메뉴 건너뛰기




Volumn 56, Issue 6, 2004, Pages 309-315

CO sniffing through heme-based sensor proteins

Author keywords

CO sensing; CO signal transduction; CooA; NPAS2

Indexed keywords

CARBON MONOXIDE; COOA PROTEIN; NEURONAL PAS DOMAIN PROTEIN 2; NITROGEN DIOXIDE; OXYGEN; PROTEIN; PROTEIN BMAL1; SENSOR PROTEIN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 7044226454     PISSN: 15216543     EISSN: None     Source Type: Journal    
DOI: 10.1080/10258140412331286937     Document Type: Review
Times cited : (17)

References (92)
  • 1
    • 0035313020 scopus 로고    scopus 로고
    • Structural aspects of denitrifying enzymes
    • Moura, I., and Moura, J. J. (2001) Structural aspects of denitrifying enzymes. Curr. Opin. Chem. Biol. 5, 168-175.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 168-175
    • Moura, I.1    Moura, J.J.2
  • 3
    • 0041706296 scopus 로고    scopus 로고
    • Soil microbial activities and carbon and nitrogen fixation
    • Chen, G., Zhu, H., and Zhang, Y. (2003) Soil microbial activities and carbon and nitrogen fixation. Res. Microbiol. 154, 393-398.
    • (2003) Res. Microbiol. , vol.154 , pp. 393-398
    • Chen, G.1    Zhu, H.2    Zhang, Y.3
  • 4
    • 0842334759 scopus 로고    scopus 로고
    • Oxygen conformance of cellular respiration. A perspective of mitochondrial physiology
    • Gnaiger, E. (2003) Oxygen conformance of cellular respiration. A perspective of mitochondrial physiology. Adv. Exp. Med. Biol. 543, 39-55.
    • (2003) Adv. Exp. Med. Biol. , vol.543 , pp. 39-55
    • Gnaiger, E.1
  • 5
    • 0032900608 scopus 로고    scopus 로고
    • Hemoglobin is an honorary enzyme
    • Brunori, M. (1999) Hemoglobin is an honorary enzyme. Trends Biochem. Sci. 24, 158-161.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 158-161
    • Brunori, M.1
  • 6
    • 0033619248 scopus 로고    scopus 로고
    • The haemoglobin enzyme
    • Imai, K. (1999) The haemoglobin enzyme. Nature 401, 437-439.
    • (1999) Nature , vol.401 , pp. 437-439
    • Imai, K.1
  • 8
    • 0347419305 scopus 로고    scopus 로고
    • The molecular machinery of Keilin's respiratory chain
    • Rich, P. R. (2003) The molecular machinery of Keilin's respiratory chain. Biochem. Soc. Trans. 31, 1095-1105.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 1095-1105
    • Rich, P.R.1
  • 9
    • 0037933181 scopus 로고    scopus 로고
    • Myoglobin function reassessed
    • Wittenberg, J. B., and Wittenberg, B. A. (2003) Myoglobin function reassessed. J. Exp. Biol. 206, 2011-2020.
    • (2003) J. Exp. Biol. , vol.206 , pp. 2011-2020
    • Wittenberg, J.B.1    Wittenberg, B.A.2
  • 10
    • 0035312317 scopus 로고    scopus 로고
    • Nitric oxide moves myoglobin centre stage
    • Brunori, M. (2001) Nitric oxide moves myoglobin centre stage. Trends Biochem. Sci. 26, 209-210.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 209-210
    • Brunori, M.1
  • 12
    • 0036525946 scopus 로고    scopus 로고
    • Nitric oxide and myoglobins
    • Moller, J. K., and Skibsted, L. H. (2002) Nitric oxide and myoglobins. Chem. Rev. 102, 1167-1178.
