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Volumn 34, Issue 2, 2014, Pages 134-143

Human cytochrome b5 reductase: Structure, function, and potential applications

Author keywords

FAD domain; FNR family; Heterologous expression; Mechanism of action; NADH domain; Phylogenetics; Purification; RCM

Indexed keywords

PROTEINS; PURIFICATION;

EID: 84901804264     PISSN: 07388551     EISSN: 15497801     Source Type: Journal    
DOI: 10.3109/07388551.2012.732031     Document Type: Review
Times cited : (67)

References (109)
  • 1
    • 0033948250 scopus 로고    scopus 로고
    • A case of methemoglobinemia type II due to NADH-cytochrome b5 reductase deficiency: Determination of the molecular basis
    • DOI 10.1002/1098-1004(200007)16:1<18::AID-HUMU4>3.0.CO;2-N
    • Aalfs CM, Salieb-Beugelaar GB, Wanders RJ, Mannens MM, Wijburg FA. 2000. A case of methemoglobinemia type II due to NADH-cytochrome b5 reductase deficiency: determination of the molecular basis. Hum Mutat 16: 18-22. (Pubitemid 30447963)
    • (2000) Human Mutation , vol.16 , Issue.1 , pp. 18-22
    • Aalfs, C.M.1    Salieb-Beugelaar, G.B.2    Wanders, R.J.A.3    Mannens, M.M.A.M.4    Wijburg, F.A.5
  • 2
    • 79952607363 scopus 로고    scopus 로고
    • Evaluation of sulfonamide detoxification pathways in haematologic malignancy patients prior to intermittent trimethoprim-sulfamethoxazole prophylaxis
    • Abouraya M, Sacco JC, Kahl BS, Trepanier LA. 2011. Evaluation of sulfonamide detoxification pathways in haematologic malignancy patients prior to intermittent trimethoprim-sulfamethoxazole prophylaxis. Br J Clin Pharmacol 71: 566-574.
    • (2011) Br J Clin Pharmacol , vol.71 , pp. 566-574
    • Abouraya, M.1    Sacco, J.C.2    Kahl, B.S.3    Trepanier, L.A.4
  • 3
    • 0026567527 scopus 로고
    • Purification and characterization of two forms of soluble NADH cytochrome b5 reductases from human erythrocytes
    • Arinç E, Güray T, Saplakoglu U, Adali O. 1992. Purification and characterization of two forms of soluble NADH cytochrome b5 reductases from human erythrocytes. Comp Biochem Physiol, B 101: 235-242.
    • (1992) Comp Biochem Physiol, B , vol.101 , pp. 235-242
    • Arinç, E.1    Güray, T.2    Saplakoglu, U.3    Adali, O.4
  • 4
    • 43949144599 scopus 로고    scopus 로고
    • Molecular dynamics simulation study on stabilities and reactivities of NADH cytochrome B5 reductase
    • DOI 10.1021/jp7101513
    • Asada T, Nagase S, Nishimoto K, Koseki S. 2008. Molecular dynamics simulation study on stabilities and reactivities of NADH cytochrome B5 reductase. J Phys Chem B 112: 5718-5727. (Pubitemid 351704588)
    • (2008) Journal of Physical Chemistry B , vol.112 , Issue.18 , pp. 5718-5727
    • Asada, T.1    Nagase, S.2    Nishimoto, K.3    Koseki, S.4
  • 5
    • 67349145536 scopus 로고    scopus 로고
    • Simulation study of interactions and reactivities between NADH cytochrome b5 reductase and cytochrome b5
    • Asada T, Nagase S, Nishimoto K, Koseki S. 2009. Simulation study of interactions and reactivities between NADH cytochrome b5 reductase and cytochrome b5. J Mol Liq 147: 139-144.
    • (2009) J Mol Liq , vol.147 , pp. 139-144
    • Asada, T.1    Nagase, S.2    Nishimoto, K.3    Koseki, S.4
  • 6
    • 0020534836 scopus 로고
    • 5 reductase from human neutrophils
    • Badwey JA, Tauber AI, Karnovsky ML. 1983. Properties of NADH cytochrome-b5 reductase from human neutrophils. Blood 62: 152-157. (Pubitemid 13070605)
    • (1983) Blood , vol.62 , Issue.1 , pp. 152-157
    • Badwey, J.A.1    Tauber, A.I.2    Karnovsky, M.L.3
  • 8
    • 0030219743 scopus 로고    scopus 로고
    • 5 reductase
    • DOI 10.1006/prep.1996.0072
    • Barber MJ, Quinn GB. 1996. High-level expression in Escherichia coli of the soluble, catalytic domain of rat hepatic cytochrome b5 reductase. Protein Expr Purif 8: 41-47. (Pubitemid 26331211)
    • (1996) Protein Expression and Purification , vol.8 , Issue.1 , pp. 41-47
    • Barber, M.J.1    Quinn, G.B.2
  • 9
    • 0034760650 scopus 로고    scopus 로고
    • Production of a recombinant hybrid hemoflavoprotein: Engineering a functional NADH:cytochrome c reductase
    • DOI 10.1006/prep.2001.1518
    • Barber MJ, Quinn GB. 2001. Production of a recombinant hybrid hemoflavoprotein: engineering a functional NADH:cytochrome c reductase. Protein Expr Purif 23: 348-358. (Pubitemid 33037804)
    • (2001) Protein Expression and Purification , vol.23 , Issue.2 , pp. 348-358
    • Barber, M.J.1    Quinn, G.B.2
  • 11
    • 0034194412 scopus 로고    scopus 로고
    • Les methemoglobinemies hereditaires
    • DOI 10.1016/S0929-693X(00)89008-9
    • Beauvais P. 2000. [Hereditary methemoglobinemias]. Arch Pediatr 7: 513-518. (Pubitemid 30305486)
    • (2000) Archives de Pediatrie , vol.7 , Issue.5 , pp. 513-518
    • Beauvais, P.1
  • 12
    • 0032502684 scopus 로고    scopus 로고
    • 5 reductase modulates the cytotoxicity of the mitomycins to Chinese hamster ovary cells
    • DOI 10.1074/jbc.273.15.8875
    • Belcourt MF, Hodnick WF, Rockwell S, Sartorelli AC. 1998. The intracellular location of NADH:cytochrome b5 reductase modulates the cytotoxicity of the mitomycins to Chinese hamster ovary cells. J Biol Chem 273: 8875-8881. (Pubitemid 28176169)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.15 , pp. 8875-8881
    • Belcourt, M.F.1    Hodnick, W.F.2    Rockwell, S.3    Sartorelli, A.C.4
  • 13
    • 0242653652 scopus 로고    scopus 로고
    • 5 Reductase that Causes Methemoglobinemia Shows the AMP Moiety of the Flavin Occupying the Substrate Binding Site
    • DOI 10.1021/bi034915c
    • Bewley MC, Davis CA, Marohnic CC, Taormina D, Barber MJ. 2003. The structure of the S127P mutant of cytochrome b5 reductase that causes methemoglobinemia shows the AMP moiety of the flavin occupying the substrate binding site. Biochemistry 42: 13145-13151. (Pubitemid 37420666)
    • (2003) Biochemistry , vol.42 , Issue.45 , pp. 13145-13151
    • Bewley, M.C.1    Davis, C.A.2    Marohnic, C.C.3    Taormina, D.4    Barber, M.J.5
  • 14
    • 0035856561 scopus 로고    scopus 로고
    • 5 reductase are now consistent
    • DOI 10.1021/bi0106336
    • Bewley MC, Marohnic CC, Barber MJ. 2001. The structure and biochemistry of NADH-dependent cytochrome b5 reductase are now consistent. Biochemistry 40: 13574-13582. (Pubitemid 33130785)
    • (2001) Biochemistry , vol.40 , Issue.45 , pp. 13574-13582
    • Bewley, M.C.1    Marohnic, C.C.2    Barber, M.J.3
  • 15
    • 0020491414 scopus 로고
    • Rat erythrocyte NADH-cytochrome b5 reductase. Quantitation and comparison between the membrane-bound and soluble forms using an antibody against the rat liver enzyme
    • Borgese N, Macconi D, Parola L, Pietrini G. 1982. Rat erythrocyte NADH-cytochrome b5 reductase. Quantitation and comparison between the membrane-bound and soluble forms using an antibody against the rat liver enzyme. J Biol Chem 257: 13854-13861.
