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Volumn 1834, Issue 9, 2013, Pages 1901-1909

H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin

Author keywords

Cyanide ligand; Hydrogen bond; Hydroxyl ligand; Resonance Raman; Truncated hemoglobin

Indexed keywords

CYANIDE; HYDROXYL GROUP; LIGAND; TRUNCATED HEMOGLOBIN; TYROSINE; WATER; HEME; HEMOGLOBIN; HYDROXIDE; HYDROXIDE ION; MYOGLOBIN;

EID: 84884641056     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.02.033     Document Type: Article
Times cited : (21)

References (26)
  • 2
    • 84860389795 scopus 로고    scopus 로고
    • The optical spectra of fluoride complexes can effectively probe H-bonding interactions in the distal cavity of heme proteins
    • E. Droghetti, F.P. Nicoletti, A. Bonamore, N. Sciamanna, A. Boffi, A. Feis, G. Smulevich, The optical spectra of fluoride complexes can effectively probe H-bonding interactions in the distal cavity of heme proteins, J. Inorg. Biochem. 105 (2011) 1338-1343.
    • (2011) J. Inorg. Biochem. , vol.105 , pp. 1338-1343
    • Droghetti, E.1    Nicoletti, F.P.2    Bonamore, A.3    Sciamanna, N.4    Boffi, A.5    Feis, A.6    Smulevich, G.7
  • 5
    • 23844469133 scopus 로고    scopus 로고
    • A novel thermostable hemoglobin from the actinobacterium Thermobifida fusca
    • DOI 10.1111/j.1742-4658.2005.04831.x
    • A. Bonamore, A. Ilari, L Giangiacomo, A. Bellelli, V. Morea, A. Boffi, A novel thermostable hemoglobin from the actinobacterium Thermobifida fusca, FEBS J. 272 (2005) 4189-4201. (Pubitemid 41160925)
    • (2005) FEBS Journal , vol.272 , Issue.16 , pp. 4189-4201
    • Bonamore, A.1    Ilari, A.2    Giangiacomo, L.3    Bellelli, A.4    Morea, V.5    Boffi, A.6
  • 6
    • 77749259052 scopus 로고    scopus 로고
    • New insights into the role of distal histidine flexibility in ligand stabilization of dehaloperoxidase-hemoglobin from Amphitrite ornate
    • F.P. Nicoletti, M. Thompson, B.D. Howes, S. Franzen, G. Smulevich, New insights into the role of distal histidine flexibility in ligand stabilization of dehaloperoxidase-hemoglobin from Amphitrite ornate, Biochemistry 49 (2010) 1903-1912.
    • (2010) Biochemistry , vol.49 , pp. 1903-1912
    • Nicoletti, F.P.1    Thompson, M.2    Howes, B.D.3    Franzen, S.4    Smulevich, G.5
  • 7
    • 0029633186 scopus 로고
    • AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules
    • DA Pearlman, DA Case, J.W. Caldwell, W.S. Ross, T.E. Cheatham III, S. DeBolt, D. Ferguson, G. Seibel, P. Kollman, AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules, Comput. Phys. Commun. 91 (1995) 1-41.
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 1-41
    • Pearlman, D.A.1    Case, D.A.2    Caldwell, J.W.3    Ross, W.S.4    Cheatham III, T.E.5    DeBolt, S.6    Ferguson, D.7    Seibel, G.8    Kollman, P.9
  • 8
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • J.-P. Ryckaert, G. Ciccotti, H.J.C. Berendsen, Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes, J. Comput. Phys. 23 (1977) 327-341.
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 9
    • 0028354425 scopus 로고
    • Spin state and axial ligand bonding in the hydroxide complexes of metmyoglobin, methemoglobin, and horseradish peroxidase at room and low temperatures
    • A. Feis, M.P. Marzocchi, M. Paoli, G. Smulevich, Spin state and axial ligand bonding in the hydroxide complexes of metmyoglobin, methemoglobin, and horseradish peroxidase at room and low temperatures, Biochemistry 33 (1994) 4577-4583. (Pubitemid 24145106)
