메뉴 건너뛰기




Volumn 39, Issue 12, 2006, Pages 918-924

Reversible binding of heme to proteins in cellular signal transduction

Author keywords

[No Author keywords available]

Indexed keywords

HEME; HEMOPROTEIN; ION CHANNEL;

EID: 33846221929     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar040020w     Document Type: Review
Times cited : (94)

References (48)
  • 1
    • 10444268892 scopus 로고    scopus 로고
    • Heme-based sensors: Defining characteristics, recent developments, and regulatory hypotheses
    • Gilles-Gonzalez, M. A.; Gonzalez, G. Heme-based sensors: defining characteristics, recent developments, and regulatory hypotheses. J. Biol. Inorg. Chem. 2005, 99, 1-22.
    • (2005) J. Biol. Inorg. Chem , vol.99 , pp. 1-22
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2
  • 2
    • 0033511832 scopus 로고    scopus 로고
    • Cell biology of heme
    • Ponka, P. Cell biology of heme. Am. J. Med Sci. 1999, 318, 241-56.
    • (1999) Am. J. Med Sci , vol.318 , pp. 241-256
    • Ponka, P.1
  • 3
    • 27544434838 scopus 로고    scopus 로고
    • 30 some years of heme oxygenase: From a "molecular wrecking ball" to a "mesmerizing" trigger of cellular events
    • Maines, M. D.; Gibbs, P. E. 30 some years of heme oxygenase: from a "molecular wrecking ball" to a "mesmerizing" trigger of cellular events. Biochem. Biophys. Res. Commun. 2005, 338, 568-77.
    • (2005) Biochem. Biophys. Res. Commun , vol.338 , pp. 568-577
    • Maines, M.D.1    Gibbs, P.E.2
  • 5
    • 13244296905 scopus 로고    scopus 로고
    • Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases
    • Wu, R.; Skaar, E. P.; Zhang, R.; Joachimiak, G.; Gornicki, P.; Schneewind, O.; Joachimiak, A. Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases. J. Biol. Chem. 2005, 280, 2840-6.
    • (2005) J. Biol. Chem , vol.280 , pp. 2840-2846
    • Wu, R.1    Skaar, E.P.2    Zhang, R.3    Joachimiak, G.4    Gornicki, P.5    Schneewind, O.6    Joachimiak, A.7
  • 6
    • 0037898944 scopus 로고    scopus 로고
    • Autocatalytic radical reactions in physiological prosthetic heme modification
    • Colas, C.; Ortiz de Montellano, P. R. Autocatalytic radical reactions in physiological prosthetic heme modification. Chem. Rev. 2003, 103, 2305-32.
    • (2003) Chem. Rev , vol.103 , pp. 2305-2332
    • Colas, C.1    Ortiz de Montellano, P.R.2
  • 8
    • 0015842332 scopus 로고
    • Oxidation of deuteroferrihaem by hydrogen peroxide
    • Jones, P.; Prudhoe, K.; Robson, T. Oxidation of deuteroferrihaem by hydrogen peroxide. Biochem. J. 1973, 135, 361-5.
    • (1973) Biochem. J , vol.135 , pp. 361-365
    • Jones, P.1    Prudhoe, K.2    Robson, T.3
  • 9
    • 0027234437 scopus 로고
    • Hemin: Levels in experimental subarachnoid hematoma and effects on dissociated vascular smooth-muscle cells
    • Letarte, P. B.; Lieberman, K.; Nagatani, K.; Haworth, R. A.; Odell, G. B.; Duff, T. A. Hemin: levels in experimental subarachnoid hematoma and effects on dissociated vascular smooth-muscle cells. J. Neurosurg. 1993, 79, 252-5.
    • (1993) J. Neurosurg , vol.79 , pp. 252-255
    • Letarte, P.B.1    Lieberman, K.2    Nagatani, K.3    Haworth, R.A.4    Odell, G.B.5    Duff, T.A.6
  • 10
    • 0034978679 scopus 로고    scopus 로고