    • (1982) J Biol Chem , vol.257 , pp. 13854-13861
    • Borgese, N.1    MacConi, D.2    Parola, L.3    Pietrini, G.4
  • 18
    • 0141463707 scopus 로고    scopus 로고
    • Congenital methemoglobinemia: A rare cause of cyanosis in the newborn-A case report
    • Da-Silva SS, Sajan IS, Underwood JP. 2003. Congenital methemoglobinemia: a rare cause of cyanosis in the newborn-a case report. Pediatrics 112: e158-e161.
    • (2003) Pediatrics , vol.112
    • Da-Silva, S.S.1    Sajan, I.S.2    Underwood, J.P.3
  • 19
    • 16544368613 scopus 로고    scopus 로고
    • 5 reductase: The roles of the recessive congenital methemoglobinemia mutants P144L, L148P, and R159
    • DOI 10.1016/j.abb.2004.08.005, PII S0003986104004564
    • Davis CA, Crowley LJ, Barber MJ. 2004. Cytochrome b5 reductase: the roles of the recessive congenital methemoglobinemia mutants P144L, L148P, and R159*. Arch Biochem Biophys 431: 233-244. (Pubitemid 39369929)
    • (2004) Archives of Biochemistry and Biophysics , vol.431 , Issue.2 , pp. 233-244
    • Ainsley Davis, C.1    Crowley, L.J.2    Barber, M.J.3
  • 20
    • 0036544589 scopus 로고    scopus 로고
    • 5 reductase fusion protein: Identification of histidines 62 and 85 as the heme axial ligands
    • DOI 10.1006/abbi.2002.2783
    • Davis CA, Dhawan IK, Johnson MK, Barber MJ. 2002. Heterologous expression of an endogenous rat cytochrome b(5)/cytochrome b(5) reductase fusion protein: identification of histidines 62 and 85 as the heme axial ligands. Arch Biochem Biophys 400: 63-75. (Pubitemid 34852261)
    • (2002) Archives of Biochemistry and Biophysics , vol.400 , Issue.1 , pp. 63-75
    • Davis, C.A.1    Dhawan, I.K.2    Johnson, M.K.3    Barber, M.J.4
  • 22
    • 36849051197 scopus 로고    scopus 로고
    • 5 and their reductases-Promising targets for structural studies by advanced solid-state NMR spectroscopy
    • DOI 10.1016/j.bbamem.2007.08.007, PII S0005273607002945
    • Dürr UH, Waskell L, Ramamoorthy A. 2007. The cytochromes P450 and b5 and their reductases-promising targets for structural studies by advanced solid-state NMR spectroscopy. Biochim Biophys Acta 1768: 3235-3259. (Pubitemid 350236080)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.12 , pp. 3235-3259
    • Durr, U.H.N.1    Waskell, L.2    Ramamoorthy, A.3
  • 25
    • 0032817558 scopus 로고    scopus 로고
    • Microsomal electron transfer in higher plants: Cloning and heterologous expression of NADH-cytochrome b5 reductase from Arabidopsis
    • Fukuchi-Mizutani M, Mizutani M, Tanaka Y, Kusumi T, Ohta D. 1999. Microsomal electron transfer in higher plants: cloning and heterologous expression of NADH-cytochrome b5 reductase from Arabidopsis. Plant Physiol 119: 353-362.
    • (1999) Plant Physiol , vol.119 , pp. 353-362
    • Fukuchi-Mizutani, M.1    Mizutani, M.2    Tanaka, Y.3    Kusumi, T.4    Ohta, D.5
  • 26
    • 0021765493 scopus 로고
    • Purification of a NADH-ferricyanide reductase from plant microsomal membranes with a zwitterionic detergent
    • Galle AM, Bonnerot C, Jolliot A, Kader JC. 1984. Purification of a NADH-ferricyanide reductase from plant microsomal membranes with a zwitterionic detergent. Biochem Biophys Res Commun 122: 1201-1205.
    • (1984) Biochem Biophys Res Commun , vol.122 , pp. 1201-1205
    • Galle, A.M.1    Bonnerot, C.2    Jolliot, A.3    Kader, J.C.4
  • 27
    • 0003103451 scopus 로고
    • The reduction of methaemoglobin in red blood cells and studies on the cause of idiopathic methaemoglobinaemia
    • Gibson QH. 1948. The reduction of methaemoglobin in red blood cells and studies on the cause of idiopathic methaemoglobinaemia. Biochem J 42: 13-23.
