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Volumn 47, Issue 34, 2008, Pages 8874-8884

Arg97 at the heme-distal side of the isolated heme-bound PAS domain of a heme-based oxygen sensor from Escherichia coli (Ec DOS) plays critical roles in autoxidation and binding to gases, particularly O2

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; NONMETALS; OXYGEN; PORPHYRINS;

EID: 50149095403     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800248c     Document Type: Article
Times cited : (40)

References (37)
  • 1
    • 33344477903 scopus 로고    scopus 로고
    • Structure-function relationships of Ec DOS, a heme-regulated phosphodiesterase from Escherichia coli
    • Sasakura, Y., Yoshimura-Suzuki, T., Kurokawa, H., and Shimizu, T. (2006) Structure-function relationships of Ec DOS, a heme-regulated phosphodiesterase from Escherichia coli. Acc. Chem. Res. 39, 37-43.
    • (2006) Acc. Chem. Res , vol.39 , pp. 37-43
    • Sasakura, Y.1    Yoshimura-Suzuki, T.2    Kurokawa, H.3    Shimizu, T.4
  • 2
    • 34547137430 scopus 로고    scopus 로고
    • Critical Role of the Heme Axial Ligand, Met95, in Locking Catalysis of the Phosphodiesterase from Escherichia coli (Ec DOS) toward Cyclic di-GMP
    • Tanaka, A., Takahashi, H., and Shimizu, T. (2007) Critical Role of the Heme Axial Ligand, Met95, in Locking Catalysis of the Phosphodiesterase from Escherichia coli (Ec DOS) toward Cyclic di-GMP. J. Biol. Chem. 282, 21301-21307.
    • (2007) J. Biol. Chem , vol.282 , pp. 21301-21307
    • Tanaka, A.1    Takahashi, H.2    Shimizu, T.3
  • 3
    • 10444268892 scopus 로고    scopus 로고
    • Heme-based sensors: Defining characteristics, recent developments, and regulatory hypothesis
    • Gilles-Gonzalez, M. A., and Gonzalez, G. (2005) Heme-based sensors: Defining characteristics, recent developments, and regulatory hypothesis. J. Inorg. Biochem. 99, 1-22.
    • (2005) J. Inorg. Biochem , vol.99 , pp. 1-22
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2
  • 4
    • 24344498616 scopus 로고    scopus 로고
    • Mechanism for transduction of the ligand-binding signal in heme-based gas sensory proteins revealed by resonance Raman spectroscopy
    • Uchida, T., and Kitagawa, T. (2005) Mechanism for transduction of the ligand-binding signal in heme-based gas sensory proteins revealed by resonance Raman spectroscopy. Acc. Chem. Res. 38, 662-670.
    • (2005) Acc. Chem. Res , vol.38 , pp. 662-670
    • Uchida, T.1    Kitagawa, T.2
  • 5
    • 2442624510 scopus 로고    scopus 로고
    • A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor
    • Kurokawa, H., Lee, D. S., Watanabe, M., Sagami, I., Mikami, B., Raman, C. S., and Shimizu, T. (2004) A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor. J. Biol. Chem. 279, 20186-20193.
    • (2004) J. Biol. Chem , vol.279 , pp. 20186-20193
    • Kurokawa, H.1    Lee, D.S.2    Watanabe, M.3    Sagami, I.4    Mikami, B.5    Raman, C.S.6    Shimizu, T.7
  • 6
    • 1542327658 scopus 로고    scopus 로고
    • Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia coli DOS heme domain (Ec DosH)
    • Park, H., Suquet, C., Satterlee, J. D., and Kang, C. (2004) Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia coli DOS heme domain (Ec DosH). Biochemistry 43, 2738-2746.
    • (2004) Biochemistry , vol.43 , pp. 2738-2746
    • Park, H.1    Suquet, C.2    Satterlee, J.D.3    Kang, C.4
  • 7
    • 0037189552 scopus 로고    scopus 로고
    • Characterization of a direct oxygen sensor heme protein from Escherichia coli: Kinetics of the heme redox states and mutations at the heme-biniding site on catalysis and structure
    • Sasakura, Y., Hirata, S., Sugiyama, S., Suzuki, S., Taguchi, S., Watanabe, M., Matsui, T., Sagami, I., and Shimizu, T. (2002) Characterization of a direct oxygen sensor heme protein from Escherichia coli: Kinetics of the heme redox states and mutations at the heme-biniding site on catalysis and structure. J. Biol. Chem. 277, 23821-23827.
