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Volumn 287, Issue 9, 2012, Pages 6851-6859

Quaternary structure controls ligand dynamics in soluble guanylate cyclase

Author keywords

[No Author keywords available]

Indexed keywords

BIMOLECULAR ASSOCIATION; BOND-BREAKING; CONFORMATIONAL CHANGE; FUNCTIONAL DOMAINS; GEMINATE REBINDING; GUANYLATE CYCLASE; HEME DOMAIN; HETERODIMERIC ENZYMES; QUATERNARY STRUCTURE; SOLUBLE GUANYLATE CYCLASE (SGC); STRUCTURAL STRAIN;

EID: 84863142015     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.299297     Document Type: Article
Times cited : (19)

References (41)
  • 1
    • 0033549499 scopus 로고    scopus 로고
    • Discovery of some of the biological effects of nitric oxide and its role in cell signaling (Nobel lecture)
    • Murad, F. (1999) Discovery of some of the biological effects of nitric oxide and its role in cell signaling (Nobel lecture). Angew. Chem. Int. Ed. 38, 1857-1868
    • (1999) Angew. Chem. Int. Ed. , vol.38 , pp. 1857-1868
    • Murad, F.1
  • 2
    • 0023505509 scopus 로고
    • Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide
    • Ignarro, L. J., Buga, G. M., Wood, K. S., Byrns, R. E., and Chaudhuri, G. (1987) Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide. Proc. Natl. Acad. Sci. U.S.A. 84, 9265-9269
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 9265-9269
    • Ignarro, L.J.1    Buga, G.M.2    Wood, K.S.3    Byrns, R.E.4    Chaudhuri, G.5
  • 3
    • 0023198721 scopus 로고
    • Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
    • DOI 10.1038/327524a0
    • Palmer, R. M., Ferrige, A. G., and Moncada, S. (1987) Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor. Nature 327, 524-526 (Pubitemid 17085822)
    • (1987) Nature , vol.327 , Issue.6122 , pp. 524-526
    • Palmer, R.M.J.1    Ferrige, A.G.2    Moncada, S.3
  • 4
    • 46349086870 scopus 로고    scopus 로고
    • Vascular system: Role of nitric oxide in cardiovascular diseases
    • Bian, K., Doursout, M. F., and Murad, F. (2008) Vascular system: role of nitric oxide in cardiovascular diseases. J. Clin. Hypertens. 10, 304-310
    • (2008) J. Clin. Hypertens. , vol.10 , pp. 304-310
    • Bian, K.1    Doursout, M.F.2    Murad, F.3
  • 5
    • 34548222509 scopus 로고    scopus 로고
    • Nitric oxide in the pulmonary vasculature
    • DOI 10.1161/ATVBAHA.107.142943, PII 0004360520070900000003
    • Coggins, M. P., and Bloch, K. D. (2007) Nitric oxide in the pulmonary vasculature. Arterioscler. Thromb. Vasc. Biol. 27, 1877-1885 (Pubitemid 47315641)
    • (2007) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.27 , Issue.9 , pp. 1877-1885
    • Coggins, M.P.1    Bloch, K.D.2
  • 6
    • 34347348956 scopus 로고    scopus 로고
    • Nitric oxide, chronic inflammation and autoimmunity
    • DOI 10.1016/j.imlet.2007.04.013, PII S0165247807001046
    • Nagy, G., Clark, J. M., Buzás, E. I., Gorman, C. L., and Cope, A. P. (2007) Nitric oxide, chronic inflammation and autoimmunity. Immunol. Lett. 111, 1-5 (Pubitemid 47017476)
    • (2007) Immunology Letters , vol.111 , Issue.1 , pp. 1-5
    • Nagy, G.1    Clark, J.M.2    Buzas, E.I.3    Gorman, C.L.4    Cope, A.P.5
  • 7
    • 0030021905 scopus 로고    scopus 로고
    • Binding of nitric oxide and carbon monoxide to soluble guanylate cyclase as observed with resonance Raman spectroscopy
    • DOI 10.1021/bi952440m
