메뉴 건너뛰기




Volumn 41, Issue 2, 2005, Pages 363-372

Open reading frame yjbI of Bacillus subtilis codes for truncated hemoglobin

Author keywords

B. subtilis; Circular dichroism; Functional genomics; Peroxidase activity; Truncated hemoglobin

Indexed keywords

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 18144378787     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2005.02.022     Document Type: Article
Times cited : (5)

References (37)
  • 2
    • 0029893918 scopus 로고    scopus 로고
    • A brief history of hemoglobins: Plant, animal, protist, and bacteria
    • R.C. Hardison A brief history of hemoglobins: plant, animal, protist, and bacteria Proc. Natl. Acad. Sci. USA 93 1996 5675 5679
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5675-5679
    • Hardison, R.C.1
  • 3
  • 4
    • 0036219963 scopus 로고    scopus 로고
    • Cytoglobin: A novel globin type ubiquitously expressed in vertebrate tissues
    • T. Burmester, B. Ebner, B. Weich, and T. Hankeln Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues Mol. Biol. Evol. 19 2002 416 421
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 416-421
    • Burmester, T.1    Ebner, B.2    Weich, B.3    Hankeln, T.4
  • 5
    • 0035839641 scopus 로고    scopus 로고
    • Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen
    • J.T. Trent III, R.A. Watts, and M.S. Hargrove Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen J. Biol. Chem. 276 2001 30106 30110
    • (2001) J. Biol. Chem. , vol.276 , pp. 30106-30110
    • Trent III, J.T.1    Watts, R.A.2    Hargrove, M.S.3
  • 6
    • 0037205447 scopus 로고    scopus 로고
    • A ubiquitously expressed human hexacoordinate hemoglobin
    • J.T. Trent III, and M.S. Hargrove A ubiquitously expressed human hexacoordinate hemoglobin J. Biol. Chem. 277 2002 19538 19545
    • (2002) J. Biol. Chem. , vol.277 , pp. 19538-19545
    • Trent III, J.T.1    Hargrove, M.S.2
  • 10
  • 11
    • 0037059826 scopus 로고    scopus 로고
    • Truncated hemoglobins: A new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants
    • J.B. Wittenberg, M. Bolognesi, B.A. Wittenberg, and M. Guertin Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants J. Biol. Chem. 277 2002 871 874
    • (2002) J. Biol. Chem. , vol.277 , pp. 871-874
    • Wittenberg, J.B.1    Bolognesi, M.2    Wittenberg, B.A.3    Guertin, M.4
  • 12
    • 0032052216 scopus 로고    scopus 로고
    • Hemoglobins from bacteria to man: Evolution of different patterns of gene expression
    • R. Hardison Hemoglobins from bacteria to man: evolution of different patterns of gene expression J. Exp. Biol. 201 1998 1099 1117
    • (1998) J. Exp. Biol. , vol.201 , pp. 1099-1117
    • Hardison, R.1
  • 13
    • 0028204502 scopus 로고
    • Nuclear genes encoding chloroplast hemoglobins in the unicellular green alga Chlamydomonas eugametos
    • M. Couture, H. Chamberland, B. St-Pierre, J. Lafontaine, and M. Guertin Nuclear genes encoding chloroplast hemoglobins in the unicellular green alga Chlamydomonas eugametos Mol. Gen. Genet. 243 1994 185 197
    • (1994) Mol. Gen. Genet. , vol.243 , pp. 185-197
    • Couture, M.1    Chamberland, H.2    St-Pierre, B.3    Lafontaine, J.4    Guertin, M.5
  • 14
    • 0000870242 scopus 로고
    • Leghemoglobin and Rhizobium respiration
    • C.A. Appleby Leghemoglobin and Rhizobium respiration Ann Rev Plant Physiol 35 1984 443 478
    • (1984) Ann Rev Plant Physiol , vol.35 , pp. 443-478
    • Appleby, C.A.1
  • 15
    • 0032524650 scopus 로고    scopus 로고
