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Volumn 253, Issue 1-2, 2003, Pages 49-54

Interaction of porphyrins with heme proteins - A brief review

Author keywords

Drug protein interaction; Hemoglobin; Myoglobin; Porphyrins

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); BEZAFIBRATE; CHLORPROMAZINE; CLOFIBRATE; CYTOCHROME C OXIDASE; GLUCOSE 6 PHOSPHATE ISOMERASE; HEMATOPORPHYRIN; HEMOGLOBIN; HEMOPROTEIN; LACTATE DEHYDROGENASE; MYOGLOBIN; NITRIC OXIDE SYNTHASE; OXYGEN; PEROXIDASE; PHENOTHIAZINE DERIVATIVE; PORPHOBILINOGEN DEAMINASE; PORPHOBILINOGEN SYNTHASE; PORPHYRIN DERIVATIVE; PROFLAVINE; PROTOPORPHYRIN; PYRUVATE KINASE; SUCCINATE DEHYDROGENASE; TRIFLUOPERAZINE;

EID: 0142181288     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1026097117057     Document Type: Review
Times cited : (31)

References (66)
  • 2
    • 0014412965 scopus 로고
    • Three-dimensional Fourier synthesis of horse oxyhemoglobin at 2.8 A resolution: The atomic model
    • Perutz MF, Muirhead H, Cox JM, Goaman LC: Three-dimensional Fourier synthesis of horse oxyhemoglobin at 2.8 A resolution: The atomic model. Nature 219: 131-139, 1968
    • (1968) Nature , vol.219 , pp. 131-139
    • Perutz, M.F.1    Muirhead, H.2    Cox, J.M.3    Goaman, L.C.4
  • 3
    • 0025344693 scopus 로고
    • Mechanisms regulating the reactions of human hemoglobin with oxygen and carbon monoxide
    • Perutz MF, Mechanisms regulating the reactions of human hemoglobin with oxygen and carbon monoxide. Ann Rev Physiol 52: 1-25, 1990
    • (1990) Ann. Rev. Physiol. , vol.52 , pp. 1-25
    • Perutz, M.F.1
  • 7
    • 0032873427 scopus 로고    scopus 로고
    • Stabilisation of the T-state of ferrous human adult haemoglobin by chlorpromazine and trifluoperazine
    • Ascenzi P, Bertollini A, Coletta M, Lucacchini A: Stabilisation of the T-state of ferrous human adult haemoglobin by chlorpromazine and trifluoperazine. Biotechnol Appl Biochem 30: 185-187, 1999
    • (1999) Biotechnol. Appl. Biochem. , vol.30 , pp. 185-187
    • Ascenzi, P.1    Bertollini, A.2    Coletta, M.3    Lucacchini, A.4
  • 8
    • 0030203638 scopus 로고    scopus 로고
    • Comparative studies on the interaction of protoporphyrin with hemoglobin and myoglobin
    • Sil S, Chakraborti AS: Comparative studies on the interaction of protoporphyrin with hemoglobin and myoglobin. Ind J Biochem Biophys 33: 285-291, 1996
    • (1996) Ind. J. Biochem. Biophys. , vol.33 , pp. 285-291
    • Sil, S.1    Chakraborti, A.S.2
  • 9
    • 0033028225 scopus 로고    scopus 로고
    • Stabilization of the T-state of human hemoglobin by proflavin, an antiseptic drug
    • Ascenzi P, Colasanti M, Fasano M, Bertollini A: Stabilization of the T-state of human hemoglobin by proflavin, an antiseptic drug. Biochem Mol Biol Int 47: 991-995, 1999
    • (1999) Biochem. Mol. Biol. Int. , vol.47 , pp. 991-995
    • Ascenzi, P.1    Colasanti, M.2    Fasano, M.3    Bertollini, A.4
  • 11
    • 0027324915 scopus 로고
    • Cooperative effect of inositol hexakisphosphate, bezafibrate and clofibric acid on the spectroscopic properties of the nitric oxide derivative of ferrous human hemoglobin
    • Ascenzi P, Bartollini A, Coletta M, Desideri A, Giardina B, Polizio F, Santucci R, Scatena R, Amiconi G: Cooperative effect of inositol hexakisphosphate, bezafibrate and clofibric acid on the spectroscopic properties of the nitric oxide derivative of ferrous human hemoglobin. J Inorg Biochem 50:263-272, 1993
