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Volumn 47, Issue 7, 2008, Pages 2087-2098

Novel heme ligand displacement by CO in the soluble hemophore HasA and its proximal ligand mutants: Implications for heme uptake and release

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; COMPLEXATION; HYDROGEN BONDS; VIBRATIONAL SPECTRA;

EID: 39649113840     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7019518     Document Type: Article
Times cited : (32)

References (61)
  • 1
    • 0028170732 scopus 로고
    • Iron acquisition from heme and hemoglobin by a Serratia marcescens extracellular protein
    • Létoffé, S., Ghigo, J. M., and Wandersman, C. (1994) Iron acquisition from heme and hemoglobin by a Serratia marcescens extracellular protein, Proc. Natl. Acad. Sci. U.S.A. 91, 9876-9880.
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 9876-9880
    • Létoffé, S.1    Ghigo, J.M.2    Wandersman, C.3
  • 2
    • 0029056415 scopus 로고
    • Protein secretion by hybrid bacterial ABC-transporters: Specific functions of the membrane ATPase and the membrane fusion protein
    • Binet, R., and Wandersman, C. (1995) Protein secretion by hybrid bacterial ABC-transporters: Specific functions of the membrane ATPase and the membrane fusion protein, EMBO J. 14, 2298-2306.
    • (1995) EMBO J , vol.14 , pp. 2298-2306
    • Binet, R.1    Wandersman, C.2
  • 3
    • 1842326840 scopus 로고    scopus 로고
    • A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli
    • Ghigo, J. M., Letoffe, S., and Wandersman, C. (1997) A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli, J. Bacteriol. 179, 3572-3579.
    • (1997) J. Bacteriol , vol.179 , pp. 3572-3579
    • Ghigo, J.M.1    Letoffe, S.2    Wandersman, C.3
  • 4
    • 0029806326 scopus 로고    scopus 로고
    • Cloning of the Serratia marcescens hasF gene encoding the Has ABC exporter outer membrane component: A TolC analogue
    • Binet, R., and Wandersman, C. (1996) Cloning of the Serratia marcescens hasF gene encoding the Has ABC exporter outer membrane component: A TolC analogue, Mol. Microbiol. 22, 265-273.
    • (1996) Mol. Microbiol , vol.22 , pp. 265-273
    • Binet, R.1    Wandersman, C.2
  • 5
    • 0031775913 scopus 로고    scopus 로고
    • Isolation and characterization of an extracellular heme-binding protein from Pseudomonas aeruginosa that shares function and sequence similarities with the Serratia marcescens HasA hemophore
    • Létoffé, S., Redeker, V., and Wandersman, C. (1998) Isolation and characterization of an extracellular heme-binding protein from Pseudomonas aeruginosa that shares function and sequence similarities with the Serratia marcescens HasA hemophore, Mol. Microbiol. 28, 1223-1234.
    • (1998) Mol. Microbiol , vol.28 , pp. 1223-1234
    • Létoffé, S.1    Redeker, V.2    Wandersman, C.3
  • 7
    • 0034773143 scopus 로고    scopus 로고
    • Identification and characterization of the hemophore-dependent heme acquisition system of Yersinia pestis
    • Rossi, M. S., Fetherston, J. D., Letoffe, S., Carniel, E., Perry, R. D., and Ghigo, J. M. (2001) Identification and characterization of the hemophore-dependent heme acquisition system of Yersinia pestis, Infect. Immun. 69, 6707-6717.
    • (2001) Infect. Immun , vol.69 , pp. 6707-6717
    • Rossi, M.S.1    Fetherston, J.D.2    Letoffe, S.3    Carniel, E.4    Perry, R.D.5    Ghigo, J.M.6
  • 8
    • 0032763117 scopus 로고    scopus 로고
    • Cloning and characterization of the Pseudomonas fluorescens ATP-binding cassette exporter, HasDEF, for the heme acquisition protein HasA
    • Idei, A., Kawai, E., Akatsuka, H., and Omori, K. (1999) Cloning and characterization of the Pseudomonas fluorescens ATP-binding cassette exporter, HasDEF, for the heme acquisition protein HasA, J. Bacteriol. 181, 7545-7551.