    • Deinum, G., Stone, J. R., Babcock, G. T., and Marletta, M. A. (1996) Binding of nitric oxide and carbon monoxide to soluble guanylate cyclase as observed with Resonance raman spectroscopy. Biochemistry 35, 1540-1547 (Pubitemid 26055288)
    • (1996) Biochemistry , vol.35 , Issue.5 , pp. 1540-1547
    • Deinum, G.1    Stone, J.R.2    Babcock, G.T.3    Marletta, M.A.4
  • 8
    • 9444240366 scopus 로고    scopus 로고
    • Femtomolar sensitivity of a NO sensor from Clostridium botulinum
    • DOI 10.1126/science.1103596
    • Nioche, P., Berka, V., Vipond, J., Minton, N., Tsai, A. L., and Raman, C. S. (2004) Femtomolar sensitivity of a NO sensor from Clostridium botulinum. Science 306, 1550-1553 (Pubitemid 39564949)
    • (2004) Science , vol.306 , Issue.5701 , pp. 1550-1553
    • Nioche, P.1    Berka, V.2    Vipond, J.3    Minton, N.4    Tsai, A.-L.5    Raman, C.S.6
  • 10
    • 25144432064 scopus 로고    scopus 로고
    • Amolecular basis for NO selectivity in soluble guanylate cyclase
    • Boon, E. M., Huang, S. H., and Marletta, M. A. (2005)Amolecular basis for NO selectivity in soluble guanylate cyclase. Nat. Chem. Biol. 1, 53-59
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 53-59
    • Boon, E.M.1    Huang, S.H.2    Marletta, M.A.3
  • 11
    • 33846491964 scopus 로고    scopus 로고
    • NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism
    • DOI 10.1038/sj.emboj.7601521, PII 7601521
    • Ma, X., Sayed, N., Beuve, A., and van den Akker, F. (2007) NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism. EMBO J. 26, 578-588 (Pubitemid 46160957)
    • (2007) EMBO Journal , vol.26 , Issue.2 , pp. 578-588
    • Ma, X.1    Sayed, N.2    Beuve, A.3    Van Den, A.F.4
  • 12
    • 77954568592 scopus 로고    scopus 로고
    • Structure of cinaciguat (BAY 58-2667) bound to Nostoc H-NOX domain reveals insights into hememimetic activation of the soluble guanylyl cyclase
    • Martin, F., Baskaran, P., Ma, X., Dunten, P. W., Schaefer, M., Stasch, J. P., Beuve, A., and van den Akker, F. (2010) Structure of cinaciguat (BAY 58-2667) bound to Nostoc H-NOX domain reveals insights into hememimetic activation of the soluble guanylyl cyclase. J. Biol. Chem. 285, 22651-22657
    • (2010) J. Biol. Chem. , vol.285 , pp. 22651-22657
    • Martin, F.1    Baskaran, P.2    Ma, X.3    Dunten, P.W.4    Schaefer, M.5    Stasch, J.P.6    Beuve, A.7    Van Den Akker, F.8
  • 15
    • 0038712079 scopus 로고    scopus 로고
    • Geminate recombination of nitric oxide to endothelial nitric-oxide synthase and mechanistic implications
    • Négrerie, M., Berka, V., Vos, M. H., Liebl, U., Lambry, J. C., Tsai, A. L., and Martin, J. L. (1999) Geminate recombination of nitric oxide to endothelial nitric-oxide synthase and mechanistic implications. J. Biol. Chem. 274, 24694-24702
    • (1999) J. Biol. Chem. , vol.274 , pp. 24694-24702
    • Négrerie, M.1    Berka, V.2    Vos, M.H.3    Liebl, U.4    Lambry, J.C.5    Tsai, A.L.6    Martin, J.L.7
  • 18
    • 0035861734 scopus 로고    scopus 로고
    • Control of nitric oxide dynamics by guanylate cyclase in its activated state
    • Négrerie, M., Bouzhir, L., Martin, J. L., and Liebl, U. (2001) Control of nitric oxide dynamics by guanylate cyclase in its activated state. J. Biol. Chem. 276, 46815-46821
    • (2001) J. Biol. Chem. , vol.276 , pp. 46815-46821
    • Négrerie, M.1    Bouzhir, L.2    Martin, J.L.3    Liebl, U.4
  • 19
    • 33746540471 scopus 로고    scopus 로고
    • Ultrafast heme dynamics in ferrous versus ferric cytochrome c studied by time-resolved resonance Raman and transient absorption spectroscopy