    • (2002) J. Biol. Chem , vol.277 , pp. 23821-23827
    • Sasakura, Y.1    Hirata, S.2    Sugiyama, S.3    Suzuki, S.4    Taguchi, S.5    Watanabe, M.6    Matsui, T.7    Sagami, I.8    Shimizu, T.9
  • 8
    • 0037031927 scopus 로고    scopus 로고
    • Stationary and time-resolved resonance Raman spectra of His77 and Met95 mutants of the isolated heme domain of a direct oxygen sensor from Escherichia coli
    • Sato, A., Sasakura, Y., Sugiyama, S., Sagami, I., Shimizu, T., Mizutani, Y., and Kitagawa, T. (2002) Stationary and time-resolved resonance Raman spectra of His77 and Met95 mutants of the isolated heme domain of a direct oxygen sensor from Escherichia coli. J. Biol. Chem. 277, 32650-32658.
    • (2002) J. Biol. Chem , vol.277 , pp. 32650-32658
    • Sato, A.1    Sasakura, Y.2    Sugiyama, S.3    Sagami, I.4    Shimizu, T.5    Mizutani, Y.6    Kitagawa, T.7
  • 9
    • 0942276394 scopus 로고    scopus 로고
    • Binding of oxygen and carbon monoxide to a heme-regulated phosphodiesterase from Escherichia coli: Kinetics and infrared spectra of the full-length wild-type enzyme, isolated PAS domain, and Met95 mutants
    • Taguchi, S., Matsui, T., Igarashi, J., Sasakura, Y., Araki, Y., Ito, O., Sugiyama, S., Sagami, I., and Shimizu, T. (2004) Binding of oxygen and carbon monoxide to a heme-regulated phosphodiesterase from Escherichia coli: Kinetics and infrared spectra of the full-length wild-type enzyme, isolated PAS domain, and Met95 mutants. J. Biol. Chem. 279, 3340-3347.
    • (2004) J. Biol. Chem , vol.279 , pp. 3340-3347
    • Taguchi, S.1    Matsui, T.2    Igarashi, J.3    Sasakura, Y.4    Araki, Y.5    Ito, O.6    Sugiyama, S.7    Sagami, I.8    Shimizu, T.9
  • 10
    • 0036436657 scopus 로고    scopus 로고
    • Unusual cyanide bindings to a heme-regualted phoephodiesterase from Escherichia coli: Effect of Met95 mutations
    • Watanabe, M., Matsui, T., Sasakura, Y., Sagami, I., and Shimizu, T. (2002) Unusual cyanide bindings to a heme-regualted phoephodiesterase from Escherichia coli: Effect of Met95 mutations. Biochem. Biophys. Res. Commun. 299, 169-172.
    • (2002) Biochem. Biophys. Res. Commun , vol.299 , pp. 169-172
    • Watanabe, M.1    Matsui, T.2    Sasakura, Y.3    Sagami, I.4    Shimizu, T.5
  • 11
    • 0344393534 scopus 로고    scopus 로고
    • Characterization of Met95 mutants of a heme-regulated phosphodiesterase from Escherichia coli: Optical absorption, magnetic circular dichroism, circular dichroism, and redox potentials
    • Hirata, S., Matsui, T., Sasakura, Y., Sugiyama, S., Yoshimura, T., Sagami, I., and Shimizu, T. (2003) Characterization of Met95 mutants of a heme-regulated phosphodiesterase from Escherichia coli: Optical absorption, magnetic circular dichroism, circular dichroism, and redox potentials. Eur. J. Biochem. 270, 4771-4779.
    • (2003) Eur. J. Biochem , vol.270 , pp. 4771-4779
    • Hirata, S.1    Matsui, T.2    Sasakura, Y.3    Sugiyama, S.4    Yoshimura, T.5    Sagami, I.6    Shimizu, T.7
  • 12
    • 4944244330 scopus 로고    scopus 로고
    • Critical role of Asp40 at the haem proximal side of haem-regulated phosphodiesterase from Escherichia coli in redox potential, auto-oxidation and catalytic control
    • Watanabe, M., Kurokawa, H., Yoshimura-Suzuki, T., Sagami, I., and Shimizu, T. (2004) Critical role of Asp40 at the haem proximal side of haem-regulated phosphodiesterase from Escherichia coli in redox potential, auto-oxidation and catalytic control. Eur. J. Biochem. 271, 3937-3942.
