메뉴 건너뛰기




Volumn 52, Issue 3, 2013, Pages 447-455

Dynamic factors affecting gaseous ligand binding in an artificial oxygen transport protein

Author keywords

[No Author keywords available]

Indexed keywords

ARTIFICIAL PROTEINS; BINDING RATE; CYTOGLOBIN; DEGREE OF PENETRATION; DEUTERIUM EXCHANGE; DISTAL HISTIDINE; DYNAMIC FACTORS; FERROUS STATE; FREEDOM OF MOTION; HEME BINDING; HEME IRON; HEMOPROTEINS; HISTIDINE LIGANDS; HISTIDINE RESIDUES; LIGAND BINDING; MUTANT PROTEINS; NEUROGLOBIN; OXYGEN AFFINITY; OXYGEN TRANSPORT; PROTEIN CORE; PROTEIN DYNAMICS; SIDE-CHAINS; WATER PENETRATION;

EID: 84872781603     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301066z     Document Type: Article
Times cited : (15)

References (26)
  • 1
    • 10444234271 scopus 로고    scopus 로고
    • Cytochrome c oxidase, ligands and electrons
    • Brunori, M., Giuffre, A., and Sarti, P. (2005) Cytochrome c oxidase, ligands and electrons J. Inorg. Biochem. 99, 324-336
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 324-336
    • Brunori, M.1    Giuffre, A.2    Sarti, P.3
  • 2
    • 0035918528 scopus 로고    scopus 로고
    • A model for ligand binding to hexacoordinate hemoglobins
    • Trent, J. T., Hvitved, A. N., and Hargrove, M. S. (2001) A model for ligand binding to hexacoordinate hemoglobins Biochemistry 40, 6155-6163
    • (2001) Biochemistry , vol.40 , pp. 6155-6163
    • Trent, J.T.1    Hvitved, A.N.2    Hargrove, M.S.3
  • 4
  • 5
    • 0014251790 scopus 로고
    • Metalloenzymes: Entatic nature of their active sites
    • Vallee, B. L. and Williams, R. J. P. (1968) Metalloenzymes: Entatic nature of their active sites Proc. Natl. Acad. Sci. U.S.A. 59, 498-505
    • (1968) Proc. Natl. Acad. Sci. U.S.A. , vol.59 , pp. 498-505
    • Vallee, B.L.1    Williams, R.J.P.2
  • 8
    • 0034724887 scopus 로고    scopus 로고
    • Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin): The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis
    • Gardner, A. M., Martin, L. A., Gardner, P. R., Dou, Y., and Olson, J. S. (2000) Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin): The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis J. Biol. Chem. 275, 12581-12589
    • (2000) J. Biol. Chem. , vol.275 , pp. 12581-12589
    • Gardner, A.M.1    Martin, L.A.2    Gardner, P.R.3    Dou, Y.4    Olson, J.S.5
  • 10
    • 0033729233 scopus 로고    scopus 로고
    • A flash photolysis method to characterize hexacoordinate hemoglobin kinetics
    • Hargrove, M. S. (2000) A flash photolysis method to characterize hexacoordinate hemoglobin kinetics Biophys. J. 79, 2733-2738
    • (2000) Biophys. J. , vol.79 , pp. 2733-2738
    • Hargrove, M.S.1
  • 11
    • 59149104856 scopus 로고    scopus 로고
    • Controlling complexity and water penetration in functional de novo protein design
    • Anderson, J. L. R., Koder, R. L., Moser, C. C., and Dutton, P. L. (2008) Controlling complexity and water penetration in functional de novo protein design Biochem. Soc. Trans. 36, 1106-1111
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1106-1111
    • Anderson, J.L.R.1    Koder, R.L.2    Moser, C.C.3    Dutton, P.L.4
  • 12
    • 42949114923 scopus 로고    scopus 로고
    • Measurement of distal histidine coordination equilibrium and kinetics in hexacoordinate hemoglobins
    • In, pp, Elsevier Academic Press Inc. San Diego. - 378
    • Smagghe, B. J., Halder, P., and Hargrove, M. S. (2008) Measurement of distal histidine coordination equilibrium and kinetics in hexacoordinate hemoglobins. In Globins and Other Nitric Oxide-Reactive Proteins, Part A, pp 359-378, Elsevier Academic Press Inc., San Diego.
    • (2008) Globins and Other Nitric Oxide-Reactive Proteins, Part A , pp. 359
