메뉴 건너뛰기




Volumn 1834, Issue 9, 2013, Pages 1932-1938

Ligand-rebinding kinetics of 2/2 hemoglobin from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125

Author keywords

Antarctic bacterial hemoglobin; Hydrostatic high pressure; Laser photolysis; Ligand binding kinetics; Oxygen; Truncated hemoglobin

Indexed keywords

AMINO ACID; GLOBIN; HEMOGLOBIN; OXYGEN; TRUNCATED HEMOGLOBIN; CARBON MONOXIDE; HEME; IRON; MYOGLOBIN; NEUROGLOBIN; REACTIVE OXYGEN METABOLITE;

EID: 84884177102     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.02.013     Document Type: Article
Times cited : (9)

References (36)
  • 1
    • 78649500833 scopus 로고    scopus 로고
    • Cold-adapted bacteria and the globin case study in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125
    • R. Russo, D. Giordano, A. Riccio, G. Di Prisco, C. Verde, Cold-adapted bacteria and the globin case study in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125, Mar. Genomics 3 (2010) 125-131.
    • (2010) Mar. Genomics , vol.3 , pp. 125-131
    • Russo, R.1    Giordano, D.2    Riccio, A.3    Di Prisco, G.4    Verde, C.5
  • 5
    • 33744980249 scopus 로고    scopus 로고
    • Complete genome sequence of Yersinia pestis strains antiqua and Nepal516: Evidence of gene reduction in an emerging pathogen
    • DOI 10.1128/JB.00124-06
    • P.S. Chain, P. Hu, S.A. Malfatti, L. Radnedge, F. Larimer, L.M. Vergez, P. Worsham, M.C. Chu, G.L. Andersen, Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen, J. Bacteriol. 188 (2006) 4453-4463. (Pubitemid 43865765)
    • (2006) Journal of Bacteriology , vol.188 , Issue.12 , pp. 4453-4463
    • Chain, P.S.G.1    Hu, P.2    Malfatti, S.A.3    Radnedge, L.4    Larimer, F.5    Vergez, L.M.6    Worsham, P.7    Chu, M.C.8    Andersen, G.L.9
  • 6
    • 77950281429 scopus 로고    scopus 로고
    • Proteomics of life at low temperatures: Trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125
    • F. Piette, S. D'Amico, C. Struvay, G. Mazzuchelli, J. Renaut, M.L. Tutino, A. Danchin, P. Leprince, G. Feller, Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125, Mol. Microbiol. 76 (2010) 120-132.
    • (2010) Mol. Microbiol. , vol.76 , pp. 120-132
    • Piette, F.1    D'Amico, S.2    Struvay, C.3    Mazzuchelli, G.4    Renaut, J.5    Tutino, M.L.6    Danchin, A.7    Leprince, P.8    Feller, G.9
  • 7
    • 79958264198 scopus 로고    scopus 로고
    • Life in the cold: A proteomic study of cold-repressed proteins in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125
    • F. Piette, S. D'Amico, G. Mazzuchelli, A. Danchin, P. Leprince, G. Feller, Life in the cold: a proteomic study of cold-repressed proteins in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125, Appl. Environ. Microbiol. 77 (2011) 3881-3883.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 3881-3883
    • Piette, F.1    D'Amico, S.2    Mazzuchelli, G.3    Danchin, A.4    Leprince, P.5    Feller, G.6
  • 8
    • 44049108195 scopus 로고    scopus 로고
    • Diversity of globin function: Enzymatic, transport, storage, and sensing
    • S.N. Vinogradov, L. Moens, Diversity of globin function: enzymatic, transport, storage, and sensing, J. Biol. Chem. 283 (2008) 8773-8777.
    • (2008) J. Biol. Chem. , vol.283 , pp. 8773-8777
    • Vinogradov, S.N.1    Moens, L.2
  • 9
    • 77954660667 scopus 로고    scopus 로고
    • The role of a 2-on-2 hemoglobin in oxidative and nitrosative stress resistance of Antarctic Pseudoalteromonas haloplanktis TAC125
    • E. Parrilli, M. Giuliani, D. Giordano, R. Russo, G. Marino, C. Verde, M.L. Tutino, The role of a 2-on-2 hemoglobin in oxidative and nitrosative stress resistance of Antarctic Pseudoalteromonas haloplanktis TAC125, Biochimie 92 (2010) 1003-1009.
    • (2010) Biochimie , vol.92 , pp. 1003-1009
    • Parrilli, E.1    Giuliani, M.2    Giordano, D.3    Russo, R.4    Marino, G.5    Verde, C.6    Tutino, M.L.7
  • 11
    • 34447502126 scopus 로고    scopus 로고
    • The truncated hemoglobins in the Antarctic psychrophilic bacterium Pseudoalteromonas haloplanktis TAC125
    • DOI 10.1016/j.gene.2007.02.037, PII S0378111907002156
    • D. Giordano, E. Parrilli, A. Dettaï, R. Russo, G. Barbiero, G. Marino, G. Lecointre, G. Di Prisco, L. Tutino, C. Verde, The truncated hemoglobins in the Antarctic psychrophilic bacterium Pseudoalteromonas haloplanktis TAC125, Gene 398 (2007) 69-77. (Pubitemid 47078996)
    • (2007) Gene , vol.398 , Issue.1-2 SPEC. ISSUE , pp. 69-77
    • Giordano, D.1    Parrilli, E.2    Dettai, A.3    Russo, R.4    Barbiero, G.5    Marino, G.6    Lecointre, G.7    Di Prisco, G.8    Tutino, L.9    Verde, C.10
  • 12
  • 14
    • 0012155523 scopus 로고