    • (2004) Eur. J. Biochem , vol.271 , pp. 3937-3942
    • Watanabe, M.1    Kurokawa, H.2    Yoshimura-Suzuki, T.3    Sagami, I.4    Shimizu, T.5
  • 13
    • 33644749541 scopus 로고    scopus 로고
    • Critical roles of Leu99 and Leu115 at the heme distal side in auto-oxidation and the redox potential of a heme-regulated phosphodiesterase from Escherichia coli
    • Yokota, N., Araki, Y., Kurokawa, H., Ito, O., Igarashi, J., and Shimizu, T. (2006) Critical roles of Leu99 and Leu115 at the heme distal side in auto-oxidation and the redox potential of a heme-regulated phosphodiesterase from Escherichia coli. FEBS J. 273, 1210-1223.
    • (2006) FEBS J , vol.273 , pp. 1210-1223
    • Yokota, N.1    Araki, Y.2    Kurokawa, H.3    Ito, O.4    Igarashi, J.5    Shimizu, T.6
  • 14
    • 33644537046 scopus 로고    scopus 로고
    • 2 sensing; A single convergent structure of the heme moiety is relevant to the downregulation of kinase activity
    • 2 sensing; A single convergent structure of the heme moiety is relevant to the downregulation of kinase activity. Biochemistry 45, 2515-2523.
    • (2006) Biochemistry , vol.45 , pp. 2515-2523
    • Tanaka, A.1    Nakamura, H.2    Shiro, Y.3    Fujii, H.4
  • 16
    • 37349032156 scopus 로고    scopus 로고
    • Ligand binding and inhibition of an oxygen-sensitive soluble guanylate cyclase, Gly-88E, from Drosophila
    • Huang, S. H., Rio, D. C., and Marietta, M. (2007) Ligand binding and inhibition of an oxygen-sensitive soluble guanylate cyclase, Gly-88E, from Drosophila. Biochemistry 46, 15115-15122.
    • (2007) Biochemistry , vol.46 , pp. 15115-15122
    • Huang, S.H.1    Rio, D.C.2    Marietta, M.3
  • 17
    • 33646579620 scopus 로고    scopus 로고
    • Role of distal arginine in early sensing intermediates in the heme domain of the oxygen sensor FixL
    • Jasaitis, A., Hola, K., Bouzhir-Sima, L., Lambry, J. C., Balland, V., Vos, M. H., and Lieb, U. (2006) Role of distal arginine in early sensing intermediates in the heme domain of the oxygen sensor FixL. Biochemistry 45, 6018-6026.
    • (2006) Biochemistry , vol.45 , pp. 6018-6026
    • Jasaitis, A.1    Hola, K.2    Bouzhir-Sima, L.3    Lambry, J.C.4    Balland, V.5    Vos, M.H.6    Lieb, U.7
  • 19
    • 33144485743 scopus 로고    scopus 로고
    • Functional implications of the propionate 7-arginine 220 interaction in the FixLH oxygen sensor from Bradyhizobium japonicum
    • Balland, V., Bouzhir-Sima, L., Anxolabéhère-Mallart, E., Boussac, A., Vos, M. H., Lieble, U., and Mattioli, T. A. (2006) Functional implications of the propionate 7-arginine 220 interaction in the FixLH oxygen sensor from Bradyhizobium japonicum. Biochemistry 45, 2072-2084.
    • (2006) Biochemistry , vol.45 , pp. 2072-2084
    • Balland, V.1    Bouzhir-Sima, L.2    Anxolabéhère-Mallart, E.3    Boussac, A.4    Vos, M.H.5    Lieble, U.6    Mattioli, T.A.7
  • 21
    • 34249081123 scopus 로고    scopus 로고
    • Resonance Raman observation of the structural dynamics of FixL on signal transduction and ligand discrimination
    • Hiruma, Y., Kikuchi, A., Tanaka, A., Shiro, Y., and Mizutani, Y. (2007) Resonance Raman observation of the structural dynamics of FixL on signal transduction and ligand discrimination. Biochemistry 46, 6086-6096.