    • (1994) Biochemistry , vol.33 , Issue.15 , pp. 4577-4583
    • Feis, A.1    Marzocchi, M.P.2    Paoli, M.3    Smulevich, G.4
  • 10
    • 0000680130 scopus 로고
    • Two-dimensional vibrational analysis of the Lippincott-Schröder potential for OH-O, NH-O and NH-N hydrogen bonds and the deuterium isotope effect
    • T Saitoh, K. Mori, R. Itoh, Two-dimensional vibrational analysis of the Lippincott-Schröder potential for OH-O, NH-O and NH-N hydrogen bonds and the deuterium isotope effect, Chem. Phys. 60 (1982) 161-180.
    • (1982) Chem. Phys. , vol.60 , pp. 161-180
    • Saitoh, T.1    Mori, K.2    Itoh, R.3
  • 11
    • 0021473156 scopus 로고
    • Iron-carbon bond lengths in carbonmonoxy and cyanomet complexes of the monomeric haemoglobin III from Chironomus thummi thummi: A critical comparison between resonance Raman and X-ray diffraction studies
    • N.-T. Yu, B. Benko, EA Kerr, K. Gersonde, Iron-carbon bond lengths in carbonmonoxy and cyanomet complexes of the monomeric haemoglobin III from Chironomus thummi thummi: a critical comparison between resonance Raman and X-ray diffraction studies, Proc. Natl. Acad. Sci. U. S.A. 81 (1984) 5106-5110.
    • (1984) Proc. Natl. Acad. Sci. U. S.A. , vol.81 , pp. 5106-5110
    • Yu, N.-T.1    Benko, B.2    Kerr, E.A.3    Gersonde, K.4
  • 12
    • 0028279008 scopus 로고
    • Resonance Raman study of cyanide-ligated horseradish peroxidase. Detection of two binding geometries and direct evidence for the 'push-pull' effect
    • J. Al-Mustafa, J.R. Kincaid, Resonance Raman study of cyanide-ligated horseradish peroxidase. Detection of two binding geometries and direct evidence for the "push-pull" effect, Biochemistry 33 (1994) 2191-2197. (Pubitemid 24099617)
    • (1994) Biochemistry , vol.33 , Issue.8 , pp. 2191-2197
    • Al-Mustafa, J.1    Kincaid, J.R.2
  • 13
    • 0031037679 scopus 로고    scopus 로고
    • Mutation of distal residues of horseradish peroxidase: Influence on substrate binding and cavity properties
    • DOI 10.1021/bi962502o
    • B.D. Howes, J.N. Rodriguez-Lopez, AT. Smith, G. Smulevich, Mutation of distal residues of horseradish peroxidase: influence on substrate binding and cavity properties, Biochemistry 36 (1997) 1532-1543. (Pubitemid 27074978)
    • (1997) Biochemistry , vol.36 , Issue.6 , pp. 1532-1543
    • Howes, B.D.1    Rodriguez-Lopez, J.N.2    Smith, A.T.3    Smulevich, G.4
  • 14
    • 0031837411 scopus 로고    scopus 로고
    • Spin-state equilibria and axial ligand bonding in FixL hydroxide: A resonance raman study
    • DOI 10.1007/s007750050232
    • G.S. Lukat-Rodgers, K.R. Rodgers, Spin-state equilibria and axial ligand bonding in FixL hydroxide: a resonance Raman study, J. Biol. Inorg. Chem. 3 (1998) 274-281. (Pubitemid 28299770)
    • (1998) Journal of Biological Inorganic Chemistry , vol.3 , Issue.3 , pp. 274-281
    • Lukat-Rodgers, G.S.1    Rodgers, K.R.2
  • 15
    • 10644274523 scopus 로고    scopus 로고
    • Structural and functional properties of hemoglobins from unicellular organisms as revealed by resonance Raman spectroscopy
    • DOI 10.1016/j.jinorgbio.2004.10.017, PII S0162013404003228, Heme-Diatomic Interactions, Part 1
    • T Egawa, S.-R. Yeh, Structural and functional properties of hemoglobins from unicellular organisms as revealed by resonance Raman spectroscopy, J. Inorg. Biochem. 99 (2005) 72-96. (Pubitemid 39646480)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 72-96
    • Egawa, T.1    Yeh, S.-R.2
  • 16
    • 0023448147 scopus 로고
