메뉴 건너뛰기




Volumn 20, Issue 3, 2010, Pages 532-541

Biochemical and cellular investigation of vitreoscilla hemoglobin (VHb) variants possessing efficient peroxidase activity

Author keywords

Catalytic constant; Enzyme kinetics; Iron superoxide dismutase; Peroxidase like activity; Proteomic analysis; Vitreoscilla hemoglobin

Indexed keywords

ARGININE; CARBON MONOXIDE; FERRIC ION; FERRIC UPTAKE REGULATOR; FERROUS ION; HEME; HEMOGLOBIN; HISTIDINE; HYDROGEN PEROXIDE; IRON; IRON SUPEROXIDE DISMUTASE; PEROXIDASE; PROLINE;

EID: 77954279964     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (8)

References (50)
  • 1
    • 37049078774 scopus 로고
    • 2 by MP-8 using 2,2-azinobis- (3-ethylbenzothiazoline-6-sulphonate) (ABTS) as reducing substrate
    • 2 by MP-8 using 2,2-azinobis- (3-ethylbenzothiazoline-6-sulphonate) (ABTS) as reducing substrate. J. Chem. Soc. Perkin Trans. 2: 1407-1414.
    • (1990) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 1407-1414
    • Adams, P.A.1
  • 2
    • 0027298810 scopus 로고
    • Structural and functional characterization of sperm whale myoglobin mutants: Role of arginine (E10) in ligand stabilization
    • Allocatelli, C. T., F. Cutruzzola, A. Brancaccio, M. Brunori, J. Qin, and G. N. La Mar. 1993. Structural and functional characterization of sperm whale myoglobin mutants: Role of arginine (E10) in ligand stabilization. Biochemistry 32: 6041-6049.
    • (1993) Biochemistry , vol.32 , pp. 6041-6049
    • Allocatelli, C.T.1    Cutruzzola, F.2    Brancaccio, A.3    Brunori, M.4    Qin, J.5    la Mar, G.N.6
  • 3
    • 0141789646 scopus 로고    scopus 로고
    • Enhanced ribosome and tRNA contents in Escherichia coli expressing a truncated Vitreoscilla hemoglobin mutant analyzed by flow field-flow fractionation
    • Andersson, C. I., C. Arfvidsson, P. T. Kallio, K. G. Wahlund, and L. Bulow. 2003. Enhanced ribosome and tRNA contents in Escherichia coli expressing a truncated Vitreoscilla hemoglobin mutant analyzed by flow field-flow fractionation. Biotechnol. Lett. 25: 1499-1504.
    • (2003) Biotechnol. Lett. , vol.25 , pp. 1499-1504
    • Andersson, C.I.1    Arfvidsson, C.2    Kallio, P.T.3    Wahlund, K.G.4    Bulow, L.5
  • 4
    • 0028671076 scopus 로고    scopus 로고
    • Removal of phenol from coupling of talc and peroxidase: Application for depollution of waste water containing phenolic compounds
    • Arseguel, D. and M. Baboulne. 2004. Removal of phenol from coupling of talc and peroxidase: Application for depollution of waste water containing phenolic compounds. J. Chem. Technol. Biotechnol. 61: 331-335.
    • (2004) J. Chem. Technol. Biotechnol. , vol.61 , pp. 331-335
    • Arseguel, D.1    Baboulne, M.2
  • 5
    • 0024533263 scopus 로고
    • pH effects on the haem iron co-ordination state in the nitric oxide and deoxy derivatives of ferrous horseradish peroxidase and cytochrome c peroxidase
    • Ascenzi, P., M. Brunori, M. Coletta, and A. Desideri. 1989. pH effects on the haem iron co-ordination state in the nitric oxide and deoxy derivatives of ferrous horseradish peroxidase and cytochrome c peroxidase. Biochem. J. 258: 473-478.
    • (1989) Biochem. J. , vol.258 , pp. 473-478
    • Ascenzi, P.1    Brunori, M.2    Coletta, M.3    Desideri, A.4
  • 6
    • 34047156098 scopus 로고    scopus 로고
    • A proline to glycine mutation in the Lck SH3-domain affects conformational sampling and increases ligand binding affinity
    • Bauer, F. and H. Sticht. 2007. A proline to glycine mutation in the Lck SH3-domain affects conformational sampling and increases ligand binding affinity. FEBS Lett. 581: 1555-1560.
