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Volumn 44, Issue 3, 2005, Pages 939-946

Resonance Raman evidence for the presence of two heme pocket conformations with varied activities in CO-bound bovine soluble guanylate cyclase and their conversion

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL ORGANS; CELLS; IRON; ISOTOPES; RESONANCE; SUBSTRATES;

EID: 12344279982     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0489208     Document Type: Article
Times cited : (36)

References (50)
  • 1
    • 0027284439 scopus 로고
    • The nitric oxide and cGMP signal transduction system: Regulation and mechanism of action
    • Schmidt, H. H., Lohmann, S. M., and Walter, U. (1993) The nitric oxide and cGMP signal transduction system: regulation and mechanism of action, Biochim. Biophys. Acta 1178, 153-175.
    • (1993) Biochim. Biophys. Acta , vol.1178 , pp. 153-175
    • Schmidt, H.H.1    Lohmann, S.M.2    Walter, U.3
  • 2
    • 0029792562 scopus 로고    scopus 로고
    • Nitric oxide-cyclic GMP signal transduction system
    • Hobbs, A., and Ignarro, L. J. (1996) Nitric oxide-cyclic GMP signal transduction system. Methods. Enzymol. 269, 134-148.
    • (1996) Methods. Enzymol. , vol.269 , pp. 134-148
    • Hobbs, A.1    Ignarro, L.J.2
  • 5
    • 0025857699 scopus 로고
    • Purification of heme-containing soluble guanylyl cyclase
    • Mulsch, A., and Gerzer, R. (1991) Purification of heme-containing soluble guanylyl cyclase, Methods Enzymol. 195, 377-383.
    • (1991) Methods Enzymol. , vol.195 , pp. 377-383
    • Mulsch, A.1    Gerzer, R.2
  • 6
    • 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
    • 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.
    • (1994) Biochemistry , vol.33 , pp. 5636-5640
    • Stone, J.R.1    Marletta, M.A.2
  • 7
    • 0025001895 scopus 로고
    • Expression of soluble guanylyl cyclase. Catalytic activity requires two enzyme subunits
    • Harteneck, C., Koesling, D., Soling, A., Schultz, G., and Bohme, E. (1990) Expression of soluble guanylyl cyclase. Catalytic activity requires two enzyme subunits, FEBS Lett 272, 221-223.
    • (1990) FEBS Lett. , vol.272 , pp. 221-223
    • Harteneck, C.1    Koesling, D.2    Soling, A.3    Schultz, G.4    Bohme, E.5
  • 8
    • 0025968704 scopus 로고
    • Expression of soluble guanylate cyclase activity requires both enzyme subunits
    • Buechler, W. A., Nakane, M., and Murad, F. (1991) Expression of soluble guanylate cyclase activity requires both enzyme subunits, Biochem. Biophys. Res. Commun. 174, 351-357.
    • (1991) Biochem. Biophys. Res. Commun. , vol.174 , pp. 351-357
    • Buechler, W.A.1    Nakane, M.2    Murad, F.3
  • 9
    • 0031472326 scopus 로고    scopus 로고
    • Localization of the heme binding region in soluble guanylate cyclase
    • Zhao, Y., and Marietta, M. A. (1997) Localization of the heme binding region in soluble guanylate cyclase, Biochemistry 36, 15959-15964.
    • (1997) Biochemistry , vol.36 , pp. 15959-15964
    • Zhao, Y.1    Marietta, M.A.2
  • 11
    • 0032584316 scopus 로고    scopus 로고
    • Identification of histidine 105 in the β1 subunit of soluble guanylate cyclase as the heme proximal ligand
    • Zhao, Y., Schelvis, J. P. M., Babcock, G. T., and Marietta, M. A. (1998) Identification of histidine 105 in the β1 subunit of soluble guanylate cyclase as the heme proximal ligand, Biochemistry 37, 4502-4509.
    • (1998) Biochemistry , vol.37 , pp. 4502-4509
    • Zhao, Y.1    Schelvis, J.P.M.2    Babcock, G.T.3    Marietta, M.A.4
  • 12
    • 0021894599 scopus 로고
    • The pharmacological and physiological role of cyclic GMP in vascular smooth muscle relaxation
    • Ignarro, L. J., and Kadowitz, P. J. (1985) The pharmacological and physiological role of cyclic GMP in vascular smooth muscle relaxation, Annu. Rev. Pharmacol. Toxicol. 25, 171-191.
