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Volumn 316, Issue 4, 2004, Pages 1101-1106

Structure-function studies of the Vitreoscilla hemoglobin D-region

Author keywords

Bacterial hemoglobin; Flavin domain; Heme protein interactions; Hemoglobin flavoprotein interactions

Indexed keywords

GLOBIN; HEME; HEMOGLOBIN; QUERCETIN;

EID: 1642325905     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.02.154     Document Type: Article
Times cited : (23)

References (20)
  • 2
    • 0019923105 scopus 로고
    • Control of heme content in Vitreoscilla by oxygen
    • Boerman S.J., Webster D.A. Control of heme content in Vitreoscilla by oxygen. J. Gen. Appl. Microbiol. 28:1982;35-43.
    • (1982) J. Gen. Appl. Microbiol. , vol.28 , pp. 35-43
    • Boerman, S.J.1    Webster, D.A.2
  • 4
    • 0033951878 scopus 로고    scopus 로고
    • Cloning and expression of Vitreoscilla hemoglobin gene in Burkholderia sp. strain DNT for enhancement of 2,4-dinitrotoluene degradation
    • Patel S.M., Stark B.C., Hwang K.W., Dikshit K.L., Webster D.A. Cloning and expression of Vitreoscilla hemoglobin gene in Burkholderia sp. strain DNT for enhancement of 2,4-dinitrotoluene degradation. Biotechnol. Prog. 16:2000;26-30.
    • (2000) Biotechnol. Prog. , vol.16 , pp. 26-30
    • Patel, S.M.1    Stark, B.C.2    Hwang, K.W.3    Dikshit, K.L.4    Webster, D.A.5
  • 5
    • 0034925187 scopus 로고    scopus 로고
    • Effects of culture conditions on enhancement of 2,4-dinitrotoluene degradation by Burkholderia engineered with the Vitreoscilla hemoglobin gene
    • Nasr M.A., Hwang K.W., Akbas M., Webster D.A., Stark B.C. Effects of culture conditions on enhancement of 2,4-dinitrotoluene degradation by Burkholderia engineered with the Vitreoscilla hemoglobin gene. Biotechnol. Prog. 17:2001;359-361.
    • (2001) Biotechnol. Prog. , vol.17 , pp. 359-361
    • Nasr, M.A.1    Hwang, K.W.2    Akbas, M.3    Webster, D.A.4    Stark, B.C.5
  • 6
    • 0031569849 scopus 로고    scopus 로고
    • Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp.
    • Tarricone C., Galizzi A., Coda A., Ascenzi P., Bolognesi M. Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp. Structure. 5:1997;497-507.
    • (1997) Structure , vol.5 , pp. 497-507
    • Tarricone, C.1    Galizzi, A.2    Coda, A.3    Ascenzi, P.4    Bolognesi, M.5
  • 7
    • 0016192420 scopus 로고
    • Reduced nicotinamide adenine dinucleotide cytochrome o reductase associated with cytochrome o purified from Vitreoscilla. Evidence for an intermediate oxygenated form of cytochrome o
    • Webster D.A., Liu C.Y. Reduced nicotinamide adenine dinucleotide cytochrome o reductase associated with cytochrome o purified from Vitreoscilla. Evidence for an intermediate oxygenated form of cytochrome o. J. Biol. Chem. 249:1974;4257-4260.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4257-4260
    • Webster, D.A.1    Liu, C.Y.2
  • 8
    • 0029610660 scopus 로고
    • Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 Å resolution
    • Ermler U., Siddiqui R.A., Cramm R., Friedrich B. Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75. Å resolution EMBO J. 14:1995;6067-6077.
    • (1995) EMBO J. , vol.14 , pp. 6067-6077
    • Ermler, U.1    Siddiqui, R.A.2    Cramm, R.3    Friedrich, B.4
  • 10
    • 0037031866 scopus 로고    scopus 로고
    • Vitreoscilla hemoglobin binds to subunit I of cytochrome bo ubiquinol oxidases