    • (2007) FEBS Lett , vol.581 , pp. 1555-1560
    • Bauer, F.1    Sticht, H.2
  • 7
    • 0000101292 scopus 로고
    • Biosynthesis of the tetrapyrrole pigment precursor, delta-aminolevulinic acid, from glutamate
    • Beale, S. I. 1990. Biosynthesis of the tetrapyrrole pigment precursor, delta-aminolevulinic acid, from glutamate. Plant Physiol. 93: 1273-1279.
    • (1990) Plant Physiol , vol.93 , pp. 1273-1279
    • Beale, S.I.1
  • 9
    • 33947587599 scopus 로고    scopus 로고
    • Elimination of 4-chlorophenol by soybean peroxidase and hydrogen peroxide: Kinetic model and intrinsic parameters
    • Bodalo, A., J. L. Gomez, E. Gomez, A. M. Hidalgo, M. Gomez, and A. M. Yelo. 2007. Elimination of 4-chlorophenol by soybean peroxidase and hydrogen peroxide: Kinetic model and intrinsic parameters. Biochem. Eng. J. 34: 242-247.
    • (2007) Biochem. Eng. J. , vol.34 , pp. 242-247
    • Bodalo, A.1    Gomez, J.L.2    Gomez, E.3    Hidalgo, A.M.4    Gomez, M.5    Yelo, A.M.6
  • 10
    • 0033588328 scopus 로고    scopus 로고
    • Anticooperative ligand binding properties of recombinant ferric Vitreoscilla homodimeric hemoglobin: A thermodynamic, kinetic and X-ray crystallographic study
    • Bolognesi, M., A. Boffi, M. Coletta, A. Mozzarelli, A. Pesce, C. Tarricone, and P. Ascenzi. 1999. Anticooperative ligand binding properties of recombinant ferric Vitreoscilla homodimeric hemoglobin: A thermodynamic, kinetic and X-ray crystallographic study. J. Mol. Biol. 291: 637-650.
    • (1999) J. Mol. Biol. , vol.291 , pp. 637-650
    • Bolognesi, M.1    Boffi, A.2    Coletta, M.3    Mozzarelli, A.4    Pesce, A.5    Tarricone, C.6    Ascenzi, P.7
  • 11
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 13
    • 0036148389 scopus 로고    scopus 로고
    • Fur-mediated transcriptional and post-transcriptional regulation of FeSOD expression in Escherichia coli
    • Dubrac, S. and D. Touati. 2002. Fur-mediated transcriptional and post-transcriptional regulation of FeSOD expression in Escherichia coli. Microbiology 148: 147-156.
    • (2002) Microbiology , vol.148 , pp. 147-156
    • Dubrac, S.1    Touati, D.2
  • 14
    • 1242341363 scopus 로고    scopus 로고
    • Direct electrochemical characterization of Vitreoscilla sp. hemoglobin entrapped in organic films
    • Fan, C., J. Zhong, R. Guan, and G. Li. 2003. Direct electrochemical characterization of Vitreoscilla sp. hemoglobin entrapped in organic films. Biochim. Biophys. Acta 1649: 123-126.
    • (2003) Biochim. Biophys. Acta. , vol.1649 , pp. 123-126
    • Fan, C.1    Zhong, J.2    Guan, R.3    Li, G.4
  • 15
    • 0036010276 scopus 로고    scopus 로고
    • Improved cell growth in tobacco suspension cultures expressing Vitreoscilla hemoglobin
    • Farres, J. and P. T. Kallio. 2002. Improved cell growth in tobacco suspension cultures expressing Vitreoscilla hemoglobin. Biotechnol. Prog. 18: 229-233.