    • DOI 10.1021/jp0559377
    • Negrerie, M., Cianetti, S., Vos, M. H., Martin, J. L., and Kruglik, S. G. (2006) Ultrafast heme dynamics in ferrous versus ferric cytochrome c studied by time-resolved resonance Raman and transient absorption spectroscopy. J. Phys. Chem. B 110, 12766-12781 (Pubitemid 44139469)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.25 , pp. 12766-12781
    • Negrerie, M.1    Cianetti, S.2    Vos, M.H.3    Jean-Louis, M.4    Kruglik, S.G.5
  • 20
    • 0032614730 scopus 로고    scopus 로고
    • New high-sensitivity 10-ns time-resolution spectrophotometric technique adapted to in vivo analysis of the photosynthetic apparatus
    • Beal, D., Rappaport, F., and Joliot, P. (1999) A new high-sensitivity 10-ns time-resolution spectrophotometric technique adapted to in vivo analysis of the photosynthetic apparatus. Rev. Sci. Instrum. 70, 202-207 (Pubitemid 129308951)
    • (1999) Review of Scientific Instruments , vol.70 , Issue.1 PART 1 , pp. 202-207
    • Beal, D.1    Rappaport, F.2    Joliot, P.3
  • 21
    • 28944448524 scopus 로고    scopus 로고
    • Characterization of functional heme domains from soluble guanylate cyclase
    • DOI 10.1021/bi051601b
    • Karow, D. S., Pan, D., Davis, J. H., Behrends, S., Mathies, R. A., and Marletta, M. A. (2005) Characterization of functional heme domains from soluble guanylate cyclase. Biochemistry 44, 16266-16274 (Pubitemid 41785825)
    • (2005) Biochemistry , vol.44 , Issue.49 , pp. 16266-16274
    • Karow, D.S.1    Pan, D.2    Davis, J.H.3    Behrends, S.4    Mathies, R.A.5    Marletta, M.A.6
  • 22
    • 3543102591 scopus 로고    scopus 로고
    • Spectroscopic characterization of the soluble guanylate cyclase-like heme domains from Vibrio cholerae and Thermoanaerobacter tengcongensis
    • DOI 10.1021/bi049374l
    • Karow, D. S., Pan, D., Tran, R., Pellicena, P., Presley, A., Mathies, R. A., and Marletta, M. A. (2004) Spectroscopic characterization of the soluble guanylate cyclase-like heme domains from Vibrio cholerae and Thermoanaerobacter tengcongensis. Biochemistry 43, 10203-10211 (Pubitemid 39030911)
    • (2004) Biochemistry , vol.43 , Issue.31 , pp. 10203-10211
    • Karow, D.S.1    Pan, D.2    Tran, R.3    Pellicena, P.4    Presley, A.5    Mathies, R.A.6    Marletta, M.A.7
  • 23
    • 0035873788 scopus 로고    scopus 로고
    • Water penetration and binding to ferric myoglobin
    • DOI 10.1021/bi010067e
    • Cao, W., Christian, J. F., Champion, P. M., Rosca, F., and Sage J. T. (2001) Water penetration and binding to ferric myoglobin. Biochemistry 40, 5728-5737 (Pubitemid 32440877)
    • (2001) Biochemistry , vol.40 , Issue.19 , pp. 5728-5737
    • Cao, W.1    Christian, J.F.2    Champion, P.M.3    Rosca, F.4    Sage, J.T.5
  • 24
    • 0034329425 scopus 로고    scopus 로고
    • Unprecedented proximal binding of nitric oxide to heme: Implications for guanylate cyclase
    • Lawson, D. M., Stevenson, C. E., 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.2    Andrew, C.R.3    Eady, R.R.4
  • 25
    • 77956637397 scopus 로고    scopus 로고
    • Modulating heme redox potential through protein-induced porphyrin distortion
    • Olea, C., Jr., Kuriyan, J., and Marletta, M. A. (2010) Modulating heme redox potential through protein-induced porphyrin distortion. J. Am. Chem. Soc. 132, 12794-12795
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 12794-12795