    • (1985) Annu. Rev. Pharmacol. Toxicol. , vol.25 , pp. 171-191
    • Ignarro, L.J.1    Kadowitz, P.J.2
  • 13
    • 0022599662 scopus 로고
    • Endothelium-dependent inhibition of platelet aggregation
    • Azuma, H., Ishikawa, M., and Sekizaki, S. (1986) Endothelium-dependent inhibition of platelet aggregation, Br. J. Pharmacol. 88, 411-415.
    • (1986) Br. J. Pharmacol. , vol.88 , pp. 411-415
    • Azuma, H.1    Ishikawa, M.2    Sekizaki, S.3
  • 14
    • 0024296032 scopus 로고
    • Endothelium-derived relaxing factor release on activation of NMDA receptors suggests role as intercellular messenger in the brain
    • Garthwaite, J., Charles, S. L., and Chess-Williams, R. (1988) Endothelium-derived relaxing factor release on activation of NMDA receptors suggests role as intercellular messenger in the brain, Nature 336, 385-388.
    • (1988) Nature , vol.336 , pp. 385-388
    • Garthwaite, J.1    Charles, S.L.2    Chess-Williams, R.3
  • 15
    • 0029028563 scopus 로고
    • Studies of the heme coordination and ligand binding properties of soluble guanylyl cyclase (sGC): Characterization of Fe(II)sGC and Fe(II)sGC(CO) by electronic absorption and magnetic circular dichroism spectroscopies and failure of CO to activate the enzyme
    • Burstyn, J. N., Yu, A. E., Dierks, E. A., Hawkins, B. K., and Dawson, J. H. (1995) Studies of the heme coordination and ligand binding properties of soluble guanylyl cyclase (sGC): characterization of Fe(II)sGC and Fe(II)sGC(CO) by electronic absorption and magnetic circular dichroism spectroscopies and failure of CO to activate the enzyme, Biochemistry 34, 5896-5903.
    • (1995) Biochemistry , vol.34 , pp. 5896-5903
    • Burstyn, J.N.1    Yu, A.E.2    Dierks, E.A.3    Hawkins, B.K.4    Dawson, J.H.5
  • 16
    • 0028861061 scopus 로고
    • Heme stoichiometry of heterodimeric soluble guanylate cyclase
    • Stone, J. R., and Marietta, M. A. (1995) Heme stoichiometry of heterodimeric soluble guanylate cyclase, Biochemistry 34, 14668-14674.
    • (1995) Biochemistry , vol.34 , pp. 14668-14674
    • Stone, J.R.1    Marietta, M.A.2
  • 17
    • 0022354914 scopus 로고
    • Effects of hydroxyl radical scavengers KCN and CO on ultraviolet light-induced activation of crude soluble guanylate cyclase
    • Karlsson, J. O., Axelsson, K. L., and Andersson, R. C. (1985) Effects of hydroxyl radical scavengers KCN and CO on ultraviolet light-induced activation of crude soluble guanylate cyclase, J. Cyclic Nucleotide Protein Phosphorylation Res. 10, 309-315.
    • (1985) J. Cyclic Nucleotide Protein Phosphorylation Res. , vol.10 , pp. 309-315
    • Karlsson, J.O.1    Axelsson, K.L.2    Andersson, R.C.3
  • 18
    • 0023490534 scopus 로고
    • Inhibition of platelet aggregation by carbon monoxide is mediated by activation of guanylate cyclase
    • Brune, B., and Ullrich, V. (1987) Inhibition of platelet aggregation by carbon monoxide is mediated by activation of guanylate cyclase, Mol. Pharmacol. 32, 497-504.
    • (1987) Mol. Pharmacol. , vol.32 , pp. 497-504
    • Brune, B.1    Ullrich, V.2
  • 19
    • 0030476908 scopus 로고    scopus 로고
    • Sensitizing soluble guanylyl cyclase to become a highly CO-sensitive enzyme
    • Friebe, A., Schultz, G., and Koesling, D. (1996) Sensitizing soluble guanylyl cyclase to become a highly CO-sensitive enzyme, EMBO J. 15, 6863-6868.
    • (1996) EMBO J. , vol.15 , pp. 6863-6868
    • Friebe, A.1    Schultz, G.2    Koesling, D.3
  • 20
    • 0029166002 scopus 로고
    • YC-1 inhibited human platelet aggregation through NO-independent activation of soluble guanylate cyclase
    • Wu, C. C., Ko, F. N., Kuo, S., Lee, F. Y., and Teng, C. M. (1995) YC-1 inhibited human platelet aggregation through NO-independent activation of soluble guanylate cyclase, Br. J. Pharmacol. 116, 1973-1978.
