메뉴 건너뛰기




Volumn 56, Issue 3, 2009, Pages 509-513

Flavonoids as reductants of ferryl hemoglobin

Author keywords

Ferryl hemoglobin; Flavonoids; Methemoglobin; Oxyhemoglobin

Indexed keywords

CATECHIN; FERRYLHEMOGLOBIN; FLAVONOID; HEMOGLOBIN; HYDROGEN PEROXIDE; METHEMOGLOBIN; OXYHEMOGLOBIN; REDUCING AGENT;

EID: 74049090909     PISSN: 0001527X     EISSN: 1734154X     Source Type: Journal    
DOI: 10.18388/abp.2009_2487     Document Type: Article
Times cited : (50)

References (27)
  • 3
    • 0038043329 scopus 로고    scopus 로고
    • t-BOOH-induced oxidative damage in sicle red blood cells and the role of flavonoids
    • Cesquini M, Torsoni MA, Stoppa GR, Ogo SH (2003) t-BOOH-induced oxidative damage in sicle red blood cells and the role of flavonoids. Biomed Pharmacol 57: 124-129.
    • (2003) Biomed Pharmacol , vol.57 , pp. 124-129
    • Cesquini, M.1    Torsoni, M.A.2    Stoppa, G.R.3    Ogo, S.H.4
  • 4
    • 52049095278 scopus 로고    scopus 로고
    • Peroxidase activity of hemoglobin towards ascorbate and urate: A synergistic protective strategy against toxicity of Hemoglobin-Based Oxygen Carriers (HBOC)
    • Cooper CE, Silaghi-Dumitrescu R, Rukengwa M, Alayash AI, Buehler PW (2008) Peroxidase activity of hemoglobin towards ascorbate and urate: A synergistic protective strategy against toxicity of Hemoglobin-Based Oxygen Carriers (HBOC). Biochim Biophys Acta 1784: 1415-1420.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1415-1420
    • Cooper, C.E.1    Silaghi-Dumitrescu, R.2    Rukengwa, M.3    Alayash, A.I.4    Buehler, P.W.5
  • 5
    • 0035749744 scopus 로고    scopus 로고
    • Role of flavonoids in oxidative stress
    • Cotelle N (2001) Role of flavonoids in oxidative stress. Curr Top Med Chem 1: 569-590.
    • (2001) Curr Top Med Chem , vol.1 , pp. 569-590
    • Cotelle, N.1
  • 6
    • 0028365895 scopus 로고
    • Peroxidative activities of hemoglobin and hemoglobin derivatives
    • Everse J, Johnson MC, Marini MA (1994) Peroxidative activities of hemoglobin and hemoglobin derivatives. Methods Enzymol 231: 547-561.
    • (1994) Methods Enzymol , vol.231 , pp. 547-561
    • Everse, J.1    Johnson, M.C.2    Marini, M.A.3
  • 7
    • 0031056208 scopus 로고    scopus 로고
    • The toxicities of native and modified hemoglobins
    • Everse J, Hsia N (1997) The toxicities of native and modified hemoglobins. Free Radic Biol Med 22: 1075-1099.
    • (1997) Free Radic Biol Med , vol.22 , pp. 1075-1099
    • Everse, J.1    Hsia, N.2
  • 8
    • 0025201423 scopus 로고
    • A novel antioxidant role for haemoglobin The comproportionation of ferrylhemoglobin with oxyhemoglobin
    • Giulivi C, Davies KJA (1990) A novel antioxidant role for haemoglobin. The comproportionation of ferrylhemoglobin with oxyhemoglobin. J Biol Chem 265: 19453-19460.
    • (1990) J Biol Chem , vol.265 , pp. 19453-19460
    • Giulivi, C.1    Davies, K.J.A.2
  • 9
    • 0028237681 scopus 로고
    • Hydrogen peroxide-mediated ferrylhemoglobin generation in vitro and in red blood cells
    • Giulivi C, Davies KJA (1994) Hydrogen peroxide-mediated ferrylhemoglobin generation in vitro and in red blood cells. Methods Enzymol 231: 490-496.