    • Role for the Salmonella flavohemoglobin in protection from nitric oxide
    • M.J. Crawford, and D.E. Goldberg Role for the Salmonella flavohemoglobin in protection from nitric oxide J. Biol. Chem. 273 1998 12543 12547
    • (1998) J. Biol. Chem. , vol.273 , pp. 12543-12547
    • Crawford, M.J.1    Goldberg, D.E.2
  • 16
    • 0033017012 scopus 로고    scopus 로고
    • Anoxic function for the Escherichia coli flavohaemoglobin (Hmp): Reversible binding of nitric oxide and reduction to nitrous oxide
    • S.O. Kim, Y. Orii, D. Lloyd, M.N. Hughes, and R.K. Poole Anoxic function for the Escherichia coli flavohaemoglobin (Hmp): reversible binding of nitric oxide and reduction to nitrous oxide FEBS Lett. 445 1999 389 394
    • (1999) FEBS Lett. , vol.445 , pp. 389-394
    • Kim, S.O.1    Orii, Y.2    Lloyd, D.3    Hughes, M.N.4    Poole, R.K.5
  • 18
    • 0028242684 scopus 로고
    • Primary sequence and evidence for a physiological function of the flavohemoprotein of Alcaligenes eutrophus
    • R. Cramm, R.A. Siddiqui, and B. Friedrich Primary sequence and evidence for a physiological function of the flavohemoprotein of Alcaligenes eutrophus J. Biol. Chem. 269 1994 7349 7354
    • (1994) J. Biol. Chem. , vol.269 , pp. 7349-7354
    • Cramm, R.1    Siddiqui, R.A.2    Friedrich, B.3
  • 19
    • 0037013274 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis hemoglobin HbO associates with membranes and stimulates cellular respiration of recombinant Escherichia coli
    • R. Pathania, N.K. Navani, G. Rajamohan, and K.L. Dikshit Mycobacterium tuberculosis hemoglobin HbO associates with membranes and stimulates cellular respiration of recombinant Escherichia coli J. Biol. Chem. 277 2002 15293 15302
    • (2002) J. Biol. Chem. , vol.277 , pp. 15293-15302
    • Pathania, R.1    Navani, N.K.2    Rajamohan, G.3    Dikshit, K.L.4
  • 21
    • 3042727978 scopus 로고    scopus 로고
    • Neuroglobin: A respiratory protein of the nervous system
    • T. Burmester, and T. Hankeln Neuroglobin: a respiratory protein of the nervous system News Physiol. Sci. 19 2004 110 113
    • (2004) News Physiol. Sci. , vol.19 , pp. 110-113
    • Burmester, T.1    Hankeln, T.2
  • 24
    • 0035066385 scopus 로고    scopus 로고
    • Nonvertebrate hemoglobins: Functions and molecular adaptations
    • R.E. Weber, and S.N. Vinogradov Nonvertebrate hemoglobins: functions and molecular adaptations Physiol. Rev. 81 2001 569 628
    • (2001) Physiol. Rev. , vol.81 , pp. 569-628
    • Weber, R.E.1    Vinogradov, S.N.2
  • 25
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • M.M. Santoro, and D.W. Bolen Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants Biochemistry 27 1988 8063 8068
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 27
    • 0013792676 scopus 로고
    • Protein-heme interactions in heme-proteins: Cytochrome c
    • D.W. Urry Protein-heme interactions in heme-proteins: cytochrome c Proc. Natl. Acad. Sci. USA 54 1965 640 648
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 640-648
    • Urry, D.W.1
  • 28
    • 0019751640 scopus 로고
    • Circular dichroism spectra of hemoglobins
    • G. Geraci, and L.J. Parkhurst Circular dichroism spectra of hemoglobins Methods Enzymol. 76 1981 262 275
    • (1981) Methods Enzymol. , vol.76 , pp. 262-275
    • Geraci, G.1    Parkhurst, L.J.2
  • 29
    • 0016380496 scopus 로고
    • The Trp-59 fluorescence of ferricytochrome c as a sensitive measure of the over-all protein conformation