    • (1999) J. Bacteriol , vol.181 , pp. 7545-7551
    • Idei, A.1    Kawai, E.2    Akatsuka, H.3    Omori, K.4
  • 9
    • 39649105297 scopus 로고    scopus 로고
    • www.sanger.ac.uk/Projects/E_carotovora, 2006.
    • (2006)
  • 10
    • 0030946074 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular heme-binding protein, HasA, involved in heme iron acquisition
    • Izadi, N., Henry, Y., Haladjian, J., Goldberg, M. E., Wandersman, C., Delepierre, M., and Lecroisey, A. (1997) Purification and characterization of an extracellular heme-binding protein, HasA, involved in heme iron acquisition, Biochemistry 36, 7050-7057.
    • (1997) Biochemistry , vol.36 , pp. 7050-7057
    • Izadi, N.1    Henry, Y.2    Haladjian, J.3    Goldberg, M.E.4    Wandersman, C.5    Delepierre, M.6    Lecroisey, A.7
  • 11
    • 33845892486 scopus 로고    scopus 로고
    • The crystal structure of the secreted dimeric form of the hemophore HasA reveals a domain swapping with an exchanged heme ligand
    • Czjzek, M., Letoffe, S., Wandersman, C., Delepierre, M., Lecroisey, A., and Izadi-Pruneyre, N. (2007) The crystal structure of the secreted dimeric form of the hemophore HasA reveals a domain swapping with an exchanged heme ligand, J. Mol. Biol. 365, 1176-1186.
    • (2007) J. Mol. Biol , vol.365 , pp. 1176-1186
    • Czjzek, M.1    Letoffe, S.2    Wandersman, C.3    Delepierre, M.4    Lecroisey, A.5    Izadi-Pruneyre, N.6
  • 14
    • 0024555936 scopus 로고
    • Characteristics in tyrosine coordinations of four hemoglobins M probed by resonance Raman spectroscopy
    • Nagai, M., Yoneyama, Y., and Kitagawa, T. (1989) Characteristics in tyrosine coordinations of four hemoglobins M probed by resonance Raman spectroscopy, Biochemistry 28, 2418-2422.
    • (1989) Biochemistry , vol.28 , pp. 2418-2422
    • Nagai, M.1    Yoneyama, Y.2    Kitagawa, T.3
  • 15
    • 0024975103 scopus 로고
    • Structural and electronic properties of the liver fluke heme cavity by nuclear magnetic resonance and optical spectroscopy. Evidence for a distal tyrosine residue in a normally functioning hemoglobin
    • Lecomte, J. T., Smit, J. D., Winterhalter, K. H., and La Mar, G. N. (1989) Structural and electronic properties of the liver fluke heme cavity by nuclear magnetic resonance and optical spectroscopy. Evidence for a distal tyrosine residue in a normally functioning hemoglobin, J. Mol. Biol. 209, 235-247.
    • (1989) J. Mol. Biol , vol.209 , pp. 235-247
    • Lecomte, J.T.1    Smit, J.D.2    Winterhalter, K.H.3    La Mar, G.N.4
  • 16
    • 0025167226 scopus 로고
    • Hemoglobins of the Lucina pectinata/bacteria symbiosis. II. An electron paramagnetic resonance and optical spectral study of the ferric proteins
    • Kraus, D. W., Wittenberg, J. B., Lu, J. F., and Peisach, J. (1990) Hemoglobins of the Lucina pectinata/bacteria symbiosis. II. An electron paramagnetic resonance and optical spectral study of the ferric proteins, J. Biol. Chem. 265, 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
  • 17
    • 0033576249 scopus 로고    scopus 로고
    • Identification of the ligands to the ferric heme of Chlamydomonas chloroplast hemoglobin: Evidence for ligation of tyrosine-63 (B10) to the heme
    • Das, T. K., Couture, M., Lee, H. C., Peisach, J., Rousseau, D. L., Wittenberg, B. A., Wittenberg, J. B., and Guertin, M. (1999) Identification of the ligands to the ferric heme of Chlamydomonas chloroplast hemoglobin: Evidence for ligation of tyrosine-63 (B10) to the heme, Biochemistry 38, 15360-15368.