    • (1994) Methods Enzymol , vol.231 , pp. 490-496
    • Giulivi, C.1    Davies, K.J.A.2
  • 12
    • 0036774226 scopus 로고    scopus 로고
    • Flavonoid antioxidants: chemistry, metabolism and structure-activity relationships
    • Heim KE, Tagliaferro AR, Bobilya DJ (2002) Flavonoid antioxidants: chemistry, metabolism and structure-activity relationships. J Nutr Biochem 13: 572-584.
    • (2002) J Nutr Biochem , vol.13 , pp. 572-584
    • Heim, K.E.1    Tagliaferro, A.R.2    Bobilya, D.J.3
  • 13
    • 0037371492 scopus 로고    scopus 로고
    • Kinetics of the reactions of nitrogen monoxide and nitrite with ferryl haemoglobin
    • Herold S, Rehmann F-J (2003) Kinetics of the reactions of nitrogen monoxide and nitrite with ferryl haemoglobin. Free Radic Biol Med 34: 531-545.
    • (2003) Free Radic Biol Med , vol.34 , pp. 531-545
    • Herold, S.1    Rehmann, F.J.2
  • 14
    • 48649083488 scopus 로고    scopus 로고
    • Effects of (-)epigallicatechin gallate on the redox reactions of human hemoglobin
    • Jia Y, Alayash AI (2008) Effects of (-)epigallicatechin gallate on the redox reactions of human hemoglobin. Free Radic Biol Med 45: 659-666.
    • (2008) Free Radic Biol Med , vol.45 , pp. 659-666
    • Jia, Y.1    Alayash, A.I.2
  • 15
    • 0022001719 scopus 로고
    • Initiation of membrane lipid peroxidation by activated metmyoglobin and methemoglobin
    • Kanner J, Harel S (1985) Initiation of membrane lipid peroxidation by activated metmyoglobin and methemo-globin. Arch Biochem Biophys 237: 314-321.
    • (1985) Arch Biochem Biophys , vol.237 , pp. 314-321
    • Kanner, J.1    Harel, S.2
  • 16
    • 33846018587 scopus 로고    scopus 로고
    • Inactivation of alcohol dehydrogenase (ADH) by ferryl derivatives of human hemoglobin
    • Kowalczyk A, Puchala M, Wesolowska K, Serafin E (2007) Inactivation of alcohol dehydrogenase (ADH) by ferryl derivatives of human hemoglobin. Biochim Biophys Acta 1774: 86-92.
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 86-92
    • Kowalczyk, A.1    Puchala, M.2    Wesolowska, K.3    Serafin, E.4
  • 17
    • 0027366718 scopus 로고
    • Detection and reactions of the globin radical in hemoglobin
    • McArthur KM, Davies MJ (1993) Detection and reactions of the globin radical in hemoglobin. Biochim Biophys Acta 1202: 173-181.
    • (1993) Biochim Biophys Acta , vol.1202 , pp. 173-181
    • McArthur, K.M.1    Davies, M.J.2
  • 18
    • 0015502066 scopus 로고
    • The generation of superoxide anion during the autooxidation of haemoglobin
    • Misra HP, Fridovich I (1972) The generation of superoxide anion during the autooxidation of haemoglobin. J Biol Chem 247: 6960-6962.
    • (1972) J Biol Chem , vol.247 , pp. 6960-6962
    • Misra, H.P.1    Fridovich, I.2
  • 19
    • 0037081807 scopus 로고    scopus 로고
    • Kinetic analysis and mechanistic aspects of autooxidation of catechins
    • Mochizuki M, Yamazaki S, Kano K, Ikeda T (2002) Kinetic analysis and mechanistic aspects of autooxidation of catechins. Biochim Biophys Acta 1569: 35-44.