    • (1993) J. Inorg. Biochem. , vol.50 , pp. 263-272
    • Ascenzi, P.1    Bartollini, A.2    Coletta, M.3    Desideri, A.4    Giardina, B.5    Polizio, F.6    Santucci, R.7    Scatena, R.8    Amiconi, G.9
  • 12
    • 0026876192 scopus 로고
    • Photochemotherapy of cancer: Experimental research
    • Moan J, Berg K: Photochemotherapy of cancer: experimental research. Photochem Photobiol 55: 931-948, 1992
    • (1992) Photochem. Photobiol. , vol.55 , pp. 931-948
    • Moan, J.1    Berg, K.2
  • 13
    • 0030939781 scopus 로고    scopus 로고
    • 5-Aminolevulinic acid-based photodynamic therapy. Clinical research and future challenges
    • Peng Q, Warloe T, Berg K, Moan J, Kongshaug M, Gieresky KE, Nesland JM: 5-Aminolevulinic acid-based photodynamic therapy. Clinical research and future challenges. Cancer 79: 2282-2308, 1997
    • (1997) Cancer , vol.79 , pp. 2282-2308
    • Peng, Q.1    Warloe, T.2    Berg, K.3    Moan, J.4    Kongshaug, M.5    Gieresky, K.E.6    Nesland, J.M.7
  • 15
    • 0032052666 scopus 로고    scopus 로고
    • Photodynamic therapy of intracranial tissues: A preclinical comparative study of four different photosensitizers
    • Lilge L, Wilson BC: Photodynamic therapy of intracranial tissues: A preclinical comparative study of four different photosensitizers. J Clin Laser Med Surg 16: 81-91, 1998
    • (1998) J. Clin. Laser Med. Surg. , vol.16 , pp. 81-91
    • Lilge, L.1    Wilson, B.C.2
  • 19
    • 0003127226 scopus 로고
    • Mechanisms and metabolic modulation of photosensitization
    • V. Jain, H. Goel (eds). Indian Photobiological Society, New Delhi
    • Jain V: Mechanisms and metabolic modulation of photosensitization. In: V. Jain, H. Goel (eds). Selected Topics in Photobiology. Indian Photobiological Society, New Delhi, 1992, pp 130-147
    • (1992) Selected Topics in Photobiology , pp. 130-147
    • Jain, V.1
  • 20
    • 0022727451 scopus 로고
    • Cellular uptake of hydroxyethylvinyldeuteroporphyrin (HVD) and photoactivation of cultivated human leukemia (REH6) cells
    • Dellinger M, Vever-Bizet C, Brault D, Delgado O, Rosenfeld C: Cellular uptake of hydroxyethylvinyldeuteroporphyrin (HVD) and photoactivation of cultivated human leukemia (REH6) cells. Photochem Photobiol 43: 639-647, 1986
    • (1986) Photochem. Photobiol. , vol.43 , pp. 639-647
    • Dellinger, M.1    Vever-Bizet, C.2    Brault, D.3    Delgado, O.4    Rosenfeld, C.5
  • 24
    • 0031114879 scopus 로고    scopus 로고
    • Effects of photofrin II and light on cellular adenine nucleotides and their modulation
    • Khanum F, Jain V: Effects of photofrin II and light on cellular adenine nucleotides and their modulation. Ind J Exp Biol 35: 356-360, 1997
    • (1997) Ind. J. Exp. Biol. , vol.35 , pp. 356-360
    • Khanum, F.1    Jain, V.2
  • 25
    • 0028832436 scopus 로고
    • Temperature-induced changes in fluorescence properties as a probe of porphyrin microenvironment in lipid membranes. 2. The partition of hematoporphyrin and protoporphyrin in mitochondria
    • Ricchelli F, Gobbo S, Jori C, Salet C, Moreno G: Temperature-induced changes in fluorescence properties as a probe of porphyrin microenvironment in lipid membranes. 2. The partition of hematoporphyrin and protoporphyrin in mitochondria. Eur J Biochem 233: 165-170, 1995