    • (1948) Biochem J , vol.42 , pp. 13-23
    • Gibson, Q.H.1
  • 29
    • 0025170830 scopus 로고
    • 5 reductase from sheep lung and its electrophoretic, spectral and some other properties
    • DOI 10.1016/0020-711X(90)90210-T
    • Guray T, Arinç E. 1990. Purification of NADH-cytochrome b5 reductase from sheep lung and its electrophoretic, spectral and some other properties. Int J Biochem 22: 1029-1037. (Pubitemid 20319073)
    • (1990) International Journal of Biochemistry , vol.22 , Issue.9 , pp. 1029-1037
    • Guray, T.1    Arinc, E.2
  • 30
    • 4344717788 scopus 로고    scopus 로고
    • Expression of a Stokesia laevis epoxygenase gene
    • DOI 10.1016/j.phytochem.2004.06.006, PII S0031942204002559
    • Hatanaka T, Shimizu R, Hildebrand D. 2004. Expression of a Stokesia laevis epoxygenase gene. Phytochemistry 65: 2189-2196. (Pubitemid 39140665)
    • (2004) Phytochemistry , vol.65 , Issue.15 , pp. 2189-2196
    • Hatanaka, T.1    Shimizu, R.2    Hildebrand, D.3
  • 32
    • 0038813752 scopus 로고    scopus 로고
    • 5 reductase activity increases the cytotoxicity of mitomycin C (MC) and the total number of MC-DNA adducts in Chinese hamster ovary cells
    • DOI 10.1074/jbc.M209722200
    • Holtz KM, Rockwell S, Tomasz M, Sartorelli AC. 2003. Nuclear overexpression of NADH:cytochrome b5 reductase activity increases the cytotoxicity of mitomycin C (MC) and the total number of MCDNA adducts in Chinese hamster ovary cells. J Biol Chem 278: 5029-5034. (Pubitemid 36801012)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.7 , pp. 5029-5034
    • Holtz, K.M.1    Rockwell, S.2    Tomasz, M.3    Sartorelli, A.C.4
  • 33
  • 34
    • 0025367107 scopus 로고
    • 5 reductase
    • DOI 10.1016/0006-291X(90)91168-R
    • Hyde GE, Campbell WH. 1990. High-level expression in Escherichia coli of the catalytically active flavin domain of corn leaf NADH:nitrate reductase and its comparison to human NADH:cytochrome B5 reductase. Biochem Biophys Res Commun 168: 1285-1291. (Pubitemid 20176019)
    • (1990) Biochemical and Biophysical Research Communications , vol.168 , Issue.3 , pp. 1285-1291
    • Hyde, G.E.1    Campbell, W.H.2
  • 35
    • 0021771672 scopus 로고
    • One-electron oxidationreduction properties of hepatic NADH-cytochrome b5 reductase
    • Iyanagi T, Watanabe S, Anan KF. 1984. One-electron oxidationreduction properties of hepatic NADH-cytochrome b5 reductase. Biochemistry 23: 1418-1425.
    • (1984) Biochemistry , vol.23 , pp. 1418-1425
    • Iyanagi, T.1    Watanabe, S.2    Anan, K.F.3
  • 36
    • 0029881835 scopus 로고    scopus 로고
    • A novel mutation found in the 3' domain of NADH-cytochrome B5 reductase in an African-American family with type I congenital methemoglobinemia
    • Jenkins MM, Prchal JT. 1996. A novel mutation found in the 3' domain of NADH-cytochrome B5 reductase in an African-American family with type I congenital methemoglobinemia. Blood 87: 2993-2999.
    • (1996) Blood , vol.87 , pp. 2993-2999
    • Jenkins, M.M.1    Prchal, J.T.2
  • 37
    • 0031016046 scopus 로고    scopus 로고
    • A high-frequency polymorphism of NADH-cytochrome b5 reductase in African-Americans
    • DOI 10.1007/s004390050347
    • Jenkins MM, Prchal JT. 1997. A high-frequency polymorphism of NADH-cytochrome b5 reductase in African-Americans. Hum Genet 99: 248-250. (Pubitemid 27073330)
    • (1997) Human Genetics , vol.99 , Issue.2 , pp. 248-250
    • Jenkins, M.M.1    Prchal, J.T.2
  • 38
    • 0001277128 scopus 로고
    • Electrophoresis of red cell NADH- and NADPH-diaphorases in normal subjects and patients with congenital methemoglobinemia
    • Kaplan JC, Beutler E. 1967. Electrophoresis of red cell NADH- and NADPH-diaphorases in normal subjects and patients with congenital methemoglobinemia. Biochem Biophys Res Commun 29: 605-610.
    • (1967) Biochem Biophys Res Commun , vol.29 , pp. 605-610
    • Kaplan, J.C.1    Beutler, E.2
  • 39
    • 79951931273 scopus 로고    scopus 로고
    • Severe mental retardation and recessive congenital methemoglobinemia in three Indian patients: Compound heterozygous for NADH-cytochrome b5 reductase gene mutations
    • Kedar PS, Warang P, Ghosh K, Colah RB. 2011. Severe mental retardation and recessive congenital methemoglobinemia in three Indian patients: compound heterozygous for NADH-cytochrome b5 reductase gene mutations. Am J Hematol 86: 327-329.
    • (2011) Am J Hematol , vol.86 , pp. 327-329
    • Kedar, P.S.1    Warang, P.2    Ghosh, K.3    Colah, R.B.4
  • 40
    • 0021100464 scopus 로고
    • Isolation and partial characterization of the NH2-terminal membrane-binding domain of NADH-cytochrome b5 reductase
    • Kensil CR, Hediger MA, Ozols J, Strittmatter P. 1983. Isolation and partial characterization of the NH2-terminal membrane-binding domain of NADH-cytochrome b5 reductase. J Biol Chem 258: 14656-14663.
    • (1983) J Biol Chem , vol.258 , pp. 14656-14663
    • Kensil, C.R.1    Hediger, M.A.2    Ozols, J.3    Strittmatter, P.4
  • 42
    • 0037423305 scopus 로고    scopus 로고
    • 5 reductase in catalysis and control of the rate-limiting step in electron transfer
    • DOI 10.1074/jbc.M209838200
    • Kimura S, Kawamura M, Iyanagi T. 2003. Role of Thr(66) in porcine NADH-cytochrome b5 reductase in catalysis and control of the rate-limiting step in electron transfer. J Biol Chem 278: 3580-3589. (Pubitemid 36801081)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.6 , pp. 3580-3589
    • Kimura, S.1    Kawamura, M.2    Iyanagi, T.3
  • 43
    • 0034759905 scopus 로고    scopus 로고
    • 5 reductase catalytic domain on protein stability and catalysis
    • Kimura S, Nishida H, Iyanagi T. 2001. Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on protein stability and catalysis. J Biochem 130: 481-490. (Pubitemid 33021591)
    • (2001) Journal of Biochemistry , vol.130 , Issue.4 , pp. 481-490
    • Kimura, S.1    Nishida, H.2    Iyanagi, T.3
  • 44
    • 20444409704 scopus 로고    scopus 로고
    • Two-cistronic expression plasmids for high-level gene expression in Escherichia coli preventing translational initiation inhibition caused by the intramolecular local secondary structure of mRNA
    • DOI 10.1093/jb/mvi065
    • Kimura S, Umemura T, Iyanagi T. 2005. Two-cistronic expression plasmids for high-level gene expression in Escherichia coli preventing translational initiation inhibition caused by the intramolecular local secondary structure of mRNA. J Biochem 137: 523-533. (Pubitemid 40806052)
    • (2005) Journal of Biochemistry , vol.137 , Issue.4 , pp. 523-533
    • Kimura, S.1    Umemura, T.2    Iyanagi, T.3
  • 45
    • 0019598623 scopus 로고
    • Purification and properties of human erythrocyte membrane NADH-cytochrome b5 reductase
    • Kitajima S, Yasukochi Y, Minakami S. 1981. Purification and properties of human erythrocyte membrane NADH-cytochrome b5 reductase. Arch Biochem Biophys 210: 330-339.