    • Characterization of a human plasma membrane heme transporter in intestinal and hepatocyte cell lines
    • Worthington, M. T.; Cohn, S. M.; Miller, S. K.; Luo, R. Q.; Berg, C. L. Characterization of a human plasma membrane heme transporter in intestinal and hepatocyte cell lines. Am. J. Physiol. 2001, 280, G1172-7.
    • (2001) Am. J. Physiol , vol.280
    • Worthington, M.T.1    Cohn, S.M.2    Miller, S.K.3    Luo, R.Q.4    Berg, C.L.5
  • 12
    • 0034112116 scopus 로고    scopus 로고
    • Bacterial heme sources: The role of heme, hemoprotein receptors and hemophores
    • Wandersman, C.; Stojiljkovic, I. Bacterial heme sources: the role of heme, hemoprotein receptors and hemophores. Curr. Opin. Microbiol. 2000, 3, 215-20.
    • (2000) Curr. Opin. Microbiol , vol.3 , pp. 215-220
    • Wandersman, C.1    Stojiljkovic, I.2
  • 13
    • 0028241788 scopus 로고
    • Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation
    • Gilles-Gonzalez, M. A.; Gonzalez, G.; Perutz, M. F.; Kiger, L.; Marden, M. C.; Poyart, C. Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation. Biochemistry 1994, 33, 8067-73.
    • (1994) Biochemistry , vol.33 , pp. 8067-8073
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2    Perutz, M.F.3    Kiger, L.4    Marden, M.C.5    Poyart, C.6
  • 14
    • 0021275463 scopus 로고
    • Regulation of soluble guanylate cyclase activity by porphyrins and metalloporphyrins
    • Ignarro, L. J.; Ballot, B.; Wood, K. S. Regulation of soluble guanylate cyclase activity by porphyrins and metalloporphyrins. J. Biol. Chem. 1984, 259, 6201-7.
    • (1984) J. Biol. Chem , vol.259 , pp. 6201-6207
    • Ignarro, L.J.1    Ballot, B.2    Wood, K.S.3
  • 15
    • 25144497879 scopus 로고    scopus 로고
    • Ligand discrimination in soluble guanylate cyclase and the H-NOX family of heme sensor proteins
    • Boon, E. M.; Marietta, M. A. Ligand discrimination in soluble guanylate cyclase and the H-NOX family of heme sensor proteins. Curr. Opin. Chem. Biol. 2005, 9, 441-6.
    • (2005) Curr. Opin. Chem. Biol , vol.9 , pp. 441-446
    • Boon, E.M.1    Marietta, M.A.2
  • 16
    • 0030021905 scopus 로고    scopus 로고
    • Binding of nitric oxide and carbon monoxide to soluble guanylate cyclase as observed with resonance raman spectroscopy
    • Deinum, G.; Stone, J. R.; Babcock, G. T.; Marletta, M. A. Binding of nitric oxide and carbon monoxide to soluble guanylate cyclase as observed with resonance raman spectroscopy. Biochemistry 1996, 35, 1540-7.
    • (1996) Biochemistry , vol.35 , pp. 1540-1547
    • Deinum, G.1    Stone, J.R.2    Babcock, G.T.3    Marletta, M.A.4
  • 17
    • 0028228808 scopus 로고
    • Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states
    • Stone, J. R.; Marietta, M. A. Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states. Biochemistry 1994, 33, 5636-40.
    • (1994) Biochemistry , vol.33 , pp. 5636-5640
    • Stone, J.R.1    Marietta, M.A.2
  • 19
    • 1842326840 scopus 로고    scopus 로고
    • A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli
    • Ghigo, J. M.; Letoffe, S.; Wandersman, C. A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli. J. Bacteriol. 1997, 179, 3572-9.
    • (1997) J. Bacteriol , vol.179 , pp. 3572-3579
    • Ghigo, J.M.1    Letoffe, S.2    Wandersman, C.3
  • 22
    • 0026559542 scopus 로고