    • (1999) Biochemistry , vol.38 , pp. 15360-15368
    • Das, T.K.1    Couture, M.2    Lee, H.C.3    Peisach, J.4    Rousseau, D.L.5    Wittenberg, B.A.6    Wittenberg, J.B.7    Guertin, M.8
  • 18
    • 0027505784 scopus 로고
    • Roles of proximal ligand in heme proteins: Replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase
    • Adachi, S., Nagano, S., Ishimori, K., Watanabe, Y., Morishima, I., Egawa, T., Kitagawa, T., and Makino, R. (1993) Roles of proximal ligand in heme proteins: Replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase, Biochemistry 32, 241-252.
    • (1993) Biochemistry , vol.32 , pp. 241-252
    • Adachi, S.1    Nagano, S.2    Ishimori, K.3    Watanabe, Y.4    Morishima, I.5    Egawa, T.6    Kitagawa, T.7    Makino, R.8
  • 22
    • 0034908388 scopus 로고    scopus 로고
    • Haemophore-mediated bacterial haem transport: Evidence for a common or overlapping site for haem-free and haem-loaded haemophore on its specific outer membrane receptor
    • Létoffé, S., Deniau, C., Wolff, N., Dassa, E., Delepelaire, P., Lecroisey, A., and Wandersman, C. (2001) Haemophore-mediated bacterial haem transport: Evidence for a common or overlapping site for haem-free and haem-loaded haemophore on its specific outer membrane receptor, Mol. Microbiol. 41, 439-450.
    • (2001) Mol. Microbiol , vol.41 , pp. 439-450
    • Létoffé, S.1    Deniau, C.2    Wolff, N.3    Dassa, E.4    Delepelaire, P.5    Lecroisey, A.6    Wandersman, C.7
  • 23
    • 10444269414 scopus 로고    scopus 로고
    • CO as a vibrational probe of heme protein active sites
    • Spiro, T. G., and Wasbotten, I. H. (2005) CO as a vibrational probe of heme protein active sites, J. Inorg. Biochem. 99, 34-44.
    • (2005) J. Inorg. Biochem , vol.99 , pp. 34-44
    • Spiro, T.G.1    Wasbotten, I.H.2
  • 24
    • 0033806397 scopus 로고    scopus 로고
    • Role of the axial ligand in heme-CO backbonding; DFT analysis of vibrational data
    • Vogel, K. M., Kozlowski, P. M., Zgierski, M. Z., and Spiro, T. G. (2000) Role of the axial ligand in heme-CO backbonding; DFT analysis of vibrational data, Inorg. Chim. Acta 297, 11-17.
    • (2000) Inorg. Chim. Acta , vol.297 , pp. 11-17
    • Vogel, K.M.1    Kozlowski, P.M.2    Zgierski, M.Z.3    Spiro, T.G.4
  • 25
    • 0028223077 scopus 로고
    • How far can proteins bend the FeCO unit? Distal polar and steric effects in heme proteins and models
    • Ray, G. B., Li, X. Y., Ibers, J. A., Sessler, J. L., and Spiro, T. G. (1994) How far can proteins bend the FeCO unit? Distal polar and steric effects in heme proteins and models, J. Am. Chem. Soc. 116, 162-176.