    • T.Y. Tsong The Trp-59 fluorescence of ferricytochrome c as a sensitive measure of the over-all protein conformation J. Biol. Chem. 249 1974 1988 1990
    • (1974) J. Biol. Chem. , vol.249 , pp. 1988-1990
    • Tsong, T.Y.1
  • 30
    • 1442277673 scopus 로고    scopus 로고
    • Folding barrier in horse cytochrome c: Support for a classical folding pathway
    • N.P. Prabhu, R. Kumar, and A.K. Bhuyan Folding barrier in horse cytochrome c: support for a classical folding pathway J. Mol. Biol. 337 2004 195 208
    • (2004) J. Mol. Biol. , vol.337 , pp. 195-208
    • Prabhu, N.P.1    Kumar, R.2    Bhuyan, A.K.3
  • 31
    • 0029786885 scopus 로고    scopus 로고
    • Protein stability: Urea-induced versus guanidine-induced unfolding of metmyoglobin
    • R. Gupta, S. Yadav, and F. Ahmad Protein stability: urea-induced versus guanidine-induced unfolding of metmyoglobin Biochemistry 35 1996 11925 11930
    • (1996) Biochemistry , vol.35 , pp. 11925-11930
    • Gupta, R.1    Yadav, S.2    Ahmad, F.3
  • 32
    • 0034708714 scopus 로고    scopus 로고
    • Heme orientation affects holo-myoglobin folding and unfolding kinetics
    • Moczygemba, J. Guidry, and P. Wittung-Stafshede Heme orientation affects holo-myoglobin folding and unfolding kinetics FEBS Lett. 470 2000 203 206
    • (2000) FEBS Lett. , vol.470 , pp. 203-206
    • Moczygemba1    Guidry, J.2    Wittung-Stafshede, P.3
  • 34
    • 0028365895 scopus 로고
    • Peroxidative activities of hemoglobin and hemoglobin derivatives
    • J. Everse, M.C. Johnson, and M.A. Marini Peroxidative activities of hemoglobin and hemoglobin derivatives Methods Enzymol. 231 1994 547 561
    • (1994) Methods Enzymol. , vol.231 , pp. 547-561
    • Everse, J.1    Johnson, M.C.2    Marini, M.A.3
  • 35
    • 1242292278 scopus 로고    scopus 로고
    • Engineering peroxidase activity in myoglobin: The haem cavity structure and peroxide activation in the T67R/S92D mutant and its derivative reconstituted with protohaemin-l-histidine
    • R. Roncone, E. Monzani, M. Murtas, G. Battaini, A. Pennati, A.M. Sanangelantoni, S. Zuccotti, M. Bolognesi, and L. Casella Engineering peroxidase activity in myoglobin: the haem cavity structure and peroxide activation in the T67R/S92D mutant and its derivative reconstituted with protohaemin-l-histidine Biochem. J. 377 2004 717 724
    • (2004) Biochem. J. , vol.377 , pp. 717-724
    • Roncone, R.1    Monzani, E.2    Murtas, M.3    Battaini, G.4    Pennati, A.5    Sanangelantoni, A.M.6    Zuccotti, S.7    Bolognesi, M.8    Casella, L.9
  • 36
    • 0034830863 scopus 로고    scopus 로고
    • The peroxidase activity of cytochrome c-550 from Paracoccus versutus
    • R.E.M. Diederix, M. Ubbink, and G.W. Canters The peroxidase activity of cytochrome c-550 from Paracoccus versutus Eur. J. Biochem. 268 2001 4207 4216
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4207-4216
    • Diederix, R.E.M.1    Ubbink, M.2    Canters, G.W.3
  • 37
    • 0037016639 scopus 로고    scopus 로고
    • Efect of the protein matrix of cytochrome c in suppressing the inherent peroxidase activity of its heme prosthetic group
    • R.E.M. Diederix, M. Ubbink, and G.W. Canters Efect of the protein matrix of cytochrome c in suppressing the inherent peroxidase activity of its heme prosthetic group Chem. Biochem. 3 2002 110 112
    • (2002) Chem. Biochem. , vol.3 , pp. 110-112
    • Diederix, R.E.M.1    Ubbink, M.2    Canters, G.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.