    • Smagghe, B.J.1    Halder, P.2    Hargrove, M.S.3
  • 13
    • 0008231311 scopus 로고
    • Outer-sphere electron transfer reactions of the isolated active-site heme octapeptide from cytochrome-C
    • McLendon, G. and Smith, M. (1982) Outer-sphere electron transfer reactions of the isolated active-site heme octapeptide from cytochrome-C Inorg. Chem. 21, 847-850
    • (1982) Inorg. Chem. , vol.21 , pp. 847-850
    • McLendon, G.1    Smith, M.2
  • 16
    • 0038682731 scopus 로고    scopus 로고
    • 1H NMR characterization of equilibrium heme orientational disorder with functional consequences in mouse neuroglobin
    • 1H NMR characterization of equilibrium heme orientational disorder with functional consequences in mouse neuroglobin J. Am. Chem. Soc. 125, 8080-8081
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8080-8081
    • Du, W.H.1    Syvitski, R.2    Dewilde, S.3    Moens, L.4    La Mar, G.N.5
  • 17
    • 0032837780 scopus 로고    scopus 로고
    • Synthetic models for hemoglobin and myoglobin
    • Collman, J. P. and Fu, L. (1999) Synthetic models for hemoglobin and myoglobin Acc. Chem. Res. 32, 455-463
    • (1999) Acc. Chem. Res. , vol.32 , pp. 455-463
    • Collman, J.P.1    Fu, L.2
  • 18
    • 1842631425 scopus 로고    scopus 로고
    • The HP-1 maquette: From an apoprotein structure to a structured hemoprotein designed to promote redox-coupled proton exchange
    • Huang, S. S., Koder, R. L., Lewis, M., Wand, A. J., and Dutton, P. L. (2004) The HP-1 maquette: From an apoprotein structure to a structured hemoprotein designed to promote redox-coupled proton exchange Proc. Natl. Acad. Sci. U.S.A. 101, 5536-5541
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 5536-5541
    • Huang, S.S.1    Koder, R.L.2    Lewis, M.3    Wand, A.J.4    Dutton, P.L.5
  • 19
  • 20
    • 0033871781 scopus 로고    scopus 로고
    • Protein folding intermediates and pathways studied by hydrogen exchange
    • Englander, S. W. (2000) Protein folding intermediates and pathways studied by hydrogen exchange Annu. Rev. Biophys. Biomol. Struct. 29, 213-238
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 213-238
    • Englander, S.W.1
  • 21
    • 0015514905 scopus 로고
    • NMR studies of selectively hindered internal motion of substrate analogs at the active site of pyruvate kinase
    • Nowak, T. and Mildvan, A. S. (1972) NMR studies of selectively hindered internal motion of substrate analogs at the active site of pyruvate kinase Biochemistry 11, 2813-2819
    • (1972) Biochemistry , vol.11 , pp. 2813-2819
    • Nowak, T.1    Mildvan, A.S.2
  • 22
    • 0035904453 scopus 로고    scopus 로고
    • Biological relevance of metal binding before protein folding
    • Pozdnyakova, I. and Wittung-Stafshede, P. (2001) Biological relevance of metal binding before protein folding J. Am. Chem. Soc. 123, 10135-10136
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 10135-10136
    • Pozdnyakova, I.1    Wittung-Stafshede, P.2
  • 25
    • 78650883017 scopus 로고    scopus 로고
    • Computational design of intermolecular stability and specificity in protein self-assembly
    • In (Johnson, M. L. and Brand, L. Eds.) pp, Elsevier, Amsterdam. - 593
    • Nanda, V., Zahid, S., Xu, F., and Levine, D. (2011) Computational design of intermolecular stability and specificity in protein self-assembly. In Methods in Enzymology, Volume 487: Computer Methods, Part C (Johnson, M. L. and Brand, L., Eds.) pp 575-593, Elsevier, Amsterdam.
    • (2011) Methods in Enzymology, Volume 487: Computer Methods, Part C , pp. 575
    • Nanda, V.1    Zahid, S.2    Xu, F.3    Levine, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.