로고
    • Solubilization and partial characterization of rat liver squalene epoxidase
    • Ono, T., and Bloch, K. (1975) Solubilization and partial characterization of rat liver squalene epoxidase. J. Biol. Chem. 250, 1571-1579
    • (1975) J. Biol. Chem. , vol.250 , pp. 1571-1579
    • Ono, T.1    Bloch, K.2
  • 32
    • 84860196579 scopus 로고    scopus 로고
    • Heme oxygenase isoforms differ in their subcellular trafficking during hypoxia and are differentially modulated by cytochrome P450 reductase
    • Linnenbaum, M., Busker, M., Kraehling, J. R., and Behrends, S. (2012) Heme oxygenase isoforms differ in their subcellular trafficking during hypoxia and are differentially modulated by cytochrome P450 reductase. PLoS One 7, e35483
    • (2012) PLoS One , vol.7 , pp. e35483
    • Linnenbaum, M.1    Busker, M.2    Kraehling, J.R.3    Behrends, S.4
  • 33
    • 0019887888 scopus 로고
    • Purification and characterization of biliverdin reductase from rat liver
    • Kutty, R. K., and Maines, M. D. (1981) Purification and characterization of biliverdin reductase from rat liver. J. Biol. Chem. 256, 3956-3962
    • (1981) J. Biol. Chem. , vol.256 , pp. 3956-3962
    • Kutty, R.K.1    Maines, M.D.2
  • 34
    • 0035123138 scopus 로고    scopus 로고
    • Nuclear localization of biliverdin reductase in the rat kidney: Response to nephrotoxins that induce heme oxygenase-1
    • Maines, M. D., Ewing, J. F., Huang, T. J., and Panahian, N. (2001) Nuclear localization of biliverdin reductase in the rat kidney: response to nephrotoxins that induce heme oxygenase-1. J. Pharmacol. Exp. Ther. 296, 1091-1097
    • (2001) J. Pharmacol. Exp. Ther. , vol.296 , pp. 1091-1097
    • Maines, M.D.1    Ewing, J.F.2    Huang, T.J.3    Panahian, N.4
  • 35
    • 0037088596 scopus 로고    scopus 로고
    • Human biliverdin reductase is a leucine zipper-like DNA-binding protein and functions in transcriptional activation of heme oxygenase-1 by oxidative stress
    • Ahmad, Z., Salim, M., and Maines, M. D. (2002) Human biliverdin reductase is a leucine zipper-like DNA-binding protein and functions in transcriptional activation of heme oxygenase-1 by oxidative stress. J. Biol. Chem. 277, 9226-9232
    • (2002) J. Biol. Chem. , vol.277 , pp. 9226-9232
    • Ahmad, Z.1    Salim, M.2    Maines, M.D.3
  • 36
    • 48249153856 scopus 로고    scopus 로고
    • Biliverdin reductase is a transporter of haem into the nucleus and is essential for regulation of HO-1 gene expression by haematin
    • Tudor, C., Lerner-Marmarosh, N., Engelborghs, Y., Gibbs, P. E., and Maines, M. D. (2008) Biliverdin reductase is a transporter of haem into the nucleus and is essential for regulation of HO-1 gene expression by haematin. Biochem. J. 413, 405-416
    • (2008) Biochem. J. , vol.413 , pp. 405-416
    • Tudor, C.1    Lerner-Marmarosh, N.2    Engelborghs, Y.3    Gibbs, P.E.4    Maines, M.D.5
  • 37
    • 20444445069 scopus 로고    scopus 로고
    • Small interference RNA-mediated gene silencing of human biliverdin reductase, but not that of heme oxygenase-1, attenuates arsenite-mediated induction of the oxygenase and increases apoptosis in 293A kidney cells
    • Miralem, T., Hu, Z., Torno, M. D., Lelli, K. M., and Maines, M. D. (2005) Small interference RNA-mediated gene silencing of human biliverdin reductase, but not that of heme oxygenase-1, attenuates arsenite-mediated induction of the oxygenase and increases apoptosis in 293A kidney cells. J. Biol. Chem. 280, 17084-17092
    • (2005) J. Biol. Chem. , vol.280 , pp. 17084-17092
    • Miralem, T.1    Hu, Z.2    Torno, M.D.3    Lelli, K.M.4    Maines, M.D.5
  • 38