    • (2002) Biotechnol. Prog. , vol.18 , pp. 229-233
    • Farres, J.1    Kallio, P.T.2
  • 16
    • 0025986138 scopus 로고
    • Regulation of sod genes in Escherichia coli: Relevance to superoxide dismutase function
    • Fee, J. A. 1991. Regulation of sod genes in Escherichia coli: Relevance to superoxide dismutase function. Mol. Microbiol. 5: 2599-2610.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2599-2610
    • Fee, J.A.1
  • 17
    • 0021723457 scopus 로고
    • Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution
    • Finzel, B. C., T. L. Poulos, and J. Kraut. 1984. Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution. J. Biol. Chem. 259: 13027-13036.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13027-13036
    • Finzel, B.C.1    Poulos, T.L.2    Kraut, J.3
  • 18
    • 10644248642 scopus 로고    scopus 로고
    • Expression of Vitreoscilla haemoglobin in tobacco cell cultures relieves nitrosative stress in vivo and protects from NO in vitro
    • Frey, A. D., B. T. Oberle, J. Farres, and P. T. Kallio. 2004. Expression of Vitreoscilla haemoglobin in tobacco cell cultures relieves nitrosative stress in vivo and protects from NO in vitro. Plant Biotechnol. J. 2: 221-231.
    • (2004) Plant Biotechnol. J. , vol.2 , pp. 221-231
    • Frey, A.D.1    Oberle, B.T.2    Farres, J.3    Kallio, P.T.4
  • 19
    • 0041706293 scopus 로고    scopus 로고
    • Genetic engineering of Enterobacter aerogenes with the Vitreoscilla hemoglobin gene: Cell growth, survival, and antioxidant enzyme status under oxidative stress
    • Geckil, H., S. Gencer, H. Kahraman, and S. O. Erenler. 2003. Genetic engineering of Enterobacter aerogenes with the Vitreoscilla hemoglobin gene: Cell growth, survival, and antioxidant enzyme status under oxidative stress. Res. Microbiol. 154: 425-431.
    • (2003) Res. Microbiol. , vol.154 , pp. 425-431
    • Geckil, H.1    Gencer, S.2    Kahraman, H.3    Erenler, S.O.4
  • 20
    • 0006563646 scopus 로고
    • The chemical nature of the second hydrogen peroxide compound formed by cytochrome c peroxidase and horseradish peroxidase
    • George, P. 1953. The chemical nature of the second hydrogen peroxide compound formed by cytochrome c peroxidase and horseradish peroxidase. I. Titration with reducing agents. Biochem. J. 54: 267-276.
    • (1953) I. Titration with Reducing Agents. Biochem. J. , vol.54 , pp. 267-276
    • George, P.1
  • 22
    • 0036135136 scopus 로고    scopus 로고
    • Chimeric Vitreoscilla hemoglobin (VHb) carrying a flavoreductase domain relieves nitrosative stress in Escherichia coli: New insight into the functional role of VHb
    • Kaur, R., R. Pathania, V. Sharma, S. C. Mande, and K. L. Dikshit. 2002. Chimeric Vitreoscilla hemoglobin (VHb) carrying a flavoreductase domain relieves nitrosative stress in Escherichia coli: New insight into the functional role of VHb. Appl. Environ. Microbiol. 68: 152-160.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 152-160
    • Kaur, R.1    Pathania, R.2    Sharma, V.3    Mande, S.C.4    Dikshit, K.L.5
  • 23
    • 0023874286 scopus 로고
    • Heterologous expression of a bacterial haemoglobin improves the growth properties of recombinant Escherichia coli
    • Khosla, C. and J. E. Bailey. 1988. Heterologous expression of a bacterial haemoglobin improves the growth properties of recombinant Escherichia coli. Nature 331: 633-635.
    • (1988) Nature , vol.331 , pp. 633-635
    • Khosla, C.1    Bailey, J.E.2
  • 24
    • 11944257747 scopus 로고
    • Expression of intracellular hemoglobin improves protein synthesis in oxygen-limited Escherichia coli
    • Khosla, C., J. E. Curtis, J. DeModena, U. Rinas, and J. E. Bailey. 1990. Expression of intracellular hemoglobin improves protein synthesis in oxygen-limited Escherichia coli. Biotechnology (NY) 8: 849-853.
    • (1990) Biotechnology (NY) , vol.8 , pp. 849-853
    • Khosla, C.1    Curtis, J.E.2    Demodena, J.3    Rinas, U.4    Bailey, J.E.5
  • 25
    • 34147115160 scopus 로고    scopus 로고
    • An investigation of the peroxidase activity of Vitreoscilla hemoglobin
    • Kvist, M., E. S. Ryabova, E. Nordlander, and L. Bulow. 2007. An investigation of the peroxidase activity of Vitreoscilla hemoglobin. J. Biol. Inorg. Chem. 12: 324-334.
