메뉴 건너뛰기




Volumn 272, Issue 16, 2005, Pages 4189-4201

A novel thermostable hemoglobin from the actinobacterium Thermobifida fusca

Author keywords

Bacterial hemoglobins; Heme ligand binding properties; Oxygen binding; Thermostable proteins; X ray structure

Indexed keywords

HEMOGLOBIN; PROTEIN TF TRHB; UNCLASSIFIED DRUG;

EID: 23844469133     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04831.x     Document Type: Article
Times cited : (48)

References (39)
  • 3
    • 0141761124 scopus 로고    scopus 로고
    • The diversity of globin-coupled sensors
    • Freitas TAK, Hou S & Alam M (2003) The diversity of globin-coupled sensors. FEBS Lett 552, 99-104.
    • (2003) FEBS Lett , vol.552 , pp. 99-104
    • Freitas, T.A.K.1    Hou, S.2    Alam, M.3
  • 4
    • 0037059826 scopus 로고    scopus 로고
    • Truncated hemoglobins: A new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants
    • Wittenberg JB, Bolognesi M, Wittenberg BA & Guertin M (2002) Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants. J Biol Chem 277, 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
  • 5
    • 0024338305 scopus 로고
    • Use of site-directed mutagenesis to destabilize native apomyoglobin relative to folding intermediates
    • Hughson FM & Baldwin RL (1989) Use of site-directed mutagenesis to destabilize native apomyoglobin relative to folding intermediates. Biochemistry 28, 4415-4422.
    • (1989) Biochemistry , vol.28 , pp. 4415-4422
    • Hughson, F.M.1    Baldwin, R.L.2
  • 6
    • 0014413956 scopus 로고
    • Spectral studies on the denaturation of myoglobin
    • Schechter AN & Epstein CJ (1968) Spectral studies on the denaturation of myoglobin. J Mol Biol 35, 567-569.
    • (1968) J Mol Biol , vol.35 , pp. 567-569
    • Schechter, A.N.1    Epstein, C.J.2
  • 7
    • 0025891257 scopus 로고
    • Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis
    • Hughson FM, Barrick D & Baldwin RL (1991) Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis. Biochemistry 30, 4113-4118.
    • (1991) Biochemistry , vol.30 , pp. 4113-4118
    • Hughson, F.M.1    Barrick, D.2    Baldwin, R.L.3
  • 9
    • 0029737827 scopus 로고    scopus 로고
    • The stability of holomyoglobin is determined by heme affinity
    • Hargrove MS & Olson JS (1996) The stability of holomyoglobin is determined by heme affinity. Biochemistry 35, 11310-11318.
    • (1996) Biochemistry , vol.35 , pp. 11310-11318
    • Hargrove, M.S.1    Olson, J.S.2
  • 10
    • 0038624089 scopus 로고    scopus 로고
    • A TyrCD1/TrpG8 hydrogen bond network and a TyrB10TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O
    • Milani M, Savard PY, Quellet H, Ascenzi P, Guertin M & Bolognesi M (2003) A TyrCD1/TrpG8 hydrogen bond network and a TyrB10TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O. Proc Natl Acad Sci USA 100, 5766-5771.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5766-5771
    • Milani, M.1    Savard, P.Y.2    Quellet, H.3    Ascenzi, P.4    Guertin, M.5    Bolognesi, M.6
  • 11
    • 15744375834 scopus 로고    scopus 로고
    • The truncated oxygen-avid hemoglobin from Bacillus subtilis. X-Ray structure and ligand binding properties
    • in press
    • Giangiacomo L, Ilari A, Boffi A, Morea V & Chiancone E (2005) The truncated oxygen-avid hemoglobin from Bacillus subtilis. X-Ray structure and ligand binding properties. J Biol Chem in press.
    • (2005) J Biol Chem
    • Giangiacomo, L.1    Ilari, A.2    Boffi, A.3    Morea, V.4    Chiancone, E.5
  • 13
    • 0037177162 scopus 로고    scopus 로고
    • Unique ligand-protein interactions in a new truncated hemoglobin from Mycobacterium tuberculosis
    • Mukai M, Savard PY, Quellet H, Guertin M & Yeh SR (2002) Unique ligand-protein interactions in a new truncated hemoglobin from Mycobacterium tuberculosis. Biochemistry 41, 3897-3905.
    • (2002) Biochemistry , vol.41 , pp. 3897-3905
    • Mukai, M.1    Savard, P.Y.2    Quellet, H.3    Guertin, M.4    Yeh, S.R.5
  • 14
    • 0034695445 scopus 로고    scopus 로고
    • A cooperative oxygen binding hemoglobin from Mycobacterium tuberculosis. Stabilization of heme ligands by a distal tyrosine residue
    • Yeh SR, Couture M, Quellet Y, Guertin M & Rousseau DL (2000) A cooperative oxygen binding hemoglobin from Mycobacterium tuberculosis. Stabilization of heme ligands by a distal tyrosine residue. J Biol Chem 21, 1679-1684.
    • (2000) J Biol Chem , vol.21 , pp. 1679-1684
    • Yeh, S.R.1    Couture, M.2    Quellet, Y.3    Guertin, M.4    Rousseau, D.L.5
  • 15
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • Sturtevant JM (1977) Heat capacity and entropy changes in processes involving proteins. Proc Natl Acad Sci USA 74, 2236-2240.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 2236-2240
    • Sturtevant, J.M.1
  • 16
    • 0034917762 scopus 로고    scopus 로고
    • Refolding kinetics of cytochrome c (551) reveals a mechanistic difference between urea and guanidine