    • (2002) Chem. Rev. , vol.102 , pp. 1167-1178
    • Moller, J.K.1    Skibsted, L.H.2
  • 13
    • 0036090811 scopus 로고    scopus 로고
    • Biological chemistry of carbon monoxide
    • Piantadosi, C. A. (2002) Biological chemistry of carbon monoxide. Antioxid. Redox Signal. 4, 259-270.
    • (2002) Antioxid. Redox Signal. , vol.4 , pp. 259-270
    • Piantadosi, C.A.1
  • 14
    • 0347622940 scopus 로고    scopus 로고
    • Competitive, reversible, physiological? Inhibition of mitochondrial cytochrome oxidase by nitric oxide
    • Cooper, C. E. (2003) Competitive, reversible, physiological? Inhibition of mitochondrial cytochrome oxidase by nitric oxide. IUBMB Life 55, 591-597.
    • (2003) IUBMB Life , vol.55 , pp. 591-597
    • Cooper, C.E.1
  • 15
    • 0041806720 scopus 로고    scopus 로고
    • Myoglobin: The hydrogen atom of biology and a paradigm of complexity
    • Frauenfelder, H., McMahon, B. H., and Fenimore, P. W. (2003) Myoglobin: the hydrogen atom of biology and a paradigm of complexity. Proc. Natl. Acad. Sci. USA 100, 8615-8617.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8615-8617
    • Frauenfelder, H.1    McMahon, B.H.2    Fenimore, P.W.3
  • 17
    • 0346756213 scopus 로고    scopus 로고
    • Hemoglobin and nitric oxide
    • Stamler, J. S. (2003) Hemoglobin and nitric oxide. N. Engl. J. Med. 349, 402-405.
    • (2003) N. Engl. J. Med. , vol.349 , pp. 402-405
    • Stamler, J.S.1
  • 19
    • 0035957381 scopus 로고    scopus 로고
    • Erratum
    • Flögel, U., Merx, M. W., Gödecke, A., Decking, U. K., and Schrader, J. (2001) Myoglobin: a scavenger of bioactive NO. Proc. Natl. Acad. Sci. USA 98, 735-740. Erratum in: (2001) Proc. Natl. Acad. Sci. USA 98, 4276.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4276
  • 20
    • 0141783647 scopus 로고    scopus 로고
    • Bacterial hemoglobins and flavohemoglobins: Versatile proteins and their impact on microbiology and biotechnology
    • Frey, A. D., and Kallio, P. T. (2003) Bacterial hemoglobins and flavohemoglobins: versatile proteins and their impact on microbiology and biotechnology. FEMS Microbiol. Rev. 27, 525-545.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 525-545
    • Frey, A.D.1    Kallio, P.T.2
  • 21
    • 0038498077 scopus 로고    scopus 로고
    • Myoglobin protects the heart from inducible nitric-oxide synthase (iNOS)-mediated nitrosative stress
    • Gödecke, A., Molojavyi, A., Heger, J., Flögel, U., Ding, Z., Jacoby, C., and Schrader, J. (2003) Myoglobin protects the heart from inducible nitric-oxide synthase (iNOS)-mediated nitrosative stress. J. Biol. Chem. 278, 21761-21766.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21761-21766
    • Gödecke, A.1    Molojavyi, A.2    Heger, J.3    Flögel, U.4    Ding, Z.5    Jacoby, C.6    Schrader, J.7
  • 24
    • 2942614429 scopus 로고    scopus 로고
    • Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases
    • in press
    • Gardner, P. R. (2004) Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases. J. Inorg. Biochem. (in press).
    • (2004) J. Inorg. Biochem.
    • Gardner, P.R.1
  • 26
    • 0025878267 scopus 로고
    • A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti
    • Gilles-Gonzalez, M. A., Ditta, G. S., and Helinski, D. R. (1991) A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti. Nature 350, 170-172.