    • (1981) Arch Biochem Biophys , vol.210 , pp. 330-339
    • Kitajima, S.1    Yasukochi, Y.2    Minakami, S.3
  • 46
    • 0025260711 scopus 로고
    • Serine-proline replacement at residue 127 of NADH-cytochrome b5 reductase causes hereditary methemoglobinemia, generalized type
    • Kobayashi Y, Fukumaki Y, Yubisui T, Inoue J, Sakaki Y. 1990. Serineproline replacement at residue 127 of NADH-cytochrome b5 reductase causes hereditary methemoglobinemia, generalized type. Blood 75: 1408-1413. (Pubitemid 20114877)
    • (1990) Blood , vol.75 , Issue.7 , pp. 1408-1413
    • Kobayashi, Y.1    Fukumaki, Y.2    Yubisui, T.3    Inoue, J.4    Sakaki, Y.5
  • 47
    • 17544394876 scopus 로고    scopus 로고
    • Molecular basis of recessive congenital methemoglobinemia, types I and II: Exon skipping and three novel missense mutations in the NADH-cytochrome b5 reductase (diaphorase 1) gene
    • Kugler W, Pekrun A, Laspe P, Erdlenbruch B, Lakomek M. 2001. Molecular basis of recessive congenital methemoglobinemia, types I and II: Exon skipping and three novel missense mutations in the NADH-cytochrome b5 reductase (diaphorase 1) gene. Hum Mutat 17: 348.
    • (2001) Hum Mutat , vol.17 , pp. 348
    • Kugler, W.1    Pekrun, A.2    Laspe, P.3    Erdlenbruch, B.4    Lakomek, M.5
  • 48
    • 33845538326 scopus 로고    scopus 로고
    • A mutation in Arabidopsis cytochrome b5 reductase identified by high-throughput screening differentially affects hydroxylation and desaturation
    • DOI 10.1111/j.1365-313X.2006.02925.x
    • Kumar R, Wallis JG, Skidmore C, Browse J. 2006. A mutation in Arabidopsis cytochrome b5 reductase identified by high-throughput screening differentially affects hydroxylation and desaturation. Plant J 48: 920-932. (Pubitemid 44924352)
    • (2006) Plant Journal , vol.48 , Issue.6 , pp. 920-932
    • Kumar, R.1    Wallis, J.G.2    Skidmore, C.3    Browse, J.4
  • 49
    • 0032496426 scopus 로고    scopus 로고
    • Antibody-based spot test for NADH-cytochrome b5 reductase activity for the laboratory diagnosis of congenital methemoglobinemia
    • Lan FH, Tang YC, Huang CH, Wu YS, Zhu ZY. 1998. Antibody-based spot test for NADH-cytochrome b5 reductase activity for the laboratory diagnosis of congenital methemoglobinemia. Clin Chim Acta 273: 13-20.
    • (1998) Clin Chim Acta , vol.273 , pp. 13-20
    • Lan, F.H.1    Tang, Y.C.2    Huang, C.H.3    Wu, Y.S.4    Zhu, Z.Y.5
  • 50
    • 0017571643 scopus 로고
    • Leukocyte diaphorase deficiency in congenital methemoglobinemia: A valuable prognostic indicator
    • Lawson DL, Miale TD, Harvey JL, Bucciarelli RL, Nelson LS. 1977. Leukocyte diaphorase deficiency in congenital methemoglobinemia: a valuable prognostic indicator. Biol Neonate 32: 193-196. (Pubitemid 8265780)
    • (1977) Biology of the Neonate , vol.32 , Issue.3-4 , pp. 193-196
    • Lawson, D.L.1    Miale, T.D.2    Harvey, J.L.3
  • 51
    • 0542376006 scopus 로고    scopus 로고
    • 5 Reductase from Mitochondrial Outer Membrane of Bovine Heart and Turnip
    • Lee JY, Kim YH, Lee SJ. 1998. Purification and comparison of NADHcytochrome b5 reductase from mitochodrial outer membrane of bovin heart and turnip. Korean Biochem J 19: 160-164. (Pubitemid 128480929)
    • (1998) Bulletin of the Korean Chemical Society , vol.19 , Issue.2 , pp. 160-164
    • Lee, J.Y.1    Kim, Y.H.2    Lee, S.J.3
  • 52
    • 0006147301 scopus 로고
    • Purification of NADH-cytochrome b5 reductase from bovin heart mitochodria using surfactant, and the mechanism of external electron transport
    • Lee SJ, Lee JY. 1994. Purification of NADH-cytochrome b5 reductase from bovin heart mitochodria using surfactant, and the mechanism of external electron transport. Korean Biochem J 27: 254-259.
    • (1994) Korean Biochem J , vol.27 , pp. 254-259
    • Lee, S.J.1    Lee, J.Y.2
  • 53
    • 0016797546 scopus 로고
    • Generalised deficiency of cytochrome b5 reductase in congenital methaemoglobinaemia with mental retardation
    • Leroux A, Junien C, Kaplan J, Bamberger J. 1975. Generalised deficiency of cytochrome b5 reductase in congenital methaemoglobinaemia with mental retardation. Nature 258: 619-620.