    • (2007) J. Biol. Inorg. Chem. , vol.12 , pp. 324-334
    • Kvist, M.1    Ryabova, E.S.2    Nordlander, E.3    Bulow, L.4
  • 26
    • 17444391245 scopus 로고    scopus 로고
    • Horseradish peroxidasemediated aerobic and anaerobic oxidations of 3-alkylindoles
    • Ling, K. Q. and L. M. Sayre. 2005. Horseradish peroxidasemediated aerobic and anaerobic oxidations of 3-alkylindoles. Bioorg. Med. Chem. 13: 3543-3551.
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 3543-3551
    • Ling, K.Q.1    Sayre, L.M.2
  • 27
    • 0016236836 scopus 로고
    • Spectral characteristics and interconversions of the reduced oxidized and oxygenated forms of purified cytochrome o
    • Liu, C. Y. and D. A. Webster. 1974. Spectral characteristics and interconversions of the reduced oxidized and oxygenated forms of purified cytochrome o. J. Biol. Chem. 249: 4261-4266.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4261-4266
    • Liu, C.Y.1    Webster, D.A.2
  • 28
    • 0033613928 scopus 로고    scopus 로고
    • Effects of the location of distal histidine in the reaction of myoglobin with hydrogen peroxide
    • Matsui, T., S. Ozaki, E. Liong, G. N. Phillips Jr., and Y. Watanabe. 1999. Effects of the location of distal histidine in the reaction of myoglobin with hydrogen peroxide. J. Biol. Chem. 274: 2838-2844.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2838-2844
    • Matsui, T.1    Ozaki, S.2    Liong, E.3    Phillips Jr., G.N.4    Watanabe, Y.5
  • 30
    • 3242735024 scopus 로고    scopus 로고
    • Hydrogenperoxide- induced heme degradation in red blood cells: The protective roles of catalase and glutathione peroxidase
    • Nagababu, E., F. J. Chrest, and J. M. Rifkind. 2003. Hydrogenperoxide- induced heme degradation in red blood cells: The protective roles of catalase and glutathione peroxidase. Biochim. Biophys. Acta 1620: 211-217.
    • (2003) Biochim. Biophys. Acta. , vol.1620 , pp. 211-217
    • Nagababu, E.1    Chrest, F.J.2    Rifkind, J.M.3
  • 31
    • 0034647775 scopus 로고    scopus 로고
    • Heme degradation during autoxidation of oxyhemoglobin
    • Nagababu, E. and J. M. Rifkind. 2000. Heme degradation during autoxidation of oxyhemoglobin. Biochem. Biophys. Res. Commun. 273: 839-845.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 839-845
    • Nagababu, E.1    Rifkind, J.M.2
  • 32
    • 0034633998 scopus 로고    scopus 로고
    • Reaction of hydrogen peroxide with ferrylhemoglobin: Superoxide production and heme degradation
    • Nagababu, E. and J. M. Rifkind. 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    Rifkind, J.M.2
  • 33
    • 33847168011 scopus 로고    scopus 로고
    • Removal of dinitrotoluenes from water via reduction with iron and peroxidase-catalyzed oxidative polymerization: A comparison between Arthromyces ramosus peroxidase and soybean peroxidase
    • Patapas, J., M. M. Al-Ansari, K. E. Taylor, J. K. Bewtra, and N. Biswas. 2007. Removal of dinitrotoluenes from water via reduction with iron and peroxidase-catalyzed oxidative polymerization: A comparison between Arthromyces ramosus peroxidase and soybean peroxidase. Chemosphere 67: 1485-1491.