    • (1994) J. Am. Chem. Soc , vol.116 , pp. 162-176
    • Ray, G.B.1    Li, X.Y.2    Ibers, J.A.3    Sessler, J.L.4    Spiro, T.G.5
  • 27
    • 3142615826 scopus 로고    scopus 로고
    • Heme structures of five variants of hemoglobin M probed by resonance Raman spectroscopy
    • Jin, Y., Nagai, M., Nagai, Y., Nagatomo, S., and Kitagawa, T. (2004) Heme structures of five variants of hemoglobin M probed by resonance Raman spectroscopy, Biochemistry 43, 8517-8527.
    • (2004) Biochemistry , vol.43 , pp. 8517-8527
    • Jin, Y.1    Nagai, M.2    Nagai, Y.3    Nagatomo, S.4    Kitagawa, T.5
  • 28
    • 0025776927 scopus 로고
    • Unusual carbon monoxide bonding geometry in abnormal subunits of hemoglobin M Boston and hemoglobin M Saskatoon
    • Nagai, M., Yoneyama, Y., and Kitagawa, T. (1991) Unusual carbon monoxide bonding geometry in abnormal subunits of hemoglobin M Boston and hemoglobin M Saskatoon, Biochemistry 30, 6495-6503.
    • (1991) Biochemistry , vol.30 , pp. 6495-6503
    • Nagai, M.1    Yoneyama, Y.2    Kitagawa, T.3
  • 29
    • 0026677841 scopus 로고
    • Resonance Raman studies of the carbonmonoxy form of catalase. Evidence for and effects of phenolate ligation
    • Hu, S., and Kincaid, J. R. (1992) Resonance Raman studies of the carbonmonoxy form of catalase. Evidence for and effects of phenolate ligation, FEBS Lett. 314, 293-296.
    • (1992) FEBS Lett , vol.314 , pp. 293-296
    • Hu, S.1    Kincaid, J.R.2
  • 31
    • 0024962323 scopus 로고
    • Comparative spectral analysis of mammalian, fungal, and bacterial catalases. Resonance Raman evidence for iron-tyrosinate coordination
    • Sharma, K. D., Andersson, L. A., Loehr, T. M., Terner, J., and Goff, H. M. (1989) Comparative spectral analysis of mammalian, fungal, and bacterial catalases. Resonance Raman evidence for iron-tyrosinate coordination, J. Biol. Chem. 264, 12772-12779.
    • (1989) J. Biol. Chem , vol.264 , pp. 12772-12779
    • Sharma, K.D.1    Andersson, L.A.2    Loehr, T.M.3    Terner, J.4    Goff, H.M.5
  • 32
    • 28144461488 scopus 로고    scopus 로고
    • Excited state property of hardly photodissociable Heme-CO adduct studied by time-dependent density functional theory
    • Ohta, T., Pal, B., and Kitagawa, T. (2005) Excited state property of hardly photodissociable Heme-CO adduct studied by time-dependent density functional theory, J. Phys. Chem. B 109, 21110-21117.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 21110-21117
    • Ohta, T.1    Pal, B.2    Kitagawa, T.3
  • 33
    • 0035799328 scopus 로고    scopus 로고
    • Resonance Raman studies of cytochrome c′ support the binding of NO and CO to opposite sides of the heme: Implications for ligand discrimination in heme-based sensors
    • Andrew, C. R., Green, E. L., Lawson, D. M., and Eady, R. R. (2001) Resonance Raman studies of cytochrome c′ support the binding of NO and CO to opposite sides of the heme: Implications for ligand discrimination in heme-based sensors, Biochemistry 40, 4115-4122.
    • (2001) Biochemistry , vol.40 , pp. 4115-4122
    • Andrew, C.R.1    Green, E.L.2    Lawson, D.M.3    Eady, R.R.4
  • 34
    • 0037133134 scopus 로고    scopus 로고
    • Six- to five-coordinate heme-nitrosyl conversion in cytochrome c′ and its relevance to guanylate cyclase
    • Andrew, C. R., George, S. J., Lawson, D. M., and Eady, R. R. (2002) Six- to five-coordinate heme-nitrosyl conversion in cytochrome c′ and its relevance to guanylate cyclase, Biochemistry 41, 2353-2360.