    • (1975) Nature , vol.258 , pp. 619-620
    • Leroux, A.1    Junien, C.2    Kaplan, J.3    Bamberger, J.4
  • 54
    • 17444362628 scopus 로고    scopus 로고
    • Prenatal diagnosis of recessive congenital methaemoglobinaemia type II: Novel mutation in the NADH-cytochrome b5 reductase gene leading to stop codon read-through
    • DOI 10.1111/j.1600-0609.2004.00388.x
    • Leroux A, Leturcq F, Deburgrave N, Szajnert MF. 2005. Prenatal diagnosis of recessive congenital methaemoglobinaemia type II: novel mutation in the NADH-cytochrome b5 reductase gene leading to stop codon read-through. Eur J Haematol 74: 389-395. (Pubitemid 40545563)
    • (2005) European Journal of Haematology , vol.74 , Issue.5 , pp. 389-395
    • Leroux, A.1    Leturcq, F.2    Deburgrave, N.3    Szajnert, M.-F.4
  • 55
    • 0035871082 scopus 로고    scopus 로고
    • 5 reductase isoenzyme generation in humans
    • DOI 10.1042/0264-6021:3550529
    • Leroux A, Mota Vieira L, Kahn A. 2001. Transcriptional and translational mechanisms of cytochrome b5 reductase isoenzyme generation in humans. Biochem J 355: 529-535. (Pubitemid 32397814)
    • (2001) Biochemical Journal , vol.355 , Issue.2 , pp. 529-535
    • Leroux, A.1    Mota Vieira, L.2    Kahn, A.3
  • 57
    • 0019395644 scopus 로고
    • 5 reductase activity in lymphoid cell lines. Expression of the defect in Epstein-Barr virus transformed lymphoblastoid cell lines from patients with recessive congenital methemoglobinemia
    • Lostanlen D, Lenoir G, Kaplan JC. 1981. NADH cytochrome b5 reductase activity in lymphoid cell lines. Expression of the defect in epstein Barr virus transformed lymphoblastoid cell lines from patients with recessive congenital methemoglobinemia. J Clin Invest 68: 279-285. (Pubitemid 11048100)
    • (1981) Journal of Clinical Investigation , vol.68 , Issue.1 , pp. 279-285
    • Lostanlen, D.1    Lenoir, G.2    Kaplan, J.C.3
  • 59
    • 0029859401 scopus 로고    scopus 로고
    • Two novel mutations in the reduced nicotinamide adenine dinucleotide (NADH)-cytochrome b5 reductase gene of a patient with generalized type, hereditary methemoglobinemia
    • Manabe J, Arya R, Sumimoto H, Yubisui T, Bellingham AJ, Layton DM, Fukumaki Y. 1996. Two novel mutations in the reduced nicotinamide adenine dinucleotide (NADH)-cytochrome b5 reductase gene of a patient with generalized type, hereditary methemoglobinemia. Blood 88: 3208-3215. (Pubitemid 26357406)
    • (1996) Blood , vol.88 , Issue.8 , pp. 3208-3215
    • Manabe, J.-I.1    Arya, R.2    Sumimoto, H.3    Yubisui, T.4    Bellingham, A.J.5    Layton, D.M.6    Fukumaki, Y.7
  • 60
    • 20344364180 scopus 로고    scopus 로고
    • Heterogeneity of the molecular biology of methemoglobinemia: A study of eight consecutive patients
    • Maran J, Guan Y, Ou CN, Prchal JT. 2005. Heterogeneity of the molecular biology of methemoglobinemia: a study of eight consecutive patients. Haematologica 90: 687-689. (Pubitemid 40780889)
    • (2005) Haematologica , vol.90 , Issue.5 , pp. 687-689
    • Maran, J.1    Guan, Y.2    Ou, C.-N.3    Prchal, J.T.4
  • 61
    • 27244462686 scopus 로고    scopus 로고
    • 5 reductase
    • DOI 10.1006/abbi.2001.2340
    • Marohnic CC, Barber MJ. 2001. Arginine 91 is not essential for flavin incorporation in hepatic cytochrome b(5) reductase. Arch Biochem Biophys 389: 223-233. (Pubitemid 32881948)
    • (2001) Archives of Biochemistry and Biophysics , vol.389 , Issue.2 , pp. 223-233
    • Marohnic, C.C.1    Barber, M.J.2
  • 62
    • 0141791270 scopus 로고    scopus 로고
    • 5 reductase
    • DOI 10.1021/bi034819b
    • Marohnic CC, Bewley MC, Barber MJ. 2003. Engineering and characterization of a NADPH-utilizing cytochrome b5 reductase. Biochemistry 42: 11170-11182. (Pubitemid 37158884)
    • (2003) Biochemistry , vol.42 , Issue.38 , pp. 11170-11182
    • Marohnic, C.C.1    Bewley, M.C.2    Barber, M.J.3
  • 63
    • 14044249537 scopus 로고    scopus 로고
    • 5 reductase: Role of the si-face residues, proline 92 and tyrosine 93, in structure and catalysis
    • DOI 10.1021/bi048045q
    • Marohnic CC, Crowley LJ, Davis CA, Smith ET, Barber MJ. 2005. Cytochrome b5 reductase: role of the si-face residues, proline 92 and tyrosine 93, in structure and catalysis. Biochemistry 44: 2449-2461. (Pubitemid 40279548)
    • (2005) Biochemistry , vol.44 , Issue.7 , pp. 2449-2461
    • Marohnic, C.C.1    Crowley, L.J.2    Ainsley Davis, C.3    Smith, E.T.4    Barber, M.J.5
  • 64
    • 0018927492 scopus 로고
    • 5 reductase, an integral membrane protein, in rat liver cells. II. Evidence that a single enzyme accounts for the activity in its various subcellular locations
    • DOI 10.1083/jcb.85.3.516
    • Meldolesi J, Corte G, Pietrini G, Borgese N. 1980. Localization and biosynthesis of NADH-cytochrome b5 reductase, an integral membrane protein, in rat liver cells. II. Evidence that a single enzyme accounts for the activity in its various subcellular locations. J Cell Biol 85: 516-526. (Pubitemid 10007422)
    • (1980) Journal of Cell Biology , vol.85 , Issue.3 , pp. 516-526
    • Meldolesi, J.1    Corte, G.2    Pietrini, G.3    Borgese, N.4
  • 65
    • 0016618618 scopus 로고
    • Purification and properties of the intact form of NADH-cytochrome b5 reductase from rabbit liver microsomes
    • Mihara K, Sato R. 1975. Purification and properties of the intact form of NADH-cytochrome b5 reductase from rabbit liver microsomes. J Biochem 78: 1057-1073.
    • (1975) J Biochem , vol.78 , pp. 1057-1073
    • Mihara, K.1    Sato, R.2
  • 66
    • 0017833009 scopus 로고
    • Detergent-solubilized NADH-cytochrome b5 reductase
    • Mihara K, Sato R. 1978. Detergent-solubilized NADH-cytochrome b5 reductase. Meth Enzymol 52: 102-108.
    • (1978) Meth Enzymol , vol.52 , pp. 102-108
    • Mihara, K.1    Sato, R.2
  • 67
    • 0023664867 scopus 로고
    • Crystallization and preliminary x-ray crystallographic study of NADH-cytochrome b5 reductase from pig liver microsomes
    • Miki K, Kaida S, Kasai N, Iyanagi T, Kobayashi K, Hayashi K. 1987. Crystallization and preliminary x-ray crystallographic study of NADH-cytochrome b5 reductase from pig liver microsomes. J Biol Chem 262: 11801-11802.
    • (1987) J Biol Chem , vol.262 , pp. 11801-11802
    • Miki, K.1    Kaida, S.2    Kasai, N.3    Iyanagi, T.4    Kobayashi, K.5    Hayashi, K.6
  • 69
    • 77957947581 scopus 로고    scopus 로고
    • Secretory expression and purification of a soluble NADH cytochrome b5 reductase enzyme from Mucor racemosus in Pichia pastoris based on codon usage adaptation
    • Mirzaei SA, Yazdi MT, Sepehrizadeh Z. 2010. Secretory expression and purification of a soluble NADH cytochrome b5 reductase enzyme from Mucor racemosus in Pichia pastoris based on codon usage adaptation. Biotechnol Lett 32: 1705-1711.
    • (2010) Biotechnol Lett , vol.32 , pp. 1705-1711
    • Mirzaei, S.A.1    Yazdi, M.T.2    Sepehrizadeh, Z.3
  • 70
    • 0016750366 scopus 로고
    • Alpha reduced nicotinamide adenine dinucleotide-dependent reductase reactions of rat liver microsomes
    • Miyake Y, Nakamura Y, Takayama N, Horiike K. 1975. Alpha reduced nicotinamide adenine dinucleotide-dependent reductase reactions of rat liver microsomes. J Biochem 78: 773-783.