    • (1991) Nature , vol.350 , pp. 170-172
    • Gilles-Gonzalez, M.A.1    Ditta, G.S.2    Helinski, D.R.3
  • 27
    • 0001848362 scopus 로고
    • Simbiotic expression of Rhizobium meliloti nitrogen fixation genes is regulated by oxygen
    • (Hich, J. H., and Silhavy, T., eds.). ASM Press, Washington, DC
    • Agron, P. G., and Helinski, D. R. (1995) Simbiotic expression of Rhizobium meliloti nitrogen fixation genes is regulated by oxygen. In Two-Component Signal Transduction (Hich, J. H., and Silhavy, T., eds.). pp. 275-287. ASM Press, Washington, DC.
    • (1995) Two-Component Signal Transduction , pp. 275-287
    • Agron, P.G.1    Helinski, D.R.2
  • 29
    • 0033120934 scopus 로고    scopus 로고
    • Heme-based sensors in biological systems
    • Rodgers, K. R. (1999) Heme-based sensors in biological systems. Curr. Opin. Chem. Biol. 3, 158-167.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 158-167
    • Rodgers, K.R.1
  • 30
    • 0034646392 scopus 로고    scopus 로고
    • Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor
    • Delgado-Nixon, V. M., Gonzalez, G., and Gilles-Gonzalez, M. A. (2000) Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor. Biochemistry 39, 2685-2691.
    • (2000) Biochemistry , vol.39 , pp. 2685-2691
    • Delgado-Nixon, V.M.1    Gonzalez, G.2    Gilles-Gonzalez, M.A.3
  • 31
    • 0035313335 scopus 로고    scopus 로고
    • Recent advances heme-protein sensors
    • Chan, M. K. (2001) Recent advances heme-protein sensors. Curr. Opin. Chem. Biol. 5, 216-222.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 216-222
    • Chan, M.K.1
  • 33
    • 0034877185 scopus 로고    scopus 로고
    • Oxygen signal transduction
    • Gilles-Gonzales, M. A. (2001) Oxygen signal transduction. IUBMB Life 51, 165-173.
    • (2001) IUBMB Life , vol.51 , pp. 165-173
    • Gilles-Gonzales, M.A.1
  • 34
    • 0344066227 scopus 로고    scopus 로고
    • Biochemical and biophysical properties of the CO-sensing transcriptional activator CooA
    • Aono, S. (2003) Biochemical and biophysical properties of the CO-sensing transcriptional activator CooA. Acc. Chem. Res. 36, 825-831.
    • (2003) Acc. Chem. Res. , vol.36 , pp. 825-831
    • Aono, S.1
  • 35
    • 0942298565 scopus 로고    scopus 로고
    • Signal transduction by heme-containing PAS-domain proteins
    • Gilles-Gonzalez, M. A., and Gonzalez, G. (2004) Signal transduction by heme-containing PAS-domain proteins. J. Appl. Physiol. 96, 774-783.
    • (2004) J. Appl. Physiol. , vol.96 , pp. 774-783
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2
  • 36
    • 1642274684 scopus 로고    scopus 로고
    • The PAS fold: A redefination of the PAS domain based upon structural prediction
    • Hefti, M. H., Francoijs, K. J., de Vries, S. C., Dixon, R., and Vervoort, J. (2004) The PAS fold: a redefination of the PAS domain based upon structural prediction. Eur. J. Biochem. 271, 1198-1208.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1198-1208
    • Hefti, M.H.1    Francoijs, K.J.2    De Vries, S.C.3    Dixon, R.4    Vervoort, J.5
  • 37
    • 0033229863 scopus 로고    scopus 로고
    • FixL, a haemoglobin that acts as an oxygen sensor: Signalling mechanism and structural basis of its homology with PAS domains
    • Perutz, M. F., Paoli, M., and Lesk, A. M. (1999) FixL, a haemoglobin that acts as an oxygen sensor: signalling mechanism and structural basis of its homology with PAS domains. Chem. Biol. 6, R291-R297.