    • (1995) Br. J. Pharmacol. , vol.116 , pp. 1973-1978
    • Wu, C.C.1    Ko, F.N.2    Kuo, S.3    Lee, F.Y.4    Teng, C.M.5
  • 21
    • 0031566239 scopus 로고    scopus 로고
    • Inhibition of platelet adhesion to collagen by cGMP-elevating agents
    • Wu, C. C., Ko, F. N., and Teng, C. M. (1997) Inhibition of platelet adhesion to collagen by cGMP-elevating agents, Biochem. Biophys. Res. Commun. 231, 412-416.
    • (1997) Biochem. Biophys. Res. Commun. , vol.231 , pp. 412-416
    • Wu, C.C.1    Ko, F.N.2    Teng, C.M.3
  • 22
    • 0031046943 scopus 로고    scopus 로고
    • Effect of YC-1, an NO-independent, superoxide-sensitive stimulator of soluble guanylyl cyclase, on smooth muscle responsiveness to nitrovasodilators
    • Mulach, A., Bauersachs, J., Schafer, A., Stasch, J. P., Kast, R., and Buss, E. R. (1997) Effect of YC-1, an NO-independent, superoxide-sensitive stimulator of soluble guanylyl cyclase, on smooth muscle responsiveness to nitrovasodilators, Br. J. Pharmacol. 120, 681-689.
    • (1997) Br. J. Pharmacol. , vol.120 , pp. 681-689
    • Mulach, A.1    Bauersachs, J.2    Schafer, A.3    Stasch, J.P.4    Kast, R.5    Buss, E.R.6
  • 23
    • 0346643472 scopus 로고    scopus 로고
    • Effects of the soluble guanylyl cyclase activator, YC-1, on vascular tone, cyclic GMP levels and phosphodiesterase activity
    • Galle, J., Zabel, U., Hubner, U., Hatzelmann, A., Wagner, B., Wanner, C., and Schmide, H. H. H. (1999) Effects of the soluble guanylyl cyclase activator, YC-1, on vascular tone, cyclic GMP levels and phosphodiesterase activity, Br. J. Pharmacol. 127, 195-203.
    • (1999) Br. J. Pharmacol. , vol.127 , pp. 195-203
    • Galle, J.1    Zabel, U.2    Hubner, U.3    Hatzelmann, A.4    Wagner, B.5    Wanner, C.6    Schmide, H.H.H.7
  • 24
    • 0032078245 scopus 로고    scopus 로고
    • Synergistic activation of soluble guanylate cyclase by YC-1 and carbon monoxide: Implications for the role of cleavage of the iron-histidine bond during activation by nitric oxide
    • Stone, J. R., and Marietta, M. A. (1998) Synergistic activation of soluble guanylate cyclase by YC-1 and carbon monoxide: implications for the role of cleavage of the iron-histidine bond during activation by nitric oxide, Chem. Biol. 5, 255-261.
    • (1998) Chem. Biol. , vol.5 , pp. 255-261
    • Stone, J.R.1    Marietta, M.A.2
  • 25
    • 0032477817 scopus 로고    scopus 로고
    • Resonance Raman characterization of soluble guanylate cyclase expressed from baculovirus
    • Fan, B. C., Gupta, G., Danziger, R. S., Friedman, J., and Rousseau, D. L. (1998) Resonance Raman characterization of soluble guanylate cyclase expressed from baculovirus, Biochemistry 37, 1178-1184.
    • (1998) Biochemistry , vol.37 , pp. 1178-1184
    • Fan, B.C.1    Gupta, G.2    Danziger, R.S.3    Friedman, J.4    Rousseau, D.L.5
  • 26
    • 0030021905 scopus 로고    scopus 로고
    • Binding of nitric oxide and carbon monoxide to soluble guanylate cyclase as observed with Resonance Raman spectroscopy
    • Deinum, G., Stone, J. R., Babcock, G. T., and Marietta, M. A. (1996) Binding of nitric oxide and carbon monoxide to soluble guanylate cyclase as observed with Resonance Raman spectroscopy, Biochemistry 35, 1540-1547.
    • (1996) Biochemistry , vol.35 , pp. 1540-1547
    • Deinum, G.1    Stone, J.R.2    Babcock, G.T.3    Marietta, M.A.4
  • 27
    • 0030745411 scopus 로고    scopus 로고
    • Effects of GTP on bound nitric oxide of soluble guanylate cyclase probed by resonance Raman spectroscopy
    • Tomita, T., Ogura, T., Tsuyama, S., Imai, Y., and Kitagawa, T. (1997) Effects of GTP on bound nitric oxide of soluble guanylate cyclase probed by resonance Raman spectroscopy, Biochemistry 36, 10155-10160.