    • Gianni S, Brunori M & Travaglini-Allocatelli C (2001) Refolding kinetics of cytochrome c (551) reveals a mechanistic difference between urea and guanidine. Protein Sci 8, 1685-1688.
    • (2001) Protein Sci , vol.8 , pp. 1685-1688
    • Gianni, S.1    Brunori, M.2    Travaglini-Allocatelli, C.3
  • 17
    • 0034867130 scopus 로고    scopus 로고
    • Cavities and packing defects in the structural dynamics of myoglobin
    • Brunori M & Gibson QH (2001) Cavities and packing defects in the structural dynamics of myoglobin. EMBO Report 8, 674-679.
    • (2001) EMBO Report , vol.8 , pp. 674-679
    • Brunori, M.1    Gibson, Q.H.2
  • 20
    • 1542287658 scopus 로고    scopus 로고
    • The absence of proximal strain in the truncated hemoglobins from Mycobacterium tuberculosis
    • Samuni U, Quellet Y, Guertin M, Friedman JM & Yeh SR (2004) The absence of proximal strain in the truncated hemoglobins from Mycobacterium tuberculosis. J Am Chem Soc 126, 2682-2683.
    • (2004) J Am Chem Soc , vol.126 , pp. 2682-2683
    • Samuni, U.1    Quellet, Y.2    Guertin, M.3    Friedman, J.M.4    Yeh, S.R.5
  • 21
    • 12344266500 scopus 로고    scopus 로고
    • Nitric oxide detoxification - A new era for bacterial globins in biotechnology?
    • Frey AD & Kallio PT (2005) Nitric oxide detoxification - a new era for bacterial globins in biotechnology? Trends Biotechnol 23, 69-73.
    • (2005) Trends Biotechnol , vol.23 , pp. 69-73
    • Frey, A.D.1    Kallio, P.T.2
  • 22
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray crystallization data in oscillation mode
    • Otwinosky Z & Minor W (1997) Processing of X-ray crystallization data in oscillation mode. Methods Enzymol 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinosky, Z.1    Minor, W.2
  • 23
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin A & Teplyakov A (1997) MOLREP: an automated program for molecular replacement. J Appl Crystallogr 30, 1022-1025.
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 26
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereochemical quality of protein structures
    • Laskowsky RA, McArthur MW, Moss DS & Thornton J (1993) Procheck: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26, 283-291.
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowsky, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thornton, J.4
  • 31
    • 0029853148 scopus 로고    scopus 로고
    • WWW-Query: An on-line retrieval system for biological sequence banks
    • Perrière G & Gouy M (1996) WWW-Query: an on-line retrieval system for biological sequence banks. Biochimie 78, 364-369.
    • (1996) Biochimie , vol.78 , pp. 364-369
    • Perrière, G.1    Gouy, M.2
  • 32
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W & Sander C (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 33
    • 0003742069 scopus 로고
    • Department of Biochemistry and Molecular Biology, University College, London
    • Hubbard SJ & Thornton JM (1993) Naccess, computer program. Department of Biochemistry and Molecular Biology, University College, London.
    • (1993) Naccess, Computer Program
    • Hubbard, S.J.1    Thornton, J.M.2
  • 35
    • 0032815529 scopus 로고    scopus 로고
    • Pentacoordinate hemin derivatives in sodium dodecyl sulfate micelles: Model systems for the assignment of the fifth ligand in ferric heme proteins
    • Boffi A, Das TK, della Longa S, Spagnolo C & Rousseau DL (1999) Pentacoordinate hemin derivatives in sodium dodecyl sulfate micelles: model systems for the assignment of the fifth ligand in ferric heme proteins. Biophys J 77, 1143-1149.
    • (1999) Biophys J , vol.77 , pp. 1143-1149
    • Boffi, A.1    Das, T.K.2    Della Longa, S.3    Spagnolo, C.4    Rousseau, D.L.5
  • 36
    • 0028168139 scopus 로고
    • Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions
    • Matouscheck A, Matthews JM, Johnson CM & Fersht A (1994) Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. Protein Engineering 7, 1089-1094.
    • (1994) Protein Engineering , vol.7 , pp. 1089-1094
    • Matouscheck, A.1    Matthews, J.M.2    Johnson, C.M.3    Fersht, A.4
  • 37
    • 0027155577 scopus 로고
    • Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
    • Clarke J & Fersht AR (1993) Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation. Biochemistry 32, 4322-4327.
    • (1993) Biochemistry , vol.32 , pp. 4322-4327
    • Clarke, J.1    Fersht, A.R.2
  • 38
    • 0038101540 scopus 로고    scopus 로고
    • Direct measurement of equilibrium constants for high-affinity hemoglobins
    • Kundu S, Premer SA, Hoy JA, Trent JT III & Hargrove MS (2003) Direct measurement of equilibrium constants for high-affinity hemoglobins. Biophys J 84, 3931-3940.
    • (2003) Biophys J , vol.84 , pp. 3931-3940
    • Kundu, S.1    Premer, S.A.2    Hoy, J.A.3    Trent III, J.T.4    Hargrove, M.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.