    • (1975) J Biochem , vol.78 , pp. 773-783
    • Miyake, Y.1    Nakamura, Y.2    Takayama, N.3    Horiike, K.4
  • 71
    • 0037376527 scopus 로고    scopus 로고
    • 5 support the CYP2E1-mediated activation of nitrosamines in a recombinant Ames test
    • DOI 10.1016/S0003-9861(03)00040-7
    • Mokashi V, Li L, Porter TD. 2003. Cytochrome b5 reductase and cytochrome b5 support the CYP2E1-mediated activation of nitrosamines in a recombinant Ames test. Arch Biochem Biophys 412: 147-152. (Pubitemid 36324375)
    • (2003) Archives of Biochemistry and Biophysics , vol.412 , Issue.1 , pp. 147-152
    • Mokashi, V.1    Li, L.2    Porter, T.D.3
  • 72
    • 0028904457 scopus 로고
    • Specific arrangement of three amino acid residues for flavin-binding barrel structures in NADH-cytochrome b5 reductase and the other flavin-dependent reductases
    • Nishida H, Inaka K, Miki K. 1995. Specific arrangement of three amino acid residues for flavin-binding barrel structures in NADH-cytochrome b5 reductase and the other flavin-dependent reductases. FEBS Lett 361: 97-100.
    • (1995) FEBS Lett , vol.361 , pp. 97-100
    • Nishida, H.1    Inaka, K.2    Miki, K.3
  • 73
    • 0022592789 scopus 로고
    • NADH dehydrogenase from bovine neutrophil membranes: Purification and properties
    • Nisimoto Y, Wilson E, Heyl BL, Lambeth JD. 1986. NADH dehydrogenase from bovine neutrophil membranes. Purification and properties. J Biol Chem 261: 285-290. (Pubitemid 16102881)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.1 , pp. 285-290
    • Nisimoto, Y.1    Wilson, E.2    Heyl, B.L.3    Lambeth, J.D.4
  • 74
    • 33750956721 scopus 로고    scopus 로고
    • A novel mutation of the cytochrome-b5 reductase gene in an Indian patient: The molecular basis of type I methemoglobinemia
    • Nussenzveig RH, Lingam HB, Gaikwad A, Zhu Q, Jing N, Prchal JT. 2006. A novel mutation of the cytochrome-b5 reductase gene in an Indian patient: the molecular basis of type I methemoglobinemia. Haematologica 91: 1542-1545. (Pubitemid 44736122)
    • (2006) Haematologica , vol.91 , Issue.11 , pp. 1542-1545
    • Nussenzveig, R.H.1    Lingam, H.B.2    Gaikwad, A.3    Zhu, Q.4    Jing, N.5    Prchal, J.T.6
  • 75
    • 4344704702 scopus 로고    scopus 로고
    • Structure determination of membrane proteins by NMR spectroscopy
    • Opella SJ, Marassi FM. 2004. Structure determination of membrane proteins by NMR spectroscopy. Chem Rev 104: 3587-3606.
    • (2004) Chem Rev , vol.104 , pp. 3587-3606
    • Opella, S.J.1    Marassi, F.M.2
  • 76
    • 53649098157 scopus 로고    scopus 로고
    • NADH-cytochrome b5 reductase in a Turkish family with recessive congenital methaemoglobinaemia type I
    • Percy MJ, Aslan D. 2008. NADH-cytochrome b5 reductase in a Turkish family with recessive congenital methaemoglobinaemia type I. J Clin Pathol 61: 1122-1123.
    • (2008) J Clin Pathol , vol.61 , pp. 1122-1123
    • Percy, M.J.1    Aslan, D.2
  • 78
    • 10444260491 scopus 로고    scopus 로고
    • Disorders of oxidised haemoglobin
    • DOI 10.1016/j.blre.2004.02.001, PII S0268960X0400013X
    • Percy MJ, McFerran NV, Lappin TR. 2005b. Disorders of oxidised haemoglobin. Blood Rev 19: 61-68. (Pubitemid 39643112)
    • (2005) Blood Reviews , vol.19 , Issue.2 , pp. 61-68
    • Percy, M.J.1    McFerran, N.V.2    Lappin, T.R.J.3
  • 79
    • 33644622143 scopus 로고    scopus 로고
    • Expression of a novel P275L variant of NADH:Cytochrome b5 reductase gives functional insight into the conserved motif important for pyridine nucleotide binding
    • Percy MJ, Crowley LJ, Boudreaux J, Barber MJ. 2006a. Expression of a novel P275L variant of NADH:cytochrome b5 reductase gives functional insight into the conserved motif important for pyridine nucleotide binding. Arch Biochem Biophys 447: 59-67.
    • (2006) Arch Biochem Biophys , vol.447 , pp. 59-67
    • Percy, M.J.1    Crowley, L.J.2    Boudreaux, J.3    Barber, M.J.4
  • 80
    • 30344481133 scopus 로고    scopus 로고
    • 5 reductase: An aid to determine recessive congenital methemoglobinemia status in an infant
    • DOI 10.1016/j.bcmd.2005.10.001, PII S1079979605001531
    • Percy MJ, Crowley LJ, Roper D, Vulliamy TJ, Layton DM, Barber MJ. 2006b. Identification and characterization of the novel FAD-binding lobe G75S mutation in cytochrome b(5) reductase: an aid to determine recessive congenital methemoglobinemia status in an infant. Blood Cells Mol Dis 36: 81-90. (Pubitemid 43061491)
    • (2006) Blood Cells, Molecules, and Diseases , vol.36 , Issue.1 , pp. 81-90
    • Percy, M.J.1    Crowley, L.J.2    Roper, D.3    Vulliamy, T.J.4    Layton, D.M.5    Barber, M.J.6
  • 81
    • 0037111659 scopus 로고    scopus 로고
    • Familial idiopathic methemoglobinemia revisited: Original cases reveal 2 novel mutations in NADH-cytochrome b5 reductase
    • DOI 10.1182/blood-2002-05-1405
    • Percy MJ, Gillespie MJ, Savage G, Hughes AE, McMullin MF, Lappin TR. 2002. Familial idiopathic methemoglobinemia revisited: original cases reveal 2 novel mutations in NADH-cytochrome b5 reductase. Blood 100: 3447-3449. (Pubitemid 35303908)
    • (2002) Blood , vol.100 , Issue.10 , pp. 3447-3449
    • Percy, M.J.1    Gillespie, M.J.S.2    Savage, G.3    Hughes, A.E.4    McMullin, M.F.5    Lappin, T.R.J.6
  • 82
    • 42049097088 scopus 로고    scopus 로고
    • 5 reductase deficiency
    • DOI 10.1111/j.1365-2141.2008.07017.x
    • Percy MJ, Lappin TR. 2008. Recessive congenital methaemoglobinaemia: cytochrome b(5) reductase deficiency. Br J Haematol 141: 298-308. (Pubitemid 351521146)
    • (2008) British Journal of Haematology , vol.141 , Issue.3 , pp. 298-308
    • Percy, M.J.1    Lappin, T.R.2
  • 83
  • 84
    • 79957869781 scopus 로고    scopus 로고
    • Individual variability in the detoxification of carcinogenic arylhydroxylamines in human breast
    • Rhoads K, Sacco JC, Drescher N, Wong A, Trepanier LA. 2011. Individual variability in the detoxification of carcinogenic arylhydroxylamines in human breast. Toxicol Sci 121: 245-256.