    • (2002) Biochemistry , vol.41 , pp. 2353-2360
    • Andrew, C.R.1    George, S.J.2    Lawson, D.M.3    Eady, R.R.4
  • 35
    • 0029942847 scopus 로고    scopus 로고
    • Evidence for a proximal histidine interaction in the structure of cytochromes c′ in solution: A resonance Raman study
    • Othman, S., Richaud, P., Verméglio, A., and Desbois, A. (1996) Evidence for a proximal histidine interaction in the structure of cytochromes c′ in solution: A resonance Raman study, Biochemistry 35, 9224-9234.
    • (1996) Biochemistry , vol.35 , pp. 9224-9234
    • Othman, S.1    Richaud, P.2    Verméglio, A.3    Desbois, A.4
  • 36
    • 0018792074 scopus 로고
    • Assignment of the iron-nitrogen (His F8) stretching band in the resonance raman spectra of deoxymyoglobin
    • Kitagawa, T., Nagai, K., and Tsubaki, M. (1979) Assignment of the iron-nitrogen (His F8) stretching band in the resonance raman spectra of deoxymyoglobin, FEBS Lett. 104, 376-378.
    • (1979) FEBS Lett , vol.104 , pp. 376-378
    • Kitagawa, T.1    Nagai, K.2    Tsubaki, M.3
  • 37
    • 0001244916 scopus 로고
    • Differences in iron(II)-Ne-(His-F8) stretching frequencies between deoxyhemoglobins in the two alternative quaternary structures
    • Nagai, K., and Kitagawa, T. (1980) Differences in iron(II)-Ne-(His-F8) stretching frequencies between deoxyhemoglobins in the two alternative quaternary structures, Proc. Natl. Acad. Sci. U.S.A. 77, 2033-2037.
    • (1980) Proc. Natl. Acad. Sci. U.S.A , vol.77 , pp. 2033-2037
    • Nagai, K.1    Kitagawa, T.2
  • 38
    • 0019887886 scopus 로고
    • Structural implication of the heme-linked ionization of horseradish peroxidase probed by the iron-histidine stretching Raman line
    • Teraoka, J., and Kitagawa, T. (1981) Structural implication of the heme-linked ionization of horseradish peroxidase probed by the iron-histidine stretching Raman line, J. Biol. Chem. 256, 3969-3977.
    • (1981) J. Biol. Chem , vol.256 , pp. 3969-3977
    • Teraoka, J.1    Kitagawa, T.2
  • 40
    • 33845278516 scopus 로고
    • Is bound carbonyl linear or bent in heme proteins? Evidence from resonance Raman and infrared spectroscopic data
    • Li, X. Y., and Spiro, T. G. (1988) Is bound carbonyl linear or bent in heme proteins? Evidence from resonance Raman and infrared spectroscopic data, J. Am. Chem. Soc. 110, 6024-6033.
    • (1988) J. Am. Chem. Soc , vol.110 , pp. 6024-6033
    • Li, X.Y.1    Spiro, T.G.2
  • 41
    • 0023759477 scopus 로고
    • Cytochrome c peroxidase mutant active site structures probed by resonance Raman and infrared signatures of the CO adducts
    • Smulevich, G., Mauro, J. M., Fishel, L. A., English, A. M., Kraut, J., and Spiro, T. G. (1988) Cytochrome c peroxidase mutant active site structures probed by resonance Raman and infrared signatures of the CO adducts, Biochemistry 27, 5486-5492.
    • (1988) Biochemistry , vol.27 , pp. 5486-5492
    • Smulevich, G.1    Mauro, J.M.2    Fishel, L.A.3    English, A.M.4    Kraut, J.5    Spiro, T.G.6
  • 42
    • 0020484765 scopus 로고
    • Resonance Raman investigation of carbon monoxide bonding in (carbon monoxy)hemoglobin and -myoglobin: Detection of iron-carbon monoxide stretching and iron-carbon-oxygen bending vibrations and influence of the quaternary structure change
    • Tsubaki, M., Srivastava, R. B., and Yu, N. T. (1982) Resonance Raman investigation of carbon monoxide bonding in (carbon monoxy)hemoglobin and -myoglobin: Detection of iron-carbon monoxide stretching and iron-carbon-oxygen bending vibrations and influence of the quaternary structure change, Biochemistry 21, 1132-1140.