    • 18844371482 scopus 로고    scopus 로고
    • Human biliverdin reductase: A member of the insulin receptor substrate family with serine/threonine/tyrosine kinase activity
    • Lerner-Marmarosh, N., Shen, J., Torno, M. D., Kravets, A., Hu, Z., and Maines, M. D. (2005) Human biliverdin reductase: A member of the insulin receptor substrate family with serine/threonine/tyrosine kinase activity. Proc. Natl. Acad. Sci. U.S.A. 102, 7109-7114
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 7109-7114
    • Lerner-Marmarosh, N.1    Shen, J.2    Torno, M.D.3    Kravets, A.4    Hu, Z.5    Maines, M.D.6
  • 39
    • 44349190488 scopus 로고    scopus 로고
    • Human biliverdin reductase is an ERK activator; hBVR is an ERK nuclear transporter and is required for MAPK signaling
    • Lerner-Marmarosh, N., Miralem, T., Gibbs, P. E., and Maines, M. D. (2008) Human biliverdin reductase is an ERK activator; hBVR is an ERK nuclear transporter and is required for MAPK signaling. Proc. Natl. Acad. Sci. U.S.A. 105, 6870-6875
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 6870-6875
    • Lerner-Marmarosh, N.1    Miralem, T.2    Gibbs, P.E.3    Maines, M.D.4
  • 40
    • 0040141555 scopus 로고    scopus 로고
    • Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1
    • Liu, Y., and Ortiz de Montellano, P. R. (2000) Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1. J. Biol. Chem. 275, 5297-5307
    • (2000) J. Biol. Chem. , vol.275 , pp. 5297-5307
    • Liu, Y.1    Ortiz De Montellano, P.R.2
  • 41
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • Aslanidis, C., and de Jong, P. J. (1990) Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res. 18, 6069-6074
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6069-6074
    • Aslanidis, C.1    De Jong, P.J.2
  • 42
    • 33845967142 scopus 로고    scopus 로고
    • Diminished FAD binding in the Y459H and V492E Antley-Bixler syndrome mutants of human cytochrome P450 reductase
    • Marohnic, C. C., Panda, S. P., Martásek, P., and Masters, B. S. (2006) Diminished FAD binding in the Y459H and V492E Antley-Bixler syndrome mutants of human cytochrome P450 reductase. J. Biol. Chem. 281, 35975-35982
    • (2006) J. Biol. Chem. , vol.281 , pp. 35975-35982
    • Marohnic, C.C.1    Panda, S.P.2    Martásek, P.3    Masters, B.S.4
  • 44
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 48
    • 0001610304 scopus 로고
    • Notes on bias in estimation
    • Quenouille, M. H. (1956) Notes on bias in estimation. Biometrika 43, 353-360
    • (1956) Biometrika , vol.43 , pp. 353-360
    • Quenouille, M.H.1
  • 50
    • 63849254891 scopus 로고    scopus 로고
    • Measurement of membrane-bound human heme oxygenase-1 activity using a chemically defined assay system
    • Huber, W. J., 3rd, Marohnic, C. C., Peters, M., Alam, J., Reed, J. R., Masters, B. S., and Backes, W. L. (2009) Measurement of membrane-bound human heme oxygenase-1 activity using a chemically defined assay system. Drug Metab. Dispos. 37, 857-864
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 857-864
    • Huber, W.J.1    Marohnic, C.C.2    Peters, M.3    Alam, J.4    Reed, J.R.5    Masters, B.S.6    Backes, W.L.7
  • 51
    • 20444380585 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of heterogeneous protein-protein interactions: Lamm equation modeling and sedimentation coefficient distributions c(s)
    • Dam, J., Velikovsky, C. A., Mariuzza, R. A., Urbanke, C., and Schuck, P. (2005) Sedimentation velocity analysis of heterogeneous protein-protein interactions: Lamm equation modeling and sedimentation coefficient distributions c(s). Biophys. J. 89, 619-634