    • Olea Jr., C.1    Kuriyan, J.2    Marletta, M.A.3
  • 27
    • 33847720350 scopus 로고    scopus 로고
    • Dissociation of nitric oxide from soluble guanylate cyclase and heme-nitric oxide/oxygen binding domain constructs
    • DOI 10.1074/jbc.M606327200
    • Winger, J. A., Derbyshire, E. R., and Marletta, M. A. (2007) Dissociation of nitric oxide from soluble guanylate cyclase and heme-nitric oxide/oxygen binding domain constructs. J. Biol. Chem. 282, 897-907 (Pubitemid 47076536)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.2 , pp. 897-907
    • Winger, J.A.1    Derbyshire, E.R.2    Marletta, M.A.3
  • 28
    • 33748804669 scopus 로고    scopus 로고
    • Ligand selectivity of soluble guanylyl cyclase: Effect of the hydrogen-bonding tyrosine in the distal heme pocket on binding of oxygen, nitric oxide, and carbon monoxide
    • DOI 10.1074/jbc.M601078200
    • Martin, E., Berka, V., Bogatenkova, E., Murad, F., and Tsai, A. L. (2006) Ligand selectivity of soluble guanylyl cyclase: Effect of the hydrogen-bonding tyrosine in the distal heme pocket on binding of oxygen, nitric oxide, and carbon monoxide. J. Biol. Chem. 281, 27836-27845 (Pubitemid 44414495)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.38 , pp. 27836-27845
    • Martin, E.1    Berka, V.2    Bogatenkova, E.3    Murad, F.4    Tsai, A.-L.5
  • 29
    • 77952942728 scopus 로고    scopus 로고
    • Incorporation of tyrosine and glutamine residues into the soluble guanylate cyclase heme distal pocket alters NO and O2 binding
    • Derbyshire, E. R., Deng, S., and Marletta, M. A. (2010) Incorporation of tyrosine and glutamine residues into the soluble guanylate cyclase heme distal pocket alters NO and O2 binding. J. Biol. Chem. 285, 17471-17478
    • (2010) J. Biol. Chem. , vol.285 , pp. 17471-17478
    • Derbyshire, E.R.1    Deng, S.2    Marletta, M.A.3
  • 31
    • 0028228808 scopus 로고
    • Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states
    • DOI 10.1021/bi00184a036
    • Stone, J. R., and Marletta, M. A. (1994) Soluble guanylate cyclase from bovine lung: activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states. Biochemistry 33, 5636-5640 (Pubitemid 24163003)
    • (1994) Biochemistry , vol.33 , Issue.18 , pp. 5636-5640
    • Stone, J.R.1    Marletta, M.A.2
  • 32
    • 0025181994 scopus 로고
    • Activation of soluble guanylate cyclase by carbon monoxide and inhibition by superoxide anion
    • Brüne, B., Schmidt, K. U., and Ullrich, V. (1990) Activation of soluble guanylate cyclase by carbon monoxide and inhibition by superoxide anion. Eur. J. Biochem. 192, 683-688 (Pubitemid 20316870)
    • (1990) European Journal of Biochemistry , vol.192 , Issue.3 , pp. 683-688
    • Brune, B.1    Schmidt, K.-U.2    Ullrich, V.3
  • 33
    • 17744362896 scopus 로고    scopus 로고
    • CO rebinding to protoheme: Investigations of the proximal and distal contributions to the geminate rebinding barrier
    • DOI 10.1021/ja042365f
    • 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 (Pubitemid 40577642)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.16 , 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
  • 34
    • 0032584325 scopus 로고    scopus 로고
    • A possible allosteric communication pathway identified through a resonance raman study of four β337 mutants of human hemoglobin A
    • DOI 10.1021/bi9708693