    • Regulation of gene expression by oxygen in Saccharomyces cerevisiae
    • Zitomer, R. S.; Lowry, C. V. Regulation of gene expression by oxygen in Saccharomyces cerevisiae. Microbiol. Rev. 1992, 56, 1-11.
    • (1992) Microbiol. Rev , vol.56 , pp. 1-11
    • Zitomer, R.S.1    Lowry, C.V.2
  • 23
    • 10644259478 scopus 로고    scopus 로고
    • Role of Bach-1 in regulation of heme oxygenase-1 in human liver cells: Insights from studies with small interfering RNAS
    • Shan, Y.; Lambrecht, R. W.; Ghaziani, T.; Donohue, S. E.; Bonkovsky, H. L. Role of Bach-1 in regulation of heme oxygenase-1 in human liver cells: insights from studies with small interfering RNAS. J. Biol. Chem. 2004, 279, 51769-74.
    • (2004) J. Biol. Chem , vol.279 , pp. 51769-51774
    • Shan, Y.1    Lambrecht, R.W.2    Ghaziani, T.3    Donohue, S.E.4    Bonkovsky, H.L.5
  • 24
    • 0032729833 scopus 로고    scopus 로고
    • Molecular mechanism of heme signaling in yeast: The transcriptional activator Hap1 serves as the key mediator
    • Zhang, L.; Hach, A. Molecular mechanism of heme signaling in yeast: the transcriptional activator Hap1 serves as the key mediator. Cell. Mol. Life Sci. 1999, 56, 415-26.
    • (1999) Cell. Mol. Life Sci , vol.56 , pp. 415-426
    • Zhang, L.1    Hach, A.2
  • 25
    • 3042595446 scopus 로고    scopus 로고
    • A novel mode of chaperone action: Heme activation of Hap1 by enhanced association of Hsp90 with the repressed Hsp70-Hap1 complex
    • Lan, C.; Lee, H. C.; Tang, S.; Zhang, L. A novel mode of chaperone action: heme activation of Hap1 by enhanced association of Hsp90 with the repressed Hsp70-Hap1 complex. J. Biol. Chem. 2004, 279, 27607-12.
    • (2004) J. Biol. Chem , vol.279 , pp. 27607-27612
    • Lan, C.1    Lee, H.C.2    Tang, S.3    Zhang, L.4
  • 26
    • 0028821439 scopus 로고
    • Heme binds to a short sequence that serves a regulatory function in diverse proteins
    • Zhang, L.; Guarente, L. Heme binds to a short sequence that serves a regulatory function in diverse proteins. EMBO J. 1995, 14, 313-20.
    • (1995) EMBO J , vol.14 , pp. 313-320
    • Zhang, L.1    Guarente, L.2
  • 28
    • 0035860373 scopus 로고    scopus 로고
    • The solution structure and heme binding of the presequence of murine 5-aminolevulinate synthase
    • Goodfellow, B. J.; Dias, J. S.; Ferreira, G. C.; Henklein, P.; Wray, V.; Macedo, A. L. The solution structure and heme binding of the presequence of murine 5-aminolevulinate synthase. FEBS Lett. 2001, 505, 325-31.
    • (2001) FEBS Lett , vol.505 , pp. 325-331
    • Goodfellow, B.J.1    Dias, J.S.2    Ferreira, G.C.3    Henklein, P.4    Wray, V.5    Macedo, A.L.6
  • 29
    • 0029931330 scopus 로고    scopus 로고
    • High-conductance calcium-activated potassium channels; structure, pharmacology, and function
    • Kaczorowski, G. J.; Knaus, H. G.; Leonard, R. J.; McManus, O. B.; Garcia, M. L. High-conductance calcium-activated potassium channels; structure, pharmacology, and function. J. Bioenerg. Biomembr. 1996, 28, 255-67.
    • (1996) J. Bioenerg. Biomembr , vol.28 , pp. 255-267
    • Kaczorowski, G.J.1    Knaus, H.G.2    Leonard, R.J.3    McManus, O.B.4    Garcia, M.L.5
  • 30
    • 0037324895 scopus 로고    scopus 로고
    • Gating mechanism of BK (Slo1) channels: So near, yet so far