    • (2002) Biochim Biophys Acta , vol.1569 , pp. 35-44
    • Mochizuki, M.1    Yamazaki, S.2    Kano, K.3    Ikeda, T.4
  • 21
    • 0034633998 scopus 로고    scopus 로고
    • Reaction of hydrogen peroxide with ferrylhemoglobin: superoxide production and heme degradation
    • Nagababu E, RiPalatinoLinotype-Roman.-1.CID.f.kind JM (2000) Reaction of hydrogen peroxide with ferrylhemoglobin: superoxide production and heme degradation. Biochemistry 39: 12503-12511.
    • (2000) Biochemistry , vol.39 , pp. 12503-12511
    • Nagababu, E.1    RiPalatinoLinotype-Roman.-1.CI.D. kind JM, F.2
  • 22
    • 0037062603 scopus 로고    scopus 로고
    • Site-specific cross linking of human and bovine hemoglobins differentially alters oxygen binding and redox reactions producing rhombic heme and heme degradation
    • Nagababu E, Ramasamy S, RiPalatinoLinotype-Roman.-1.CID.f.kind JM, Jia Y, Alayash AI (2002) Site-specific cross linking of human and bovine hemoglobins differentially alters oxygen binding and redox reactions producing rhombic heme and heme degradation. Biochemistry 41: 7407-7415.
    • (2002) Biochemistry , vol.41 , pp. 7407-7415
    • Nagababu, E.1    Ramasamy, S.2    RiPalatinoLinotype-Roman.-1.CI.D. kind, F.3    Jia, J.M.4    Alayash AI, Y.5
  • 23
    • 0029908785 scopus 로고    scopus 로고
    • Redox cycling of human methaemo-globin by H2O2 yields persistent ferryl iron and protein-based radicals
    • Patel RP, Svistunenko DA, Darley-Usmar V, Symons MCR, Wilson MT (1996) Redox cycling of human methaemo-globin by H2O2 yields persistent ferryl iron and protein-based radicals. Free Radic Res 25: 117-123.
    • (1996) Free Radic Res , vol.25 , pp. 117-123
    • Patel, R.P.1    Svistunenko, D.A.2    Darley-Usmar, V.3    Symons, M.C.R.4    Wilson, M.T.5
  • 25
    • 33846039915 scopus 로고    scopus 로고
    • The influence of ferrylhemoglobin and methemoglobin on the human erythrocyte membrane
    • Sztiller M, Puchala M, Kowalczyk A, Bartosz G (2006) The influence of ferrylhemoglobin and methemoglobin on the human erythrocyte membrane. Redox Rep 11: 263-271.
    • (2006) Redox Rep , vol.11 , pp. 263-271
    • Sztiller, M.1    Puchala, M.2    Kowalczyk, A.3    Bartosz, G.4
  • 26
    • 0034884327 scopus 로고    scopus 로고
    • Reaction of melatonin with hemoglobin-derived oxoferryl radicals and inhibition of the hydroperoxide-induced hemoglobin denaturation in red blood cells
    • Tesoriere L, Allegra M, D'Arpa D, Butera D, Livrea MA (2001) Reaction of melatonin with hemoglobin-derived oxoferryl radicals and inhibition of the hydroperoxide-induced hemoglobin denaturation in red blood cells. J Pineal Res 31: 114-119.
    • (2001) J Pineal Res , vol.31 , pp. 114-119
    • Tesoriere, L.1    Allegra, M.2    D'Arpa, D.3    Butera, D.4    Livrea, M.A.5
  • 27
    • 0025145949 scopus 로고
    • Oxidative reactions of hemoglobin
    • Winterbourn CC (1990) Oxidative reactions of hemoglobin. Methods Enzymol 186: 265-272.
    • (1990) Methods Enzymol , vol.186 , pp. 265-272
    • Winterbourn, C.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.