    • Park K.W., Kim K.J., Howard A.J., Stark B.C., Webster D.A. Vitreoscilla hemoglobin binds to subunit I of cytochrome bo ubiquinol oxidases. J. Biol. Chem. 277:2002;33334-33337.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33334-33337
    • Park, K.W.1    Kim, K.J.2    Howard, A.J.3    Stark, B.C.4    Webster, D.A.5
  • 11
    • 0041375628 scopus 로고    scopus 로고
    • Effects of Vitreoscilla hemoglobin on the 2,4-dinitrotoluene (DNT) dioxygenase activity of Burkholderia and on DNT degradation in two phase bioreactors
    • Lin J.M., Stark B.C., Webster D.A. Effects of Vitreoscilla hemoglobin on the 2,4-dinitrotoluene (DNT) dioxygenase activity of Burkholderia and on DNT degradation in two phase bioreactors. J. Indust. Microbiol. Biotechnol. 30:2003;362-368.
    • (2003) J. Indust. Microbiol. Biotechnol. , vol.30 , pp. 362-368
    • Lin, J.M.1    Stark, B.C.2    Webster, D.A.3
  • 12
    • 0027404666 scopus 로고
    • Cloning and characterization of Pseudomonas sp. strain DNT genes for 2,4-dinitrotoluene degradation
    • Suen W.C., Spain J.C. Cloning and characterization of Pseudomonas sp. strain DNT genes for 2,4-dinitrotoluene degradation. J. Bacteriol. 175:1993;1831-1837.
    • (1993) J. Bacteriol. , vol.175 , pp. 1831-1837
    • Suen, W.C.1    Spain, J.C.2
  • 13
    • 0031819672 scopus 로고    scopus 로고
    • Site-directed mutagenesis of bacterial hemoglobin: The role of glutamine (E7) in oxygen-binding in the distal heme pocket
    • Dikshit K.L., Yutaka O., Navani N., Patel S., Huang H., Stark B.C., Webster D.A. Site-directed mutagenesis of bacterial hemoglobin: the role of glutamine (E7) in oxygen-binding in the distal heme pocket. Arch. Biochem. Biophys. 349:1998;161-166.
    • (1998) Arch. Biochem. Biophys. , vol.349 , pp. 161-166
    • Dikshit, K.L.1    Yutaka, O.2    Navani, N.3    Patel, S.4    Huang, H.5    Stark, B.C.6    Webster, D.A.7
  • 14
    • 0002263294 scopus 로고
    • Laboratory methods
    • K.M. Smith. Amsterdam: Elsevier/North Holland Biomedical Press
    • Furhop J.H., Smith K.M. Laboratory methods. Smith K.M. Porphyrin and Metalloporphyrins. 1975;757-869 Elsevier/North Holland Biomedical Press, Amsterdam.
    • (1975) Porphyrin and Metalloporphyrins , pp. 757-869
    • Furhop, J.H.1    Smith, K.M.2
  • 15
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 0023756153 scopus 로고
    • Cloning, characterization and expression of the bacterial globin gene from Vitreoscilla in Escherichia coli
    • Dikshit K.L., Webster D.A. Cloning, characterization and expression of the bacterial globin gene from Vitreoscilla in Escherichia coli. Gene. 70:1988;377-386.
    • (1988) Gene , vol.70 , pp. 377-386
    • Dikshit, K.L.1    Webster, D.A.2
  • 17
    • 0003785155 scopus 로고
    • Cold Spring Harbor, New York: Cold Spring Harbor Laboratory
    • Miller J.H. Experiments in Molecular Genetics. 1972;Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 18
    • 0020490246 scopus 로고
    • Oxygenated intermediate and carbonyl species of cytochrome o (Vitreoscilla). Characterization by infrared spectroscopy
    • Choc M.G., Webster D.A., Caughey W.S. Oxygenated intermediate and carbonyl species of cytochrome o (Vitreoscilla). Characterization by infrared spectroscopy. J. Biol. Chem. 257:1982;865-869.
    • (1982) J. Biol. Chem. , vol.257 , pp. 865-869
    • Choc, M.G.1    Webster, D.A.2    Caughey, W.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.