    • Magleby, K. L. Gating mechanism of BK (Slo1) channels: so near, yet so far. J. Gen. Physiol. 2003, 121, 81-96.
    • (2003) J. Gen. Physiol , vol.121 , pp. 81-96
    • Magleby, K.L.1
  • 31
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y.; Lee, A.; Chen, J.; Cadene, M.; Chait, B. T.; MacKinnon, R. Crystal structure and mechanism of a calcium-gated potassium channel. Nature 2002, 417, 515-22.
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 32
    • 0036714915 scopus 로고    scopus 로고
    • 2+ binding and channel opening in large conductance (BK) potassium channels
    • 2+ binding and channel opening in large conductance (BK) potassium channels. J. Gen. Physiol. 2002, 120, 267-305.
    • (2002) J. Gen. Physiol , vol.120 , pp. 267-305
    • Horrigan, F.T.1    Aldrich, R.W.2
  • 33
    • 0033067095 scopus 로고    scopus 로고
    • 2+ suggest a two-tiered allosteric gating mechanism
    • 2+ suggest a two-tiered allosteric gating mechanism. J. Gen. Physiol. 1999, 114, 93-124.
    • (1999) J. Gen. Physiol , vol.114 , pp. 93-124
    • Rothberg, B.S.1    Magleby, K.L.2
  • 34
    • 0141963861 scopus 로고    scopus 로고
    • Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK channels
    • Tang, X. D.; Xu, R.; Reynolds, M. F.; Garcia, M. L.; Heinemann, S. H.; Hoshi, T. Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK channels. Nature 2003, 425, 531-5.
    • (2003) Nature , vol.425 , pp. 531-535
    • Tang, X.D.1    Xu, R.2    Reynolds, M.F.3    Garcia, M.L.4    Heinemann, S.H.5    Hoshi, T.6
  • 36
    • 22244438901 scopus 로고    scopus 로고
    • Heme regulates allosteric activation of the Slo1 BK channel
    • Horrigan, F. T.; Heinemann, S. H.; Hoshi, T. Heme regulates allosteric activation of the Slo1 BK channel. J. Gen. Physiol. 2005, 126, 7-21.
    • (2005) J. Gen. Physiol , vol.126 , pp. 7-21
    • Horrigan, F.T.1    Heinemann, S.H.2    Hoshi, T.3
  • 41
    • 33846198877 scopus 로고    scopus 로고
    • 2+ increases the coupling of voltage-sensor activation to channel opening in BK potassium channels. Biophys. J. 2005, 88, 100a.
    • 2+ increases the coupling of voltage-sensor activation to channel opening in BK potassium channels. Biophys. J. 2005, 88, 100a.
  • 43
    • 2542461143 scopus 로고    scopus 로고
    • Carbon monoxide: To boldly go where NO has gone before
    • Ryter, S. W.; Morse, D.; Choi, A. M. Carbon monoxide: to boldly go where NO has gone before. Sci. STKE 2004, 2004, RE6.
    • (2004) Sci. STKE , vol.2004
    • Ryter, S.W.1    Morse, D.2    Choi, A.M.3
  • 44
    • 0030610004 scopus 로고    scopus 로고
    • Ca channels by carbon monoxide in vascular smooth muscle cells
    • Ca channels by carbon monoxide in vascular smooth muscle cells. J. Biol. Chem. 1997, 272, 8222-6.
    • (1997) J. Biol. Chem , vol.272 , pp. 8222-8226
    • Wang, R.1    Wu, L.2
  • 48
    • 0026686195 scopus 로고
    • Glutamyl-transfer RNA: A precursor of heme and chlorophyll biosynthesis
    • Jahn, D.; Verkamp, E.; Soll, D. Glutamyl-transfer RNA: a precursor of heme and chlorophyll biosynthesis. Trends Biochem. Sci. 1992, 17, 215-8.
    • (1992) Trends Biochem. Sci , vol.17 , pp. 215-218
    • Jahn, D.1    Verkamp, E.2    Soll, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.