    • (2007) Biochemistry , vol.46 , pp. 6086-6096
    • Hiruma, Y.1    Kikuchi, A.2    Tanaka, A.3    Shiro, Y.4    Mizutani, Y.5
  • 22
    • 0034636144 scopus 로고    scopus 로고
    • New mechanistic insights from structural studies of the oxygen-sensing domain of Bradyrhizobium japonicum FixL
    • Gong, W., Hao, B., and Chan, M. K. (2000) New mechanistic insights from structural studies of the oxygen-sensing domain of Bradyrhizobium japonicum FixL. Biochemistry 39, 3955-3962.
    • (2000) Biochemistry , vol.39 , pp. 3955-3962
    • Gong, W.1    Hao, B.2    Chan, M.K.3
  • 24
    • 0346732270 scopus 로고    scopus 로고
    • Relationships between heme incorporation, tetramer formation and catalysis of a heme-regulated phosphodiesterase from Escherichia coli: A study of deletion and site-directed mutants
    • Yoshimura, T., Sagami, I., Sasakura, Y., and Shimizu, T. (2003) Relationships between heme incorporation, tetramer formation and catalysis of a heme-regulated phosphodiesterase from Escherichia coli: A study of deletion and site-directed mutants. J. Biol. Chem. 278, 53105-53111.
    • (2003) J. Biol. Chem , vol.278 , pp. 53105-53111
    • Yoshimura, T.1    Sagami, I.2    Sasakura, Y.3    Shimizu, T.4
  • 25
    • 33947665446 scopus 로고    scopus 로고
    • Ultraviolet resonance Raman evidence for utilization of the heme 6-propionate hydrogen-bond network in signal transmission from heme to protein in Ec DOS Protein
    • El-Mashtoly, S. F., Takahashi, H., Shimizu, T., and Kitagawa, T. (2007) Ultraviolet resonance Raman evidence for utilization of the heme 6-propionate hydrogen-bond network in signal transmission from heme to protein in Ec DOS Protein. J. Am. Chem. Soc. 129, 3556-3563.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 3556-3563
    • El-Mashtoly, S.F.1    Takahashi, H.2    Shimizu, T.3    Kitagawa, T.4
  • 26
    • 38349114171 scopus 로고    scopus 로고
    • Ligand dynamics and early signaling events in the heme domain of the sensor protein dos from Escherichia coli
    • Yamashita, T., Bouzhir-Sima, L., Lambry, J. C., Liebl, U., and Vos, M. H. (2008) Ligand dynamics and early signaling events in the heme domain of the sensor protein dos from Escherichia coli. J. Biol. Chem. 283, 2344-2352.
    • (2008) J. Biol. Chem , vol.283 , pp. 2344-2352
    • Yamashita, T.1    Bouzhir-Sima, L.2    Lambry, J.C.3    Liebl, U.4    Vos, M.H.5
  • 27
    • 0038052346 scopus 로고    scopus 로고
    • Ligand binding dynamics to the heme domain of the oxygen sensor dos from Escherichia coli
    • Lieb, U., Bouzhir-Sima, L., Kiger, L., Marden, M. C., Lambry, J. C., Négrerie, M., and Vos, M. H. (2003) Ligand binding dynamics to the heme domain of the oxygen sensor dos from Escherichia coli. Biochemistry 42, 6527-6535.
    • (2003) Biochemistry , vol.42 , pp. 6527-6535
    • Lieb, U.1    Bouzhir-Sima, L.2    Kiger, L.3    Marden, M.C.4    Lambry, J.C.5    Négrerie, M.6    Vos, M.H.7
  • 28
    • 0036791007 scopus 로고    scopus 로고
    • Ultrafast ligand rebinding in the heme domain of the oxygen sensors FixL and Dos: General regulatory implications for heme-based sensors
    • Lieb, U., Bouzhir-Sima, L., Négrerie, M., Martin, J. L., and Vos, M. H. (2002) Ultrafast ligand rebinding in the heme domain of the oxygen sensors FixL and Dos: General regulatory implications for heme-based sensors. Proc. Natl. Acad. Sci. U.S.A. 99, 12771-12776.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 12771-12776
    • Lieb, U.1    Bouzhir-Sima, L.2    Négrerie, M.3    Martin, J.L.4    Vos, M.H.5
  • 29
  • 30
    • 49649105751 scopus 로고    scopus 로고
    • Roles of Arg-97 and Phe-113 in regulation of distal ligand binding to heme in the sensor domain of Ec DOS protein: Resonance raman and mutation study
    • El-Mashtoly, S. F., Nakashima, S., Tanaka, A., Shimizu, T., and Kitagawa, T. (2008) Roles of Arg-97 and Phe-113 in regulation of distal ligand binding to heme in the sensor domain of Ec DOS protein: Resonance raman and mutation study. J. Biol. Chem. 283, 19000-19010.