    • Peterson, E. S., and Friedman, J. M. (1998) A possible allosteric communication pathway identified through a resonance Raman study of four β37 mutants of human hemoglobin A. Biochemistry 37, 4346-4357 (Pubitemid 28217153)
    • (1998) Biochemistry , vol.37 , Issue.13 , pp. 4346-4357
    • Peterson, E.S.1    Friedman, J.M.2
  • 35
    • 67649553367 scopus 로고    scopus 로고
    • Linking conformation change to hemoglobin activation via chain-selective time-resolved resonance Raman spectroscopy of protoheme/mesoheme hybrids
    • Balakrishnan, G., Ibrahim, M., Mak, P. J., Hata, J., Kincaid, J. R., and Spiro, T. G. (2009) Linking conformation change to hemoglobin activation via chain-selective time-resolved resonance Raman spectroscopy of protoheme/mesoheme hybrids. J. Biol. Inorg. Chem. 14, 741-750
    • (2009) J. Biol. Inorg. Chem. , vol.14 , pp. 741-750
    • Balakrishnan, G.1    Ibrahim, M.2    Mak, P.J.3    Hata, J.4    Kincaid, J.R.5    Spiro, T.G.6
  • 36
    • 0031722046 scopus 로고    scopus 로고
    • Myoglobin mutants giving the largest geminate yield in CO rebinding in the nanosecond time domain
    • Sugimoto, T., Unno, M., Shiro, Y., Dou, Y., and Ikeda-Saito, M. (1998) Myoglobin mutants giving the largest geminate yield in CO rebinding in the nanosecond time domain. Biophys. J. 75, 2188-2194 (Pubitemid 28492101)
    • (1998) Biophysical Journal , vol.75 , Issue.5 , pp. 2188-2194
    • Sugimoto, T.1    Unno, M.2    Shiro, Y.3    Dou, Y.4    Ikeda-Saito, M.5
  • 37
    • 79953185359 scopus 로고    scopus 로고
    • Blocking the gate to ligand entry in human hemoglobin
    • Birukou I., Soman, J., and Olson, J. S. (2011) Blocking the gate to ligand entry in human hemoglobin. J. Biol. Chem. 286, 10515-10529
    • (2011) J. Biol. Chem. , vol.286 , pp. 10515-10529
    • Birukou, I.1    Soman, J.2    Olson, J.S.3
  • 38
    • 0029560867 scopus 로고
    • The ferrous heme of soluble guanylate cyclase: Formation of hexacoordinate complexes with carbon monoxide and nitrosomethane
    • DOI 10.1021/bi00050a021
    • Stone, J. R., and Marletta, M. A. (1995) The ferrous heme of soluble guanylate cyclase: Formation of hexacoordinate complexes with carbon monoxide and nitrosomethane. Biochemistry 34, 16397-16403 (Pubitemid 26006484)
    • (1995) Biochemistry , vol.34 , Issue.50 , pp. 16397-16403
    • Stone, J.R.1    Marletta, M.A.2
  • 39
    • 0028409107 scopus 로고
    • Discovery of new ligand binding pathways in myoglobin by random mutagenesis
    • Huang, X., and Boxer, S. G. (1994) Discovery of new ligand binding pathways in myoglobin by random mutagenesis. Nat. Struct. Biol. 1, 226-229
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 226-229
    • Huang, X.1    Boxer, S.G.2
  • 40
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in hemoglobin
    • Perutz, M. F. (1970) Stereochemistry of cooperative effects in hemoglobin. Nature 228, 726-739
    • (1970) Nature , vol.228 , pp. 726-739
    • Perutz, M.F.1
  • 41
    • 84655172853 scopus 로고    scopus 로고
    • Efficient expression of human soluble guanylate cyclase in Escherichia coli and its signaling-related interaction with nitric oxide
    • Zhong, F., Wang, H., Ying, T., Huang, Z. X., and Tan, X. (2010) Efficient expression of human soluble guanylate cyclase in Escherichia coli and its signaling-related interaction with nitric oxide. Amino Acids 39, 399-408
    • (2010) Amino Acids , vol.39 , pp. 399-408
    • Zhong, F.1    Wang, H.2    Ying, T.3    Huang, Z.X.4    Tan, X.5


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