    • (1995) Eur. J. Biochem. , vol.233 , pp. 165-170
    • Ricchelli, F.1    Gobbo, S.2    Jori, C.3    Salet, C.4    Moreno, G.5
  • 26
    • 0031030190 scopus 로고    scopus 로고
    • Photodynamic therapy expands its horizons
    • Reynolds T: Photodynamic therapy expands its horizons. J Natl Cancer Inst 89: 112-114, 1997
    • (1997) J. Natl. Cancer Inst. , vol.89 , pp. 112-114
    • Reynolds, T.1
  • 28
    • 0028409859 scopus 로고
    • Photodynamic therapy with photofrin II induces programmed cell death in carcinoma cell lines
    • He XY, Sikes RA, Thomas S, Chung LW, Jacques SL: Photodynamic therapy with photofrin II induces programmed cell death in carcinoma cell lines. Photochem Photobiol 59: 468-473, 1994
    • (1994) Photochem. Photobiol. , vol.59 , pp. 468-473
    • He, X.Y.1    Sikes, R.A.2    Thomas, S.3    Chung, L.W.4    Jacques, S.L.5
  • 29
    • 0032499679 scopus 로고    scopus 로고
    • Photodynamic therapy results in induction of WAF1/CIP1/p21 leading to cell cycle arrest and apoptosis
    • Ahmed N, Feyes DK, Agarwal R, Mukhter H: Photodynamic therapy results in induction of WAF1/CIP1/p21 leading to cell cycle arrest and apoptosis. Proc Natl Acad Sci USA 95: 6977-6982, 1998
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6977-6982
    • Ahmed, N.1    Feyes, D.K.2    Agarwal, R.3    Mukhter, H.4
  • 30
    • 0020110038 scopus 로고
    • The effects of photoactivated protoporphyrin on reticulocyte membranes intracellular activities and hemoglobin precipitation
    • Breitbart H, Malik Z: The effects of photoactivated protoporphyrin on reticulocyte membranes intracellular activities and hemoglobin precipitation. Photochem Photobiol 35: 365-369, 1982
    • (1982) Photochem. Photobiol. , vol.35 , pp. 365-369
    • Breitbart, H.1    Malik, Z.2
  • 31
    • 0024006467 scopus 로고
    • Impairment of red cell membrane cytoskeleton by protoporphyrin IX: Light and dark effects
    • Dadosh N, Shaklai N: Impairment of red cell membrane cytoskeleton by protoporphyrin IX: Light and dark effects. Photochem Photobiol 47: 689-697, 1988
    • (1988) Photochem. Photobiol. , vol.47 , pp. 689-697
    • Dadosh, N.1    Shaklai, N.2
  • 32
    • 0029355252 scopus 로고
    • Alterations in erythrocyte band 3 organization induced by the photosensitizer, hematoporphyrin derivative
    • Beaton S, McPherson RA, Tilley L: Alterations in erythrocyte band 3 organization induced by the photosensitizer, hematoporphyrin derivative. Photochem Photobiol 62: 353-355, 1995
    • (1995) Photochem. Photobiol. , vol.62 , pp. 353-355
    • Beaton, S.1    McPherson, R.A.2    Tilley, L.3
  • 33
    • 85044704887 scopus 로고    scopus 로고
    • Effect of erythrocyte membrane structure on the dose dependence of photohemolysis
    • Bolodon VN, Krut'ko IV, Rozin VV, Chernitski EA: Effect of erythrocyte membrane structure on the dose dependence of photohemolysis. Biofizika 41: 413-416, 1996
    • (1996) Biofizika , vol.41 , pp. 413-416
    • Bolodon, V.N.1    Krut'ko, I.V.2    Rozin, V.V.3    Chernitski, E.A.4
  • 34
    • 0023445190 scopus 로고
    • Thermodynamics of porphyrin binding to serum albumin: Effects of temperature, of porphyrin species and of albumin-carried fatty acid