    • (2005) Biophys. J. , vol.89 , pp. 619-634
    • Dam, J.1    Velikovsky, C.A.2    Mariuzza, R.A.3    Urbanke, C.4    Schuck, P.5
  • 52
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78, 1606-1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 54
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin, K., Riek, R., Wider, G., and Wüthrich, K. (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl. Acad. Sci. U.S.A. 94, 12366-12371
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 55
    • 38049144525 scopus 로고    scopus 로고
    • Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2
    • Bianchetti, C. M., Yi, L., Ragsdale, S. W., and Phillips, G. N., Jr. (2007) Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2. J. Biol. Chem. 282, 37624-37631
    • (2007) J. Biol. Chem. , vol.282 , pp. 37624-37631
    • Bianchetti, C.M.1    Yi, L.2    Ragsdale, S.W.3    Phillips, G.N.4
  • 59
    • 0028238581 scopus 로고
    • Site-directed mutagenesis of cysteine residues in biliverdin reductase. Roles in substrate and cofactor binding
    • McCoubrey, W. K., Jr., and Maines, M. D. (1994) Site-directed mutagenesis of cysteine residues in biliverdin reductase. Roles in substrate and cofactor binding. Eur. J. Biochem. 222, 597-603
    • (1994) Eur. J. Biochem. , vol.222 , pp. 597-603
    • McCoubrey, W.K.1    Maines, M.D.2
  • 60
    • 0142213304 scopus 로고    scopus 로고
    • Close encounters of the transient kind: Protein interactions in the photosynthetic redox chain investigated by NMR spectroscopy
    • Crowley, P. B., and Ubbink, M. (2003) Close encounters of the transient kind: protein interactions in the photosynthetic redox chain investigated by NMR spectroscopy. Acc. Chem. Res. 36, 723-730
    • (2003) Acc. Chem. Res. , vol.36 , pp. 723-730
    • Crowley, P.B.1    Ubbink, M.2
  • 61
    • 62849090890 scopus 로고    scopus 로고
    • The courtship of proteins: Understanding the encounter complex
    • Ubbink, M. (2009) The courtship of proteins: understanding the encounter complex. FEBS Lett. 583, 1060-1066
    • (2009) FEBS Lett. , vol.583 , pp. 1060-1066
    • Ubbink, M.1
  • 62
    • 0019390569 scopus 로고
    • 31P NMR study of the kinetics of binding of myo-inositol hexakisphosphate to human hemoglobin. Observation of fast-exchange kinetics in high affinity systems
    • Zuiderweg, E. R., Hamers, L. F., Rollema, H. S., de Bruin, S. H., and Hilbers, C. W. (1981) 31P NMR study of the kinetics of binding of myo-inositol hexakisphosphate to human hemoglobin. Observation of fast-exchange kinetics in high affinity systems. Eur. J. Biochem. 118, 95-104
    • (1981) Eur. J. Biochem. , vol.118 , pp. 95-104
    • Zuiderweg, E.R.1    Hamers, L.F.2    Rollema, H.S.3    De Bruin, S.H.4    Hilbers, C.W.5
  • 63
    • 84908402388 scopus 로고    scopus 로고
    • (Clore, G., and Potts, J., eds) Royal Society of Chemistry, Cambridge, UK
    • Zuiderweg, E. R. (2012) in Recent Developments in Biomolecular NMR (Clore, G., and Potts, J., eds) pp. 216-252, Royal Society of Chemistry, Cambridge, UK
    • Recent Developments in Biomolecular NMR , vol.2012 , pp. 216-252
    • Zuiderweg, E.R.1
  • 64
    • 77249168703 scopus 로고    scopus 로고
    • Heme oxygenase reveals its strategy for catalyzing three successive oxygenation reactions
    • Matsui, T., Unno, M., and Ikeda-Saito, M. (2010) Heme oxygenase reveals its strategy for catalyzing three successive oxygenation reactions. Acc. Chem. Res. 43, 240-247
    • (2010) Acc. Chem. Res. , vol.43 , pp. 240-247
    • Matsui, T.1    Unno, M.2    Ikeda-Saito, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.