    • (2011) Toxicol Sci , vol.121 , pp. 245-256
    • Rhoads, K.1    Sacco, J.C.2    Drescher, N.3    Wong, A.4    Trepanier, L.A.5
  • 85
    • 33746284936 scopus 로고    scopus 로고
    • 5 reductase
    • DOI 10.1016/j.abb.2006.04.021, PII S0003986106001676
    • Roma GW, Crowley LJ, Barber MJ. 2006. Expression and characterization of a functional canine variant of cytochrome b5 reductase. Arch Biochem Biophys 452: 69-82. (Pubitemid 44107330)
    • (2006) Archives of Biochemistry and Biophysics , vol.452 , Issue.1 , pp. 69-82
    • Roma, G.W.1    Crowley, L.J.2    Barber, M.J.3
  • 86
    • 26644470345 scopus 로고    scopus 로고
    • 5 reductase
    • DOI 10.1021/bi051165t
    • Roma GW, Crowley LJ, Davis CA, Barber MJ. 2005. Mutagenesis of Glycine 179 modulates both catalytic efficiency and reduced pyridine nucleotide specificity in cytochrome b5 reductase. Biochemistry 44: 13467-13476. (Pubitemid 41443674)
    • (2005) Biochemistry , vol.44 , Issue.41 , pp. 13467-13476
    • Roma, G.W.1    Crowley, L.J.2    Davis, C.A.3    Barber, M.J.4
  • 87
    • 73949092712 scopus 로고    scopus 로고
    • Cytochrome b5 and NADH cytochrome b5 reductase: Genotype-phenotype correlations for hydroxylamine reduction
    • Sacco JC, Trepanier LA. 2010. Cytochrome b5 and NADH cytochrome b5 reductase: genotype-phenotype correlations for hydroxylamine reduction. Pharmacogenet Genomics 20: 26-37.
    • (2010) Pharmacogenet Genomics , vol.20 , pp. 26-37
    • Sacco, J.C.1    Trepanier, L.A.2
  • 88
    • 0032881906 scopus 로고    scopus 로고
    • Identification of an NADH-cytochrome b(5) reductase gene from an arachidonic acidproducing fungus, Mortierella alpina 1S-4, by sequencing of the encoding cDNA and heterologous expression in a fungus, Aspergillus oryzae
    • Sakuradani E, Kobayashi M, Shimizu S. 1999. Identification of an NADH-cytochrome b(5) reductase gene from an arachidonic acidproducing fungus, Mortierella alpina 1S-4, by sequencing of the encoding cDNA and heterologous expression in a fungus, Aspergillus oryzae. Appl Environ Microbiol 65: 3873-3879.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 3873-3879
    • Sakuradani, E.1    Kobayashi, M.2    Shimizu, S.3
  • 89
    • 84855560688 scopus 로고    scopus 로고
    • Colon cancer chemopreventive efficacy of silibinin through perturbation of xenobiotic metabolizing enzymes in experimental rats
    • Sangeetha N, Viswanathan P, Balasubramanian T, Nalini N. 2012. Colon cancer chemopreventive efficacy of silibinin through perturbation of xenobiotic metabolizing enzymes in experimental rats. Eur J Pharmacol 674: 430-438.
    • (2012) Eur J Pharmacol , vol.674 , pp. 430-438
    • Sangeetha, N.1    Viswanathan, P.2    Balasubramanian, T.3    Nalini, N.4
  • 90
    • 0000614928 scopus 로고
    • The enzymic defect of hereditary methemoglobinemia: Diaphorase
    • Scott EM, Griffith IV. 1959. The enzymic defect of hereditary methemoglobinemia: diaphorase. Biochim Biophys Acta 34: 584-586.
    • (1959) Biochim Biophys Acta , vol.34 , pp. 584-586
    • Scott, E.M.1    Griffith, I.V.2
  • 91
    • 74549198889 scopus 로고    scopus 로고
    • Cloning, molecular characterization and expression of a cDNA encoding a functional NADH-cytochrome b5 reductase from mucor racemosus PTCC 5305 in E. Coli
    • Setayesh N, Sepehrizadeh Z, Jaberi E, Yazdi MT. 2009. Cloning, molecular characterization and expression of a cDNA encoding a functional NADH-cytochrome b5 reductase from Mucor racemosus PTCC 5305 in E. coli. Biol Res 42: 137-146.
    • (2009) Biol Res , vol.42 , pp. 137-146
    • Setayesh, N.1    Sepehrizadeh, Z.2    Jaberi, E.3    Yazdi, M.T.4
  • 92
    • 0030624098 scopus 로고    scopus 로고
    • Screening of novel microbial enzymes for the production of biologically and chemically useful compounds
    • Shimizu S, Ogawa J, Kataoka M, Kobayashi M. 1997. Screening of novel microbial enzymes for the production of biologically and chemically useful compounds. Adv Biochem Eng Biotechnol 58: 45-87.
    • (1997) Adv Biochem Eng Biotechnol , vol.58 , pp. 45-87
    • Shimizu, S.1    Ogawa, J.2    Kataoka, M.3    Kobayashi, M.4
  • 93
    • 0028022999 scopus 로고
    • An in-frame deletion of codon 298 of the NADH-cytochrome b5 reductase gene results in hereditary methemoglobinemia type II (generalized type). A functional implication for the role of the COOH-terminal region of the enzyme
    • Shirabe K, Fujimoto Y, Yubisui T, Takeshita M. 1994. An in-frame deletion of codon 298 of the NADH-cytochrome b5 reductase gene results in hereditary methemoglobinemia type II (generalized type). A functional implication for the role of the COOH-terminal region of the enzyme. J Biol Chem 269: 5952-5957.
    • (1994) J Biol Chem , vol.269 , pp. 5952-5957
    • Shirabe, K.1    Fujimoto, Y.2    Yubisui, T.3    Takeshita, M.4
  • 94
    • 0029013274 scopus 로고
    • A novel point mutation in a 3' splice site of the NADHcytochrome b5 reductase gene results in immunologically undetectable enzyme and impaired NADH-dependent ascorbate regeneration in cultured fibroblasts of a patient with type II hereditary methemoglobinemia
    • Shirabe K, Landi MT, Takeshita M, Uziel G, Fedrizzi E, Borgese N. 1995. A novel point mutation in a 3' splice site of the NADHcytochrome b5 reductase gene results in immunologically undetectable enzyme and impaired NADH-dependent ascorbate regeneration in cultured fibroblasts of a patient with type II hereditary methemoglobinemia. Am J Hum Genet 57: 302-310.