    • Resonance Raman studies of sterically hindered cyanomet "strapped" hemes. Effects of ligand distortion and base tension on iron-carbon bond
    • T Tanaka, N.T. Yu, CK. Chang, Resonance Raman studies of sterically hindered cyanomet "strapped" hemes. Effects of ligand distortion and base tension on iron-carbon bond, Biophys. J. 52 (1987) 801-805.
    • (1987) Biophys. J. , vol.52 , pp. 801-805
    • Tanaka, T.1    Yu, N.T.2    Chang, C.K.3
  • 17
    • 1842513886 scopus 로고    scopus 로고
    • - adducts of hemoglobin, myoglobin, and cytochrome c oxidase: Evidence for vibrational coupling between the Fe-C-N bending and porphyrin in-plane modes
    • - adducts of hemoglobin, myoglobin, and cytochrome c oxidase: evidence for vibrational coupling between the Fe-C-N bending and porphyrin in-plane modes, J. Phys. Chem. 100 (1996) 15274-15279. (Pubitemid 126788536)
    • (1996) Journal of Physical Chemistry , vol.100 , Issue.37 , pp. 15274-15279
    • Hirota, S.1    Ogura, T.2    Shinzawa-Itoh, K.3    Yoshikawa, S.4    Kitagawa, T.5
  • 18
    • 0032774244 scopus 로고    scopus 로고
    • Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: An x-ray crystallographic study
    • M. Bolognesi, C. Rosano, R. Losso, A. Borassi, M. Rizzi, J.B. Wittenberg, A. Boffi, P. Ascenzi, Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an X-Ray crystallographic study, Biophys. J. 77 (1999) 1093-1099. (Pubitemid 29362479)
    • (1999) Biophysical Journal , vol.77 , Issue.2 , pp. 1093-1099
    • Bolognesi, M.1    Rosano, C.2    Losso, R.3    Borassi, A.4    Rizzi, M.5    Wittenberg, J.B.6    Boffi, A.7    Ascenzi, P.8
  • 19
    • 0034322841 scopus 로고    scopus 로고
    • Distal interactions in the cyanide complex of ferric Chlamydomonas hemoglobin
    • DOI 10.1021/jp000452y
    • T.K. Das, M. Couture, M. Guertin, D.L. Rousseau, Distal interactions in the cyanide complex of ferric Chlamydomonas haemoglobin, J. Phys. Chem. B 104 (2000) 10750-10756. (Pubitemid 32023464)
    • (2000) Journal of Physical Chemistry B , vol.104 , Issue.46 , pp. 10750-10756
    • Das, T.K.1    Couture, M.2    Guertin, M.3    Rousseau, D.L.4
  • 22
    • 0028921266 scopus 로고
    • Resonance Raman investigation of cyanide ligated beef liver and Aspergillus niger catalases
    • J. Al-Mustafa, M. Sykora, J.R. Kincaid, Resonance Raman investigation of cyanide ligated beef liver and Aspergillus niger catalases, J. Biol. Chem. 270 (1995) 10449-10460.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10449-10460
    • Al-Mustafa, J.1    Sykora, M.2    Kincaid, J.R.3
  • 23
    • 34548502206 scopus 로고    scopus 로고
    • Structural and functional properties of a single domain hemoglobin from the food-borne pathogen Campylobactor jejuni
    • DOI 10.1074/jbc.M704415200
    • C. Lu, M. Mukai, Y. Lin, G. Wu, R.K. Poole, S.-R. Yeh, Structural and functional properties of a single domain hemoglobin from the food-borne pathogen Campylobactor jejuni, J. Biol. Chem. 282 (2007) 25917-25928. (Pubitemid 47372797)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.35 , pp. 25917-25928
    • Lu, C.1    Mukai, M.2    Lin, Y.3    Wu, G.4    Poole, R.K.5    Yeh, S.-R.6
  • 26
    • 0025167226 scopus 로고
    • Hemoglobins of the Lucina pectinata/Bacteria Symbiosis
    • D.W. Kraus, J.B. Wittenberg, J.F. Lu, J. Peisach, Hemoglobins of the Lucina pectinata/Bacteria Symbiosis, J. Biol. Chem. 265 (1990) 16054-16059.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16054-16059
    • Kraus, D.W.1    Wittenberg, J.B.2    Lu, J.F.3    Peisach, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.