    • (1999) Chem. Biol. , vol.6
    • Perutz, M.F.1    Paoli, M.2    Lesk, A.M.3
  • 40
    • 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
  • 41
    • 0042334880 scopus 로고    scopus 로고
    • Structure of the oxygen sensor in Bacillus subtilis: Signal transduction of chemotaxis by control of symmetry
    • Zhang, W., and Phillips, G. N. Jr. (2003) Structure of the oxygen sensor in Bacillus subtilis: signal transduction of chemotaxis by control of symmetry. Structure 11, 1097-1110.
    • (2003) Structure , vol.11 , pp. 1097-1110
    • Zhang, W.1    Phillips Jr., G.N.2
  • 42
    • 1642565860 scopus 로고    scopus 로고
    • Resonance Raman and ligand-binding analysis of the oxygen-sensing signal transducer protein HemAT from Bacillus subtilis
    • Aono, S., Nakajima, H., Ohta, T., and Kitagawa, T. (2004) Resonance Raman and ligand-binding analysis of the oxygen-sensing signal transducer protein HemAT from Bacillus subtilis. Methods Enzymol. 381, 618-628.
    • (2004) Methods Enzymol. , vol.381 , pp. 618-628
    • Aono, S.1    Nakajima, H.2    Ohta, T.3    Kitagawa, T.4
  • 44
    • 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
    • Liebl, U., Bouzhir-Sima, L., Negrerie, 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. USA 99, 12771-12776.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12771-12776
    • Liebl, U.1    Bouzhir-Sima, L.2    Negrerie, M.3    Martin, J.L.4    Vos, M.H.5
  • 45
    • 0037189552 scopus 로고    scopus 로고
    • Characterization of a direct oxygen sensor heme protein from Escherichia coli. Effects of the heme redox states and mutations at the heme-binding 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. Effects of the heme redox states and mutations at the heme-binding 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
  • 46
    • 0038052346 scopus 로고    scopus 로고
    • Ligand binding dynamics to the heme domain of the oxygen sensor Dos from Escherichia coli
    • Liebl, U., Bouzhir-Sima, L., Kiger, L., Marden, M. C., Lambry, J. C., Negrerie, 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
    • Liebl, U.1    Bouzhir-Sima, L.2    Kiger, L.3    Marden, M.C.4    Lambry, J.C.5    Negrerie, M.6    Vos, M.H.7
  • 47
    • 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
  • 48
    • 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 Met-95 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 Met-95 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
  • 49
    • 0032902722 scopus 로고    scopus 로고
    • Guanylate cyclase and the NO/cGMP signaling pathway
    • Denninger, J. W., and Marletta, M. A. (1999) Guanylate cyclase and the NO/cGMP signaling pathway. Biochim. Biophys. Acta. 1411, 334-350.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 334-350
    • Denninger, J.W.1    Marletta, M.A.2
  • 51
    • 0036200487 scopus 로고    scopus 로고
    • The receptor-like properties of nitric oxide-activated soluble guanylyl cyclase in intact cells
    • Bellamy, T. C., and Garthwaite, J. (2002) The receptor-like properties of nitric oxide-activated soluble guanylyl cyclase in intact cells. Mol. Cell. Biochem. 230, 165-176.
    • (2002) Mol. Cell. Biochem. , vol.230 , pp. 165-176
    • Bellamy, T.C.1    Garthwaite, J.2
  • 52
    • 0142056753 scopus 로고    scopus 로고
    • Structure, regulation, and function of mammalian membrane guanylyl cyclase receptors, with a focus on guanylyl cyclase-A
    • Kuhn, M. (2003) Structure, regulation, and function of mammalian membrane guanylyl cyclase receptors, with a focus on guanylyl cyclase-A. Circ. Res. 93, 700-709.