    • (1995) Am J Hum Genet , vol.57 , pp. 302-310
    • Shirabe, K.1    Landi, M.T.2    Takeshita, M.3    Uziel, G.4    Fedrizzi, E.5    Borgese, N.6
  • 96
    • 0026722825 scopus 로고
    • Enzymatic instability of NADH-cytochrome b5 reductase as a cause of hereditary methemoglobinemia type I (red cell type)
    • Shirabe K, Yubisui T, Borgese N, Tang CY, Hultquist DE, Takeshita M. 1992. Enzymatic instability of NADH-cytochrome b5 reductase as a cause of hereditary methemoglobinemia type I (red cell type). J Biol Chem 267: 20416-20421.
    • (1992) J Biol Chem , vol.267 , pp. 20416-20421
    • Shirabe, K.1    Yubisui, T.2    Borgese, N.3    Tang, C.Y.4    Hultquist, D.E.5    Takeshita, M.6
  • 97
  • 98
    • 21444460435 scopus 로고    scopus 로고
    • 5 reductase from developing seeds of tung (Vernicia fordii)
    • DOI 10.1016/j.plantsci.2005.03.023, PII S0168945205001184
    • Shockey JM, Dhanoa PK, Dupuy T, Chapital DC, Mullen RT, Dyer MA. 2005. Cloning, functional analysis, and subcellular localization of two isoforms of NADH:cytochrome b5 reductase from developing seeds of tung (Vernicia fordii). Plant Sci 169: 375-385. (Pubitemid 40912388)
    • (2005) Plant Science , vol.169 , Issue.2 , pp. 375-385
    • Shockey, J.M.1    Dhanoa, P.K.2    Dupuy, T.3    Chapital, D.C.4    Mullen, R.T.5    Dyer, J.M.6
  • 99
    • 79954436898 scopus 로고    scopus 로고
    • Cytochrome b5 reductase-cytochrome b5 as an active P450 redox enzyme system in Phanerochaete chrysosporium: Atypical properties and in vivo evidence of electron transfer capability to CYP63A2
    • Syed K, Kattamuri C, Thompson TB, Yadav JS. 2011. Cytochrome b5 reductase-cytochrome b5 as an active P450 redox enzyme system in Phanerochaete chrysosporium: atypical properties and in vivo evidence of electron transfer capability to CYP63A2. Arch Biochem Biophys 509: 26-32.
    • (2011) Arch Biochem Biophys , vol.509 , pp. 26-32
    • Syed, K.1    Kattamuri, C.2    Thompson, T.B.3    Yadav, J.S.4
  • 100
    • 0014742071 scopus 로고
    • Purification and properties of NADHcytochrome b5 reductase solubilized by lysosomes from rat liver microsomes
    • Takesue S, Omura T. 1970. Purification and properties of NADHcytochrome b5 reductase solubilized by lysosomes from rat liver microsomes. J Biochem 67: 267-276.
    • (1970) J Biochem , vol.67 , pp. 267-276
    • Takesue, S.1    Omura, T.2
  • 101
    • 0020851704 scopus 로고
    • Microsomal NADH-cytochrome b5 reductase of bovine brain: Purification and properties
    • Tamura M, Yubisui T, Takeshita M. 1983. Microsomal NADH-cytochrome b5 reductase of bovine brain: purification and properties. J Biochem 94: 1547-1555.
    • (1983) J Biochem , vol.94 , pp. 1547-1555
    • Tamura, M.1    Yubisui, T.2    Takeshita, M.3
  • 102
    • 0023335410 scopus 로고
    • Structural comparison of bovine erythrocyte, brain, and liver NADH-cytochrome b5 reductase by HPLC mapping
    • Tamura M, Yubisui T, Takeshita M, Kawabata S, Miyata T, Iwanaga S. 1987. Structural comparison of bovine erythrocyte, brain, and liver NADH-cytochrome b5 reductase by HPLC mapping. J Biochem 101: 1147-1159.
    • (1987) J Biochem , vol.101 , pp. 1147-1159
    • Tamura, M.1    Yubisui, T.2    Takeshita, M.3    Kawabata, S.4    Miyata, T.5    Iwanaga, S.6
  • 103
    • 0021930926 scopus 로고
    • 5 reductase
    • Tauber AI, Wright J, Higson FK, Edelman SA, Waxman DJ. 1985. Purification and characterization of the human neutrophil NADHcytochrome b5 reductase. Blood 66: 673-678. (Pubitemid 15230775)
    • (1985) Blood , vol.66 , Issue.3 , pp. 673-678
    • Tauber, A.I.1    Wright, J.2    Higson, F.K.3
  • 105
    • 0028966277 scopus 로고
    • Four new mutations in the NADH-cytochrome b5 reductase gene from patients with recessive congenital methemoglobinemia type II
    • Vieira LM, Kaplan JC, Kahn A, Leroux A. 1995. Four new mutations in the NADH-cytochrome b5 reductase gene from patients with recessive congenital methemoglobinemia type II. Blood 85: 2254-2262.
    • (1995) Blood , vol.85 , pp. 2254-2262
    • Vieira, L.M.1    Kaplan, J.C.2    Kahn, A.3    Leroux, A.4
  • 106
    • 0034658052 scopus 로고    scopus 로고
    • A novel mutation in the NADH-cytochrome b5 reductase gene of a Chinese patient with recessive congenital methemoglobinemia
    • Wang Y, Wu YS, Zheng PZ, Yang WX, Fang GA, Tang YC, Xie F, Lan FH, Zhu ZY. 2000. A novel mutation in the NADH-cytochrome b5 reductase gene of a Chinese patient with recessive congenital methemoglobinemia. Blood 95: 3250-3255. (Pubitemid 30321181)
    • (2000) Blood , vol.95 , Issue.10 , pp. 3250-3255
    • Wang, Y.1    Wu, Y.-S.2    Zheng, P.-Z.3    Yang, W.-X.4    Fang, G.-A.5    Tang, Y.-C.6    Xie, F.7    Lan, F.-H.8    Zhu, Z.-Y.9
  • 107
    • 0032034708 scopus 로고    scopus 로고
    • Leu 72 Pro mutation in the NADH cytochrome b5 reductase gene found in a Chinese hereditary methemoglobinemia patient
    • Wu Y, Huang C, Zhu Z. 1998. [Leu 72 Pro mutation in the NADH cytochrome b5 reductase gene found in a Chinese hereditary methemoglobinemia patient]. Zhonghua Xue Ye Xue Za Zhi 19: 195-197.
    • (1998) Zhonghua Xue Ye Xue Za Zhi , vol.19 , pp. 195-197
    • Wu, Y.1    Huang, C.2    Zhu, Z.3
  • 109
    • 50249086103 scopus 로고    scopus 로고
    • Establishment of a cellular model with human NADH-cytochrome b5 reductase deficiency via RNA interference
    • Zhuang Y, Wang S, Lan F. 2008. [Establishment of a cellular model with human NADH-cytochrome b5 reductase deficiency via RNA interference]. Zhonghua Yi Xue Yi Chuan Xue Za Zhi 25: 400-405.
    • (2008) Zhonghua Yi Xue Yi Chuan Xue Za Zhi , vol.25 , pp. 400-405
    • Zhuang, Y.1    Wang, S.2    Lan, F.3


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