    • Rotenberg M, Cohen S, Margalit R: Thermodynamics of porphyrin binding to serum albumin: Effects of temperature, of porphyrin species and of albumin-carried fatty acid. Photochem Photobiol 46: 689-693, 1987
    • (1987) Photochem. Photobiol. , vol.46 , pp. 689-693
    • Rotenberg, M.1    Cohen, S.2    Margalit, R.3
  • 35
    • 0027688448 scopus 로고
    • Thermodynamics of the binding of hematoporphyrin ester, a hematoporphyrin derivative-like photosensitizer, and its components to human serum albumin, human high-density lipoprotein and human low-density lipoprotein
    • Rosenberger V, Margalit R: Thermodynamics of the binding of hematoporphyrin ester, a hematoporphyrin derivative-like photosensitizer, and its components to human serum albumin, human high-density lipoprotein and human low-density lipoprotein. Photochem Photobiol 58: 627-630, 1993
    • (1993) Photochem. Photobiol. , vol.58 , pp. 627-630
    • Rosenberger, V.1    Margalit, R.2
  • 36
    • 0028104002 scopus 로고
    • Conformational changes induced in bovine serum albumin by the photodynamic action of haematoporphyrin
    • Timmins GS, Davies MJ: Conformational changes induced in bovine serum albumin by the photodynamic action of haematoporphyrin. J Photochem Photobiol B: Biol 24: 117-122, 1994
    • (1994) J. Photochem. Photobiol. B: Biol. , vol.24 , pp. 117-122
    • Timmins, G.S.1    Davies, M.J.2
  • 37
    • 0019178958 scopus 로고
    • The interaction of human serum albumin and hemopexin with porphyrins
    • Morgan WT, Smith A, Koskelo P: The interaction of human serum albumin and hemopexin with porphyrins, Biochim Biophys Acta 624: 271-285, 1980
    • (1980) Biochim. Biophys. Acta , vol.624 , pp. 271-285
    • Morgan, W.T.1    Smith, A.2    Koskelo, P.3
  • 38
    • 0023661006 scopus 로고
    • Steady-state and time-resolved spectroscopic studies on the hematoporphyrin-lipoprotein complex
    • Beltramini M, Firey PA, Ricchelli F, Rodgers AJ, Jori G: Steady-state and time-resolved spectroscopic studies on the hematoporphyrin-lipoprotein complex. Biochemistry 26: 6852-6858, 1987
    • (1987) Biochemistry , vol.26 , pp. 6852-6858
    • Beltramini, M.1    Firey, P.A.2    Ricchelli, F.3    Rodgers, A.J.4    Jori, G.5
  • 40
    • 0343051863 scopus 로고    scopus 로고
    • Folding and unfolding of delta-aminolevulinic acid dehydratase and porphobilinogen deaminase induced by uro and protoporphyrin
    • Afonso SG, de Salamanca RE, Batle A: Folding and unfolding of delta-aminolevulinic acid dehydratase and porphobilinogen deaminase induced by uro and protoporphyrin. Int J Biochem Cell Biol 29: 493-503, 1997
    • (1997) Int. J. Biochem. Cell Biol. , vol.29 , pp. 493-503
    • Afonso, S.G.1    de Salamanca, R.E.2    Batle, A.3
  • 41
    • 0031282308 scopus 로고    scopus 로고
    • Rat harderian gland porphobilinogen deaminase: Characterization studies and regulatory action of protoporphyrin IX
    • Cardalda CA, Juknat AA, Princ FG, Badle A: Rat harderian gland porphobilinogen deaminase: Characterization studies and regulatory action of protoporphyrin IX. Arch Biochem Biophys 347: 69-77, 1997
    • (1997) Arch. Biochem. Biophys. , vol.347 , pp. 69-77
    • Cardalda, C.A.1    Juknat, A.A.2    Princ, F.G.3    Badle, A.4
  • 43
    • 0021276894 scopus 로고
    • Hematoporphyrin derivative-induced photosensitivity of mitochondrial succinate dehydrogenase and selected cytosolic enzymes of R3230AC mammary adenocarcinomas of rats