    • (2003) Circ. Res. , vol.93 , pp. 700-709
    • Kuhn, M.1
  • 53
    • 0042975272 scopus 로고    scopus 로고
    • Soluble guanylyl cyclase: Physiological role as an NO receptor and the potential molecular target for therapeutic application
    • Nakane, M. (2003) Soluble guanylyl cyclase: physiological role as an NO receptor and the potential molecular target for therapeutic application. Clin. Chem. Lab. Med. 41, 865-870.
    • (2003) Clin. Chem. Lab. Med. , vol.41 , pp. 865-870
    • Nakane, M.1
  • 54
    • 0028132836 scopus 로고
    • Redox signaling: Nitrosylation and related target interactions of nitric oxide
    • Stamler, J. S. (1994) Redox signaling: nitrosylation and related target interactions of nitric oxide. Cell 78, 931-936.
    • (1994) Cell , vol.78 , pp. 931-936
    • Stamler, J.S.1
  • 55
    • 0031971053 scopus 로고    scopus 로고
    • Oxidative modifications in nitrosative stress
    • Stamler, J. S., and Hausladen, A. (1998) Oxidative modifications in nitrosative stress. Nat. Struct. Biol. 5, 247-249.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 247-249
    • Stamler, J.S.1    Hausladen, A.2
  • 57
    • 0033751725 scopus 로고    scopus 로고
    • CO sensing and regulation of gene expression by the transcriptional activator CooA
    • Aono, S., Honma, Y., Ohkubo, K., Tawara, T., Kamiya, T., and Nakajima, H. (2000) CO sensing and regulation of gene expression by the transcriptional activator CooA. J. Inorg. Biochem. 82, 51-56.
    • (2000) J. Inorg. Biochem. , vol.82 , pp. 51-56
    • Aono, S.1    Honma, Y.2    Ohkubo, K.3    Tawara, T.4    Kamiya, T.5    Nakajima, H.6
  • 58
    • 0035223846 scopus 로고    scopus 로고
    • CooA: A heme-containing regulatory protein that serves as a specific sensor of both carbon monoxide and redox state
    • Roberts, G. P., Thorsteinsson, M. V., Kerby, R. L., Lanzilotta, W. N., and Poulos, T. (2001) CooA: a heme-containing regulatory protein that serves as a specific sensor of both carbon monoxide and redox state. Prog. Nucleic Acid Res. Mol. Biol. 67, 35-63.
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.67 , pp. 35-63
    • Roberts, G.P.1    Thorsteinsson, M.V.2    Kerby, R.L.3    Lanzilotta, W.N.4    Poulos, T.5
  • 59
    • 1342346631 scopus 로고    scopus 로고
    • Functionally critical elements of CooA-related CO sensors
    • Youn, H., Kerby, R. L., Conrad, M., and Roberts, G. P. (2004) Functionally critical elements of CooA-related CO sensors. J. Bacteriol. 186, 1320-1329.
    • (2004) J. Bacteriol. , vol.186 , pp. 1320-1329
    • Youn, H.1    Kerby, R.L.2    Conrad, M.3    Roberts, G.P.4
  • 61
    • 0037147101 scopus 로고    scopus 로고
    • Circadian rhythms. Carbon monoxide and clocks
    • Boehning, D., and Snyder, S. H. (2002) Circadian rhythms. Carbon monoxide and clocks. Science 298, 2339-2340.
    • (2002) Science , vol.298 , pp. 2339-2340
    • Boehning, D.1    Snyder, S.H.2
  • 62
    • 0030597287 scopus 로고    scopus 로고
    • A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodospirillum rubrum
    • Aono, S., Nakajima, H., Saito, K., and Okada, M. (1996) A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodospirillum rubrum. Biochem. Biophys. Res. Commun. 228, 752-756.