    • (2007) Chemosphere , vol.67 , pp. 1485-1491
    • Patapas, J.1    Al-Ansari, M.M.2    Taylor, K.E.3    Bewtra, J.K.4    Biswas, N.5
  • 35
    • 0030068091 scopus 로고    scopus 로고
    • Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis
    • Rodriguez-Lopez, J. N., A. T. Smith, and R. N. Thorneley. 1996. Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis. J. Biol. Chem. 271: 4023-4030.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4023-4030
    • Rodriguez-Lopez, J.N.1    Smith, A.T.2    Thorneley, R.N.3
  • 36
    • 0035988089 scopus 로고    scopus 로고
    • Expression of double Vitreoscilla hemoglobin enhances growth and alters ribosome and tRNA levels in Escherichia coli
    • Roos, V., C. I. Andersson, C. Arfvidsson, K. G. Wahlund, and L. Bulow. 2002. Expression of double Vitreoscilla hemoglobin enhances growth and alters ribosome and tRNA levels in Escherichia coli. Biotechnol. Prog. 18: 652-656.
    • (2002) Biotechnol. Prog. , vol.18 , pp. 652-656
    • Roos, V.1    Andersson, C.I.2    Arfvidsson, C.3    Wahlund, K.G.4    Bulow, L.5
  • 37
    • 33846220580 scopus 로고    scopus 로고
    • Roles of distal arginine in activity and stability of Coprinus cinereus peroxidase elucidated by kinetic and NMR analysis of the Arg51Gln, -Asn, -Leu, and -Lys mutants
    • Schiodt, C. B., N. C. Veitch, and K. G. Welinder. 2007. Roles of distal arginine in activity and stability of Coprinus cinereus peroxidase elucidated by kinetic and NMR analysis of the Arg51Gln, -Asn, -Leu, and -Lys mutants. J. Inorg. Biochem. 101: 336-347.
    • (2007) J. Inorg. Biochem. , vol.101 , pp. 336-347
    • Schiodt, C.B.1    Veitch, N.C.2    Welinder, K.G.3
  • 38
    • 33747846320 scopus 로고    scopus 로고
    • Chimeric antibodybinding Vitreoscilla hemoglobin (VHb) mediates redox-catalysis reaction: New insight into the functional role of VHb
    • Suwanwong, Y., M. Kvist, C. Isarankura-Na-Ayudhya, N. Tansila, L. Bulow, and V. Prachayasittikul. 2006. Chimeric antibodybinding Vitreoscilla hemoglobin (VHb) mediates redox-catalysis reaction: New insight into the functional role of VHb. Int. J. Biol. Sci. 2: 208-215.
    • (2006) Int. J. Biol. Sci. , vol.2 , pp. 208-215
    • Suwanwong, Y.1    Kvist, M.2    Isarankura-Na-Ayudhya, C.3    Tansila, N.4    Bulow, L.5    Prachayasittikul, V.6
  • 39
    • 0033775922 scopus 로고    scopus 로고
    • Dual nature of the distal histidine residue in the autoxidation reaction of myoglobin and hemoglobin comparison of the H64 mutants
    • Suzuki, T., Y. H. Watanabe, M. Nagasawa, A. Matsuoka, and K. Shikama. 2000. Dual nature of the distal histidine residue in the autoxidation reaction of myoglobin and hemoglobin comparison of the H64 mutants. Eur. J. Biochem. 267: 6166-6174.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6166-6174
    • Suzuki, T.1    Watanabe, Y.H.2    Nagasawa, M.3    Matsuoka, A.4    Shikama, K.5
  • 40
    • 0031569849 scopus 로고    scopus 로고
    • Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp
    • Tarricone, C., A. Galizzi, A. Coda, P. Ascenzi, and M. Bolognesi. 1997. Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp. Structure 5: 497-507.
    • (1997) Structure , vol.5 , pp. 497-507
    • Tarricone, C.1    Galizzi, A.2    Coda, A.3    Ascenzi, P.4    Bolognesi, M.5
  • 41
    • 0032502724 scopus 로고    scopus 로고
    • The molecular mechanism of autoxidation for human oxyhemoglobin. Tilting of the distal histidine causes nonequivalent oxidation in the beta chain
    • Tsuruga, M., A. Matsuoka, A. Hachimori, Y. Sugawara, and K. Shikama. 1998. The molecular mechanism of autoxidation for human oxyhemoglobin. Tilting of the distal histidine causes nonequivalent oxidation in the beta chain. J. Biol. Chem. 273: 8607-8615.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8607-8615
    • Tsuruga, M.1    Matsuoka, A.2    Hachimori, A.3    Sugawara, Y.4    Shikama, K.5
  • 42
    • 0742324902 scopus 로고    scopus 로고
    • Horseradish peroxidase: A modern view of a classic enzyme
    • Veitch, N. C. 2004. Horseradish peroxidase: A modern view of a classic enzyme. Phytochemistry 65: 249-259.