    • (1982) Biochemistry , vol.21 , pp. 1132-1140
    • Tsubaki, M.1    Srivastava, R.B.2    Yu, N.T.3
  • 43
    • 0027947216 scopus 로고
    • Heme-heme oxygenase complex: Structure and properties of the catalytic site from resonance Raman scattering
    • Takahashi, S., Wang, J., Rousseau, D. L., Ishikawa, K., Yoshida, T., Takeuchi, N., and Ikeda-Saito, M. (1994) Heme-heme oxygenase complex: Structure and properties of the catalytic site from resonance Raman scattering, Biochemistry 33, 5531-5538.
    • (1994) Biochemistry , vol.33 , pp. 5531-5538
    • Takahashi, S.1    Wang, J.2    Rousseau, D.L.3    Ishikawa, K.4    Yoshida, T.5    Takeuchi, N.6    Ikeda-Saito, M.7
  • 44
    • 10444225424 scopus 로고    scopus 로고
    • Interactions of soluble guanylate cyclase with diatomics as probed by resonance Raman spectroscopy
    • Pal, B., and Kitagawa, T. (2005) Interactions of soluble guanylate cyclase with diatomics as probed by resonance Raman spectroscopy, J. Inorg. Biochem. 99, 267-279.
    • (2005) J. Inorg. Biochem , vol.99 , pp. 267-279
    • Pal, B.1    Kitagawa, T.2
  • 45
    • 0037134550 scopus 로고    scopus 로고
    • Resonance Raman and ligand binding studies of the oxygen-sensing signal transducer protein HemAT from Bacillus subtilis
    • Aono, S., Kato, T., Matsuki, M., Nakajima, H., Ohta, T., Uchida, T., and Kitagawa, T. (2002) Resonance Raman and ligand binding studies of the oxygen-sensing signal transducer protein HemAT from Bacillus subtilis, J. Biol. Chem. 277, 13528-13538.
    • (2002) J. Biol. Chem , vol.277 , pp. 13528-13538
    • Aono, S.1    Kato, T.2    Matsuki, M.3    Nakajima, H.4    Ohta, T.5    Uchida, T.6    Kitagawa, T.7
  • 46
    • 0032168882 scopus 로고    scopus 로고
    • Functional implications of the proximal hydrogen-bonding network in myoglobin: A resonance Raman and kinetic study of Leu89, Ser92, His97, and F-helix swap mutants
    • Peterson, E. S., Friedman, J. M., Chien, E. Y. T., and Sligar, S. G. (1998) Functional implications of the proximal hydrogen-bonding network in myoglobin: A resonance Raman and kinetic study of Leu89, Ser92, His97, and F-helix swap mutants, Biochemistry 37, 12301-12319.
    • (1998) Biochemistry , vol.37 , pp. 12301-12319
    • Peterson, E.S.1    Friedman, J.M.2    Chien, E.Y.T.3    Sligar, S.G.4
  • 48
    • 0035042514 scopus 로고    scopus 로고
    • pH-Dependent structural changes at the heme-copper binuclear center of cytochrome c oxidase
    • Das, T. K., Tomson, F. L., Gennis, R. B., Gordon, M., and Rousseau, D. L. (2001) pH-Dependent structural changes at the heme-copper binuclear center of cytochrome c oxidase, Biophys. J. 80, 2039-2045.