    • Hilf R, Small DB, Murant RS, Leakey PB, Gibson SL: Hematoporphyrin derivative-induced photosensitivity of mitochondrial succinate dehydrogenase and selected cytosolic enzymes of R3230AC mammary adenocarcinomas of rats. Cancer Res 44: 1483-1488, 1984
    • (1984) Cancer Res. , vol.44 , pp. 1483-1488
    • Hilf, R.1    Small, D.B.2    Murant, R.S.3    Leakey, P.B.4    Gibson, S.L.5
  • 44
    • 0023125704 scopus 로고
    • The mechanism of potentiation of horseradish peroxidase-catalysed oxidation of NADPH by porphyrins
    • van Steveninck J, Boegheim JP, Dubbelman TM, van der Zee J: The mechanism of potentiation of horseradish peroxidase-catalysed oxidation of NADPH by porphyrins. Biochem J 242: 611-613, 1987
    • (1987) Biochem. J. , vol.242 , pp. 611-613
    • van Steveninck, J.1    Boegheim, J.P.2    Dubbelman, T.M.3    van der Zee, J.4
  • 46
    • 0031394922 scopus 로고    scopus 로고
    • Protoporphyrin IX potentiates horseradish peroxidase-catalysed oxidation of NADH: Involvement of enzyme-porphyrin interaction
    • Sil S, Chakraborti AS: Protoporphyrin IX potentiates horseradish peroxidase-catalysed oxidation of NADH: Involvement of enzyme-porphyrin interaction. Biochem Mol Biol International: 42: 759-768, 1997
    • (1997) Biochem. Mol. Biol. International , vol.42 , pp. 759-768
    • Sil, S.1    Chakraborti, A.S.2
  • 47
    • 0020714068 scopus 로고
    • Fluorimetric studies on the dimerization equilibrium of protoporphyrin IX and its haematoderivative
    • Margalit R, Shaklai N, Cohen S: Fluorimetric studies on the dimerization equilibrium of protoporphyrin IX and its haematoderivative. Biochem J 209: 547-552, 1983
    • (1983) Biochem. J. , vol.209 , pp. 547-552
    • Margalit, R.1    Shaklai, N.2    Cohen, S.3
  • 48
    • 0027323492 scopus 로고
    • The photophysics of hematoporphyrin dimers of aggregates in aqueous solution
    • Smith GJ, Ghiggino KP: The photophysics of hematoporphyrin dimers of aggregates in aqueous solution. J Photochem Photobiol B: Biol 19: 49-54, 1993
    • (1993) J. Photochem. Photobiol. B: Biol. , vol.19 , pp. 49-54
    • Smith, G.J.1    Ghiggino, K.P.2
  • 50
    • 0017706885 scopus 로고
    • Binding of protoporphyrin to hemoglobin in red blood cells of patients with erythropoietic protoporphyria
    • van Steveninck J, Dubbelman TM, de Goeij AF, Went LN: Binding of protoporphyrin to hemoglobin in red blood cells of patients with erythropoietic protoporphyria. Hemoglobin 1: 679-690, 1977
    • (1977) Hemoglobin , vol.1 , pp. 679-690
    • van Steveninck, J.1    Dubbelman, T.M.2    de Goeij, A.F.3    Went, L.N.4
  • 51
    • 0016715953 scopus 로고
    • Erythropoietic protoporphyria and lead intoxication: The molecular basis for difference in cutaneous photosensitivity. II. Different binding of erythrocyte protoporphyrin to hemoglobin
    • Lamola AA, Piomelli S, Poh-Fitzpatric MG, Yamane T, Harber LC: Erythropoietic protoporphyria and lead intoxication: The molecular basis for difference in cutaneous photosensitivity. II. Different binding of erythrocyte protoporphyrin to hemoglobin. J Clin Invest 56: 1528-1533, 1975
    • (1975) J. Clin. Invest. , vol.56 , pp. 1528-1533
    • Lamola, A.A.1    Piomelli, S.2    Poh-Fitzpatric, M.G.3    Yamane, T.4    Harber, L.C.5
  • 52
    • 0027989869 scopus 로고