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 752-756
    • Aono, S.1    Nakajima, H.2    Saito, K.3    Okada, M.4
  • 63
    • 0030856066 scopus 로고    scopus 로고
    • CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein
    • Shelver, D., Kerby, R. L., He, Y., and Roberts, G. P. (1997) CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein. Proc. Natl. Acad. Sci. USA 94, 11216-11220.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11216-11220
    • Shelver, D.1    Kerby, R.L.2    He, Y.3    Roberts, G.P.4
  • 64
    • 0028925554 scopus 로고
    • Carbon monoxide-dependent growth of Rhodospirillum rubrum
    • Kerby, R. L., Ludden, P. W., and Roberts, G. P. (1995) Carbon monoxide-dependent growth of Rhodospirillum rubrum. J. Bacteriol. 177, 2241-2244.
    • (1995) J. Bacteriol. , vol.177 , pp. 2241-2244
    • Kerby, R.L.1    Ludden, P.W.2    Roberts, G.P.3
  • 65
    • 0026649571 scopus 로고
    • Genetic and physiological characterization of the Rhodospirillum rubrum carbon monoxide dehydrogenase system
    • Kerby, R. L., Hong, S. S., Ensign, S. A., Coppoc, L. J., Ludden, P. W., and Roberts, G. P. (1992) Genetic and physiological characterization of the Rhodospirillum rubrum carbon monoxide dehydrogenase system. J. Bacteriol. 174, 5284-5294.
    • (1992) J. Bacteriol. , vol.174 , pp. 5284-5294
    • Kerby, R.L.1    Hong, S.S.2    Ensign, S.A.3    Coppoc, L.J.4    Ludden, P.W.5    Roberts, G.P.6
  • 67
    • 0034671504 scopus 로고    scopus 로고
    • Characterization of variants altered at the N-terminal proline, a novel heme-axial ligand in CooA, the CO-sensing transcriptional activator
    • Thorsteinsson, M. V., Kerby, R. L., Conrad, M., Youn, H., Staples, C. R., Lanzilotta, W. N., Poulos, T. J., Serate, J., and Roberts, G. P. (2000) Characterization of variants altered at the N-terminal proline, a novel heme-axial ligand in CooA, the CO-sensing transcriptional activator. J. Biol. Chem. 275, 39332-39338.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39332-39338
    • Thorsteinsson, M.V.1    Kerby, R.L.2    Conrad, M.3    Youn, H.4    Staples, C.R.5    Lanzilotta, W.N.6    Poulos, T.J.7    Serate, J.8    Roberts, G.P.9
  • 68
    • 0035831489 scopus 로고    scopus 로고
    • Redox properties and coordination structure of the heme in the co-sensing transcriptional activator CooA
    • Nakajima, H., Honma, Y., Tawara, T., Kato, T., Park, S. Y., Miyatake, H., Shiro, Y., and Aono, S. (2001) Redox properties and coordination structure of the heme in the co-sensing transcriptional activator CooA. J. Biol. Chem. 276, 7055-7061.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7055-7061
    • Nakajima, H.1    Honma, Y.2    Tawara, T.3    Kato, T.4    Park, S.Y.5    Miyatake, H.6    Shiro, Y.7    Aono, S.8
  • 69
    • 0040182564 scopus 로고    scopus 로고
    • Identification of histidine 77 as the axial heme ligand of carbonmonoxy CooA by picosecond time-resolved resonance Raman spectroscopy
    • Uchida, T., Ishikawa, H., Ishimori, K., Morishima, I., Nakajima, H., Aono, S., Mizutani, Y., and Kitagawa, T. (2000) Identification of histidine 77 as the axial heme ligand of carbonmonoxy CooA by picosecond time-resolved resonance Raman spectroscopy. Biochemistry 39, 12747-12752.