    • Specific volumes of water at high pressures, obtained from ultrasonic-propagation measurements
    • R. Vedam, G. Holton, Specific volumes of water at high pressures, obtained from ultrasonic-propagation measurements, J. Acoust. Soc. Am. 43 (1968) 108-116.
    • (1968) J. Acoust. Soc. Am. , vol.43 , pp. 108-116
    • Vedam, R.1    Holton, G.2
  • 15
    • 0020712468 scopus 로고
    • The effect of high pressure upon proteins and other biomolecules
    • G. Weber, H.G. Dickamer, The effect of high pressure upon proteins and other biomolecules, Q. Rev. Biophys. 16 (1983) 89-112.
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 89-112
    • Weber, G.1    Dickamer, H.G.2
  • 16
    • 33645960997 scopus 로고    scopus 로고
    • Protein stability and dynamicsinthe pressure-temperature plane
    • F. Meersman, L. Smeller, K. Heremans, Protein stability and dynamicsinthe pressure-temperature plane, Biochim. Biophys. Acta 1764 (2006) 346-354.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 346-354
    • Meersman, F.1    Smeller, L.2    Heremans, K.3
  • 17
    • 33646900712 scopus 로고    scopus 로고
    • Probing conformational fluctuation of proteins by pressure perturbation
    • DOI 10.1021/cr040440z
    • K. Akasaka, Probing conformational fluctuation of proteins by pressure perturbation, Chem. Rev. 106 (2006) 1814-1835. (Pubitemid 43792782)
    • (2006) Chemical Reviews , vol.106 , Issue.5 , pp. 1814-1835
    • Akasaka, K.1
  • 20
    • 79953778829 scopus 로고    scopus 로고
    • Kinetics inside the protein: Shape of the geminate kinetics in myoglobin
    • D. Hamdane, L. Kiger, G. Hui-Bon-Hoa, M.C. Marden, Kinetics inside the protein: shape of the geminate kinetics in myoglobin, J. Phys. Chem. B 115 (2011) 3919-3923.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 3919-3923
    • Hamdane, D.1    Kiger, L.2    Hui-Bon-Hoa, G.3    Marden, M.C.4
  • 23
    • 0024519403 scopus 로고
    • Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin. Site-directed mutagenesis of the distal histidine
    • B.A. Springer, K.D. Egeberg, S.G. Sligar, R.J. Rohlfs, A.J. Mathews, J.S. Olson, Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin. Site-directed mutagenesis of the distal histidine, J. Biol. Chem. 264 (1989) 3057-3060. (Pubitemid 19063357)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.6 , pp. 3057-3060
    • Springer, B.A.1    Egeberg, K.D.2    Sligar, S.G.3    Rohlfs, R.J.4    Mathews, A.J.5    Olson, J.S.6
  • 26
    • 84868117103 scopus 로고    scopus 로고
    • Comparative genomics of neuroglobin reveals its early origins
    • J. Dröge, A. Pande, E.W. Englander, W. Makałowski, Comparative genomics of neuroglobin reveals its early origins, PLoS One 7 (2012) e47972.
    • (2012) PLoS One , vol.7
    • Dröge, J.1    Pande, A.2    Englander, E.W.3    Makałowski, W.4
  • 27
  • 33
    • 79957794175 scopus 로고    scopus 로고
    • Electron transfer function versus oxygen delivery: A comparative study for several hexacoordinated globins across the animal kingdom
    • L. Kiger, L. Tilleman, E. Geuens, D. Hoogewijs, C. Lechauve, L. Moens, S. Dewilde, M.C. Marden, Electron transfer function versus oxygen delivery: a comparative study for several hexacoordinated globins across the animal kingdom, PLoS One 6 (2011) e20478.
    • (2011) PLoS One , vol.6
    • Kiger, L.1    Tilleman, L.2    Geuens, E.3    Hoogewijs, D.4    Lechauve, C.5    Moens, L.6    Dewilde, S.7    Marden, M.C.8
  • 34
    • 79960662890 scopus 로고    scopus 로고
    • Oxygen supply from the bird's eye perspective: Globin E is a respiratory protein in the chicken retina
    • M. Blank, L. Kiger, A. Thielebein, F. Gerlach, T. Hankeln, M.C. Marden, T. Burmester, Oxygen supply from the bird's eye perspective: globin E is a respiratory protein in the chicken retina, J. Biol. Chem. 286 (2011) 26507-26515.
    • (2011) J. Biol. Chem. , vol.286 , pp. 26507-26515
    • Blank, M.1    Kiger, L.2    Thielebein, A.3    Gerlach, F.4    Hankeln, T.5    Marden, M.C.6    Burmester, T.7
  • 35
    • 4143067901 scopus 로고    scopus 로고
    • Neuroglobin and other hexacoordinated hemoglobins show a weak temperature dependence of oxygen binding
    • DOI 10.1529/biophysj.104.042168
    • J. Uzan, S. Dewilde, T. Burmester, T. Hankeln, L. Moens, D. Hamdane, M.C. Marden, L. Kiger, Neuroglobin and other hexacoordinated hemoglobins show a weak temperature dependence of oxygen binding, Biophys. J. 87 (2004) 1196-1204. (Pubitemid 39095096)
    • (2004) Biophysical Journal , vol.87 , Issue.2 , pp. 1196-1204
    • Uzan, J.1    Dewilde, S.2    Burmester, T.3    Hankeln, T.4    Moens, L.5    Hamdane, D.6    Marden, M.C.7    Kiger, L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.