    • Fluorescent derivatives of human hemoglobin. Differences in interaction of the porphyrin with the protein between the alpha and beta subunits
    • Sudhakar K, Loe S, Yonetani T, Vanderkooi JM: Fluorescent derivatives of human hemoglobin. Differences in interaction of the porphyrin with the protein between the alpha and beta subunits. J Biol Chem 269: 23095-23101, 1994
    • (1994) J. Biol. Chem. , vol.269 , pp. 23095-23101
    • Sudhakar, K.1    Loe, S.2    Yonetani, T.3    Vanderkooi, J.M.4
  • 54
    • 0033653885 scopus 로고    scopus 로고
    • Haematoporphyrin enhances the peroxidase activity of hemoglobin
    • Sil S, Kar M, Chakraborti AS: Haematoporphyrin enhances the peroxidase activity of hemoglobin. J Porphyrins Phthalocyanines 4: 168-174, 2000
    • (2000) J. Porphyrins Phthalocyanines , vol.4 , pp. 168-174
    • Sil, S.1    Kar, M.2    Chakraborti, A.S.3
  • 55
    • 0036687148 scopus 로고    scopus 로고
    • Hematoporphyrin interacts with myoglobin and alters its functions
    • Sil S, Chakraborti AS: Hematoporphyrin interacts with myoglobin and alters its functions. Mol Cell Biochem 237: 103-110, 2002
    • (2002) Mol. Cell Biochem. , vol.237 , pp. 103-110
    • Sil, S.1    Chakraborti, A.S.2
  • 59
    • 0024514277 scopus 로고
    • Interaction of zinc protoporphyrin with intact oxyhemoglobin
    • Hirsch RE, Lin MJ, Park CM: Interaction of zinc protoporphyrin with intact oxyhemoglobin. Biochemistry 28: 1851-1855, 1989
    • (1989) Biochemistry , vol.28 , pp. 1851-1855
    • Hirsch, R.E.1    Lin, M.J.2    Park, C.M.3
  • 62
    • 0032577878 scopus 로고    scopus 로고
    • Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide
    • Nagababu E, Rifkind JM: Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide. Biochem Biophys Res Commun 247: 592-596, 1998
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 592-596
    • Nagababu, E.1    Rifkind, J.M.2
  • 63
    • 0032558387 scopus 로고    scopus 로고
    • Superoxide produced in the heme pocket of the β chain of hemoglobin reacts with the β 93 cysteine to produce a thiol radical
    • Balagopalkrishna C, Abugo OO, Horsky J, Mancharan PJ, Nagababu E, Rifkind JM: Superoxide produced in the heme pocket of the β chain of hemoglobin reacts with the β 93 cysteine to produce a thiol radical. Biochemistry 37: 13194-13199, 1998
    • (1998) Biochemistry , vol.37 , pp. 13194-13199
    • Balagopalkrishna, C.1    Abugo, O.O.2    Horsky, J.3    Mancharan, P.J.4    Nagababu, E.5    Rifkind, J.M.6
  • 64
    • 0022472686 scopus 로고
    • Biological effects of the superoxide radical
    • Fridovich I: Biological effects of the superoxide radical. Arch Biochem Biophys 247: 1-11, 1986
    • (1986) Arch. Biochem. Biophys. , vol.247 , pp. 1-11
    • Fridovich, I.1
  • 66
    • 0028365895 scopus 로고
    • Peroxidase activities of hemoglobin and hemoglobin derivatives
    • J. Everse, K.D. Vandegriff, R.M. Winslow (eds). Academic Press, New York
    • Everse J, Johnson MC, Marini MA: Peroxidase activities of hemoglobin and hemoglobin derivatives. In: J. Everse, K.D. Vandegriff, R.M. Winslow (eds). Methods in Enzymology, vol. 231. Academic Press, New York, 1994, pp 547-561
    • (1994) Methods in Enzymology , vol.231 , pp. 547-561
    • Everse, J.1    Johnson, M.C.2    Marini, M.A.3


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