    • (2000) Biochemistry , vol.39 , pp. 12747-12752
    • Uchida, T.1    Ishikawa, H.2    Ishimori, K.3    Morishima, I.4    Nakajima, H.5    Aono, S.6    Mizutani, Y.7    Kitagawa, T.8
  • 70
    • 0035851190 scopus 로고    scopus 로고
    • Ligand-switching intermediates for the CO-sensing transcriptional activator CooA measured by pulse radiolysis
    • Nakajima, H., Nakagawa, E., Kobayashi, K., Tagawa, S., and Aono, S. (2001) Ligand-switching intermediates for the CO-sensing transcriptional activator CooA measured by pulse radiolysis. J. Biol. Chem. 276, 37895-37899.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37895-37899
    • Nakajima, H.1    Nakagawa, E.2    Kobayashi, K.3    Tagawa, S.4    Aono, S.5
  • 72
    • 0034681189 scopus 로고    scopus 로고
    • Electronic absorption, EPR, and resonance raman spectroscopy of CooA, a CO-sensing transcription activator from R. rubrum, reveals a five-coordinate NO-heme
    • Reynolds, M. F., Parks, R. B., Burstyn, J. N., Shelver, D., Thorsteinsson, M. V., Kerby, R. L., Roberts, G. P., Vogel, K. M., and Spiro, T. G. (2000) Electronic absorption, EPR, and resonance raman spectroscopy of CooA, a CO-sensing transcription activator from R. rubrum, reveals a five-coordinate NO-heme. Biochemistry 39, 388-396.
    • (2000) Biochemistry , vol.39 , pp. 388-396
    • Reynolds, M.F.1    Parks, R.B.2    Burstyn, J.N.3    Shelver, D.4    Thorsteinsson, M.V.5    Kerby, R.L.6    Roberts, G.P.7    Vogel, K.M.8    Spiro, T.G.9
  • 75
    • 0033516892 scopus 로고    scopus 로고
    • Recognition of target DNA and transcription activation by the CO-sensing transcriptional activator CooA
    • Aono, S., Takasaki, H., Unno, H., Kamiya, T., and Nakajima, H. (1999) Recognition of target DNA and transcription activation by the CO-sensing transcriptional activator CooA. Biochem. Biophys. Res. Commun. 261, 270-275.
    • (1999) Biochem. Biophys. Res. Commun. , vol.261 , pp. 270-275
    • Aono, S.1    Takasaki, H.2    Unno, H.3    Kamiya, T.4    Nakajima, H.5
  • 76
    • 0030051489 scopus 로고    scopus 로고
    • Characterization of a CO-responsive transcriptional activator from Rhodospirillum rubrum
    • He, Y., Shelver, D., Kerby, R. L., and Roberts, G. P. (1996) Characterization of a CO-responsive transcriptional activator from Rhodospirillum rubrum. J. Biol. Chem. 271, 120-123.
    • (1996) J. Biol. Chem. , vol.271 , pp. 120-123
    • He, Y.1    Shelver, D.2    Kerby, R.L.3    Roberts, G.P.4
  • 77
    • 10344238576 scopus 로고    scopus 로고
    • Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum
    • Fox, J. D., He, Y., Shelver, D., Roberts, G. P., and Ludden, P. W. (1996) Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum. J. Bacteriol. 178, 6200-6208.
    • (1996) J. Bacteriol. , vol.178 , pp. 6200-6208
    • Fox, J.D.1    He, Y.2    Shelver, D.3    Roberts, G.P.4    Ludden, P.W.5
  • 78
    • 0033574410 scopus 로고    scopus 로고
    • Transcription activation by CooA, the CO-sensing factor from Rhodospirillum rubrum. The interaction between CooA and the C-terminal domain of the α subunit of RNA polymerase
    • He, Y., Gaal, T., Karls, R., Donohue, T. J., Gourse, R. L., and Roberts, G. P. (1999) Transcription activation by CooA, the CO-sensing factor from Rhodospirillum rubrum. The interaction between CooA and the C-terminal domain of the α subunit of RNA polymerase. J. Biol. Chem. 274, 10840-10845.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10840-10845
    • He, Y.1    Gaal, T.2    Karls, R.3    Donohue, T.J.4    Gourse, R.L.5    Roberts, G.P.6
  • 79
    • 0034684238 scopus 로고    scopus 로고
    • Nitrophorins and related antihemostatic lipocalins from Rhodnius prolixus and other blood-sucking arthropods
    • Montfort, W. R., Weichsel, A., and Andersen, J. F. (2001) Nitrophorins and related antihemostatic lipocalins from Rhodnius prolixus and other blood-sucking arthropods. Biochim. Biophys. Acta 1482, 110-118.