    • (2001) Biophys. J , vol.80 , pp. 2039-2045
    • Das, T.K.1    Tomson, F.L.2    Gennis, R.B.3    Gordon, M.4    Rousseau, D.L.5
  • 50
    • 0028180138 scopus 로고
    • Resonance Raman and Fourier transform infrared studies on the subunit I histidine mutants of the cytochrome bo complex in Escherichia coli. Molecular structure of redox metal centers
    • Uno, T., Mogi, T., Tsubaki, M., Nishimura, Y., and Anraku, Y. (1994) Resonance Raman and Fourier transform infrared studies on the subunit I histidine mutants of the cytochrome bo complex in Escherichia coli. Molecular structure of redox metal centers, J. Biol. Chem. 269, 11912-11920.
    • (1994) J. Biol. Chem , vol.269 , pp. 11912-11920
    • Uno, T.1    Mogi, T.2    Tsubaki, M.3    Nishimura, Y.4    Anraku, Y.5
  • 51
    • 8344236821 scopus 로고    scopus 로고
    • SOUL in mouse eyes is a new hexameric heme-binding protein with characteristic optical absorption, resonance Raman spectral, and heme-binding properties
    • Sato, E., Sagami, I., Uchida, T., Sato, A., Kitagawa, T., Igarashi, J., and Shimizu, T. (2004) SOUL in mouse eyes is a new hexameric heme-binding protein with characteristic optical absorption, resonance Raman spectral, and heme-binding properties, Biochemistry 43, 14189-14198.
    • (2004) Biochemistry , vol.43 , pp. 14189-14198
    • Sato, E.1    Sagami, I.2    Uchida, T.3    Sato, A.4    Kitagawa, T.5    Igarashi, J.6    Shimizu, T.7
  • 53
  • 54
    • 17744362896 scopus 로고    scopus 로고
    • CO rebinding to protoheme: Investigations of the proximal and distal contributions to the geminate rebinding barrier
    • Ye, X., Yu, A., Georgiev, G. Y., Gruia, F., Ionascu, D., Cao, W., Sage, J. T., and Champion, P. M. (2005) CO rebinding to protoheme: Investigations of the proximal and distal contributions to the geminate rebinding barrier, J. Am. Chem. Soc. 127, 5854-5861.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 5854-5861
    • Ye, X.1    Yu, A.2    Georgiev, G.Y.3    Gruia, F.4    Ionascu, D.5    Cao, W.6    Sage, J.T.7    Champion, P.M.8
  • 56
    • 0034635333 scopus 로고    scopus 로고
    • Active and inhibited human catalase structures: Ligand and NADPH binding and catalytic mechanism
    • Putnam, C. D., Arvai, A. S., Bourne, Y., and Tainer, J. A. (2000) Active and inhibited human catalase structures: Ligand and NADPH binding and catalytic mechanism, J. Mol. Biol. 296, 295-309.
    • (2000) J. Mol. Biol , vol.296 , pp. 295-309
    • Putnam, C.D.1    Arvai, A.S.2    Bourne, Y.3    Tainer, J.A.4
  • 57
    • 0034329425 scopus 로고    scopus 로고
    • Unprecedented proximal binding of nitric oxide to heme: Implications for guanylate cyclase
    • Lawson, D. M., Stevenson, C. E. M., Andrew, C. R., and Eady, R. R. (2000) Unprecedented proximal binding of nitric oxide to heme: Implications for guanylate cyclase, EMBO J. 19, 5661-5671.
    • (2000) EMBO J , vol.19 , pp. 5661-5671
    • Lawson, D.M.1    Stevenson, C.E.M.2    Andrew, C.R.3    Eady, R.R.4
  • 58
    • 0043127340 scopus 로고    scopus 로고
    • A novel kinetic trap for NO release from cytochrome c′: A possible mechanism for NO release from activated soluble guanylate cyclase
    • Andrew, C. R., Rodgers, K. R., and Eady, R. R. (2003) A novel kinetic trap for NO release from cytochrome c′: A possible mechanism for NO release from activated soluble guanylate cyclase, J. Am. Chem. Soc. 125, 9548-9549.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 9548-9549
    • Andrew, C.R.1    Rodgers, K.R.2    Eady, R.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.