    • (2004) Phytochemistry , vol.65 , pp. 249-259
    • Veitch, N.C.1
  • 44
    • 0022486777 scopus 로고
    • Primary sequence of a dimeric bacterial haemoglobin from Vitreoscilla
    • Wakabayashi, S., H. Matsubara, and D. A. Webster. 1986. Primary sequence of a dimeric bacterial haemoglobin from Vitreoscilla. Nature 322: 481-483.
    • (1986) Nature , vol.322 , pp. 481-483
    • Wakabayashi, S.1    Matsubara, H.2    Webster, D.A.3
  • 45
    • 42949144463 scopus 로고    scopus 로고
    • Applications of the VHb gene vgb for improved microbial fermentation processes
    • Wei, X. X. and G. Q. Chen. 2008. Applications of the VHb gene vgb for improved microbial fermentation processes. Methods Enzymol. 436: 273-287.
    • (2008) Methods Enzymol , vol.436 , pp. 273-287
    • Wei, X.X.1    Chen, G.Q.2
  • 46
    • 0022272178 scopus 로고
    • Free-radical production and oxidative reactions of hemoglobin
    • Winterbourn, C. C. 1985. Free-radical production and oxidative reactions of hemoglobin. Environ. Health Perspect. 64: 321-330.
    • (1985) Environ. Health Perspect. , vol.64 , pp. 321-330
    • Winterbourn, C.C.1
  • 47
    • 37349057887 scopus 로고    scopus 로고
    • A high-sensitive amperometric hydrogen peroxide biosensor based on the immobilization of hemoglobin on gold colloid/L-cysteine/gold colloid/nanoparticles Pt-chitosan composite film-modified platinum disk electrode
    • Yang, G., R. Yuan, and Y. Q. Chai. 2008. A high-sensitive amperometric hydrogen peroxide biosensor based on the immobilization of hemoglobin on gold colloid/L-cysteine/gold colloid/nanoparticles Pt-chitosan composite film-modified platinum disk electrode. Colloids Surf. B Biointerfaces 61: 93-100.
    • (2008) Colloids Surf. B Biointerfaces. , vol.61 , pp. 93-100
    • Yang, G.1    Yuan, R.2    Chai, Y.Q.3
  • 48
    • 6344285767 scopus 로고    scopus 로고
    • A hydrogen peroxide sensor based on the peroxidase activity of hemoglobin immobilized on gold nanoparticles-modified ITO electrode
    • Zhang, J. and M. Oyama. 2004. A hydrogen peroxide sensor based on the peroxidase activity of hemoglobin immobilized on gold nanoparticles-modified ITO electrode. Electrochim. Acta 50: 85-90.
    • (2004) Electrochim. Acta. , vol.50 , pp. 85-90
    • Zhang, J.1    Oyama, M.2
  • 49
    • 0034707734 scopus 로고    scopus 로고
    • Stopped-flow spectrophotometric determination of hydrogen peroxide with hemoglobin as catalyst
    • Zhang, K., L. Mao, and R. Cai. 2000. Stopped-flow spectrophotometric determination of hydrogen peroxide with hemoglobin as catalyst. Talanta 51: 179-186.
    • (2000) Talanta , vol.51 , pp. 179-186
    • Zhang, K.1    Mao, L.2    Cai, R.3
  • 50
    • 33846557230 scopus 로고    scopus 로고
    • Recent developments and future prospects of Vitreoscilla hemoglobin application in metabolic engineering
    • Zhang, L., Y. Li, Z. Wang, Y. Xia, W. Chen, and K. Tang. 2007. Recent developments and future prospects of Vitreoscilla hemoglobin application in metabolic engineering. Biotechnol. Adv. 25: 123-136.
    • (2007) Biotechnol. Adv. , vol.25 , pp. 123-136
    • Zhang, L.1    Li, Y.2    Wang, Z.3    Xia, Y.4    Chen, W.5    Tang, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.