    • (2001) Biochim. Biophys. Acta , vol.1482 , pp. 110-118
    • Montfort, W.R.1    Weichsel, A.2    Andersen, J.F.3
  • 81
    • 0032510778 scopus 로고    scopus 로고
    • The basic-helix-loop-helix-PAS orphan MOP3 forms transcriptionally active complexes with circadian and hypoxia factors
    • Hogenesch, J. B., Gu, Y. Z., Jain, S., and Bradfield, C. A. (1998) The basic-helix-loop-helix-PAS orphan MOP3 forms transcriptionally active complexes with circadian and hypoxia factors. Proc. Natl. Acad. Sci. USA 95, 5474-5479.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5474-5479
    • Hogenesch, J.B.1    Gu, Y.Z.2    Jain, S.3    Bradfield, C.A.4
  • 82
    • 0035919479 scopus 로고    scopus 로고
    • Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors
    • Rutter, J., Reick, M., Wu, L. C. and McKnight, S. L. (2001) Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors. Science 293, 510-514.
    • (2001) Science , vol.293 , pp. 510-514
    • Rutter, J.1    Reick, M.2    Wu, L.C.3    McKnight, S.L.4
  • 84
    • 0035919618 scopus 로고    scopus 로고
    • NPAS2: An analog of clock operative in the mammalian forebrain
    • Reick, M., Garcia, J. A., Dudley, C., and McKnight, S. L. (2001) NPAS2: an analog of clock operative in the mammalian forebrain. Science 293, 506-509.
    • (2001) Science , vol.293 , pp. 506-509
    • Reick, M.1    Garcia, J.A.2    Dudley, C.3    McKnight, S.L.4
  • 86
    • 0028073463 scopus 로고
    • Brain heme oxygenase isoenzymes and nitric oxide synthase are co-localized in select neurons
    • Vincent, S. R., Das, S., and Maines, M. D. (1994) Brain heme oxygenase isoenzymes and nitric oxide synthase are co-localized in select neurons. Neuroscience 63, 223-231.
    • (1994) Neuroscience , vol.63 , pp. 223-231
    • Vincent, S.R.1    Das, S.2    Maines, M.D.3
  • 88
    • 0035997367 scopus 로고    scopus 로고
    • Metabolism and the control of circadian rhythms
    • Rutter, J., Reick, M., and McKnight, S. L. (2002) Metabolism and the control of circadian rhythms. Annu. Rev. Biochem. 71, 307-331.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 307-331
    • Rutter, J.1    Reick, M.2    McKnight, S.L.3
  • 89
    • 0141876062 scopus 로고    scopus 로고
    • Circadian rhythms, oxidative stress, and antioxidative defense mechanisms
    • Hardeland, R., Coto-Montes, A., and Poeggeler, B. (2003) Circadian rhythms, oxidative stress, and antioxidative defense mechanisms. Chronobiol. Int. 20, 921-962.
    • (2003) Chronobiol. Int. , vol.20 , pp. 921-962
    • Hardeland, R.1    Coto-Montes, A.2    Poeggeler, B.3
  • 90
    • 0035544154 scopus 로고    scopus 로고
    • 15N chemical shift assignments of the N-terminal PAS domain of mPAS2
    • 15N chemical shift assignments of the N-terminal PAS domain of mPAS2. J. Biomol. NMR 21, 383-384.
    • (2001) J. Biomol. NMR , vol.21 , pp. 383-384
    • Holdeman, T.C.1    Gardner, K.H.2
  • 92
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.