    • (2008) J. Biol. Chem , vol.283 , pp. 19000-19010
    • El-Mashtoly, S.F.1    Nakashima, S.2    Tanaka, A.3    Shimizu, T.4    Kitagawa, T.5
  • 31
    • 0029954838 scopus 로고    scopus 로고
    • Mechanism of hydrogen cyanide binding to myoglobin
    • Dou, Y., Olson, J. S., Wilkinson, A. J., and Ikeda-Saito, M. (1996) Mechanism of hydrogen cyanide binding to myoglobin. Biochemistry 35, 7107-7113.
    • (1996) Biochemistry , vol.35 , pp. 7107-7113
    • Dou, Y.1    Olson, J.S.2    Wilkinson, A.J.3    Ikeda-Saito, M.4
  • 33
    • 0037054860 scopus 로고    scopus 로고
    • Production and characterization of Met80X mutants of yeast iso-1-cytochrome c: Spectral, photochemical and binding studies on ferrous derivatives
    • Silkstone, G., Stanway, G., Brzezinsky, P., and Wilson, M. T. (2002) Production and characterization of Met80X mutants of yeast iso-1-cytochrome c: Spectral, photochemical and binding studies on ferrous derivatives. Biophys. Chem. 98, 65-77.
    • (2002) Biophys. Chem , vol.98 , pp. 65-77
    • Silkstone, G.1    Stanway, G.2    Brzezinsky, P.3    Wilson, M.T.4
  • 34
    • 33847261166 scopus 로고    scopus 로고
    • Ligand dynamics in an electron transfer protein: Picosecond geminate recombination of carbon monoxide to heme in mutant forms of cytochrome c
    • Silkstone, G., Jasaitis, A., Wilson, M. T., and Vos, M. H. (2007) Ligand dynamics in an electron transfer protein: Picosecond geminate recombination of carbon monoxide to heme in mutant forms of cytochrome c. J. Biol. Chem. 282, 1638-1649.
    • (2007) J. Biol. Chem , vol.282 , pp. 1638-1649
    • Silkstone, G.1    Jasaitis, A.2    Wilson, M.T.3    Vos, M.H.4
  • 35
    • 0025243607 scopus 로고
    • Analysis of the kinetic barrier for ligand binding to sperm whale myoglobin using site-directed mutagenesis and laser photolysis
    • Carver, T. E., Rohlfs, R. J., Olson, J. S., Gibson, Q. H., Blackmore, R. S., Springer, B. A., and Sligar, S. G. (1990) Analysis of the kinetic barrier for ligand binding to sperm whale myoglobin using site-directed mutagenesis and laser photolysis. J. Biol. Chem. 265, 20007-20020.
    • (1990) J. Biol. Chem , vol.265 , pp. 20007-20020
    • Carver, T.E.1    Rohlfs, R.J.2    Olson, J.S.3    Gibson, Q.H.4    Blackmore, R.S.5    Springer, B.A.6    Sligar, S.G.7
  • 36
    • 0018790637 scopus 로고
    • Correlation between the Quantum Yields of Photodissociation and C-O Stretching Frequencies of Carbon Monoxide Hemoproteins
    • Shimada, H., Iizuka, T., Ueno, R., and Ishimura, Y. (1979) Correlation between the Quantum Yields of Photodissociation and C-O Stretching Frequencies of Carbon Monoxide Hemoproteins. FEBS Lett. 98, 290-294.
    • (1979) FEBS Lett , vol.98 , pp. 290-294
    • Shimada, H.1    Iizuka, T.2    Ueno, R.3    Ishimura, Y.4


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