    • (1997) Biochemistry , vol.36 , pp. 10155-10160
    • Tomita, T.1    Ogura, T.2    Tsuyama, S.3    Imai, Y.4    Kitagawa, T.5
  • 28
    • 0028137347 scopus 로고
    • Resonance Raman spectroscopy of soluble guanylyl cyclase reveals displacement of distal and proximal heme ligands by NO
    • Yu, A. E., Hu, S. Z., Spiro, T. G., and Burstyn, J. N. (1994) Resonance Raman Spectroscopy of Soluble Guanylyl Cyclase Reveals Displacement of Distal and Proximal Heme Ligands by NO, J. Am. Chem. Soc. 116, 4117-4118.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 4117-4118
    • Yu, A.E.1    Hu, S.Z.2    Spiro, T.G.3    Burstyn, J.N.4
  • 29
    • 0028890481 scopus 로고
    • Electron paramagnetic resonance spectral evidence for the formation of a pentacoordinate-nitrosyl-heme complex on soluble guanylate cyclase
    • Stone, J. R., Sandos, R. H., Dunham, W. R., and Marietta, M. A. (1995) Electron paramagnetic resonance spectral evidence for the formation of a pentacoordinate-nitrosyl-heme complex on soluble guanylate cyclase, Biochem. Biophys. Res. Commun. 207, 572-577.
    • (1995) Biochem. Biophys. Res. Commun. , vol.207 , pp. 572-577
    • Stone, J.R.1    Sandos, R.H.2    Dunham, W.R.3    Marietta, M.A.4
  • 30
    • 0019879880 scopus 로고
    • Soluble guanylate cyclase purified from bovine lung contains heme and copper
    • Gerzer, R., Bohme, E., Hofmann, F., and Schultz, G. (1981) Soluble guanylate cyclase purified from bovine lung contains heme and copper, FEBS Lett. 132, 71-74.
    • (1981) FEBS Lett. , vol.132 , pp. 71-74
    • Gerzer, R.1    Bohme, E.2    Hofmann, F.3    Schultz, G.4
  • 31
    • 0032760663 scopus 로고    scopus 로고
    • Variable forms of soluble guanylyl cyclase: Protein-ligand interactions and the issue of activation by carbon monoxide
    • Vogel, K. M., Hu, S. Z., Spiro, T. G., Dierks, E. A., Yu, A. E., and Burstyn, J. N. (1999) Variable forms of soluble guanylyl cyclase: protein-ligand interactions and the issue of activation by carbon monoxide, J. Biol. Inorg. Chem. 4, 804-813.
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 804-813
    • Vogel, K.M.1    Hu, S.Z.2    Spiro, T.G.3    Dierks, E.A.4    Yu, A.E.5    Burstyn, J.N.6
  • 32
    • 0000348848 scopus 로고    scopus 로고
    • Bound CO is a molecular probe of electrostatic potential in the distal pocket of myoglobin
    • Phillips, G. N., Jr., Teodoro, M. L., Li, T., Smith, B., and Olson, J. S. (1999) Bound CO Is a Molecular Probe of Electrostatic Potential in the Distal Pocket of Myoglobin, J. Phys. Chem. B 103, 8817-8829.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 8817-8829
    • Phillips Jr., G.N.1    Teodoro, M.L.2    Li, T.3    Smith, B.4    Olson, J.S.5
  • 33
    • 0033520701 scopus 로고    scopus 로고
    • Determinants of the FeXO [X = C, N, O] vibrational frequencies in heme proteins and models from experiment and density functional theory
    • Vogel, K. M., Kozolowski, P. M., Zgierski, M. Z., and Spiro, T. G. (1999) Determinants of the FeXO [X = C, N, O] Vibrational Frequencies in Heme Proteins and Models from Experiment and Density Functional Theory, J. Am. Chem. Soc. 121, 9915-9921.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9915-9921
    • Vogel, K.M.1    Kozolowski, P.M.2    Zgierski, M.Z.3    Spiro, T.G.4
  • 34
    • 0032542021 scopus 로고    scopus 로고
    • Resonance Raman characterization of the heme domain of soluble guanylate cyclase
    • Schelvis, J. P. M., Zhao, Y., Marietta, M. A., and Babcock, G. T. (1998) Resonance Raman characterization of the heme domain of soluble guanylate cyclase, Biochemistry 37, 16289-16297.
    • (1998) Biochemistry , vol.37 , pp. 16289-16297
    • Schelvis, J.P.M.1    Zhao, Y.2    Marietta, M.A.3    Babcock, G.T.4
  • 36
    • 0030796164 scopus 로고    scopus 로고
    • Purification of bovine soluble guanylate cyclase and ADP-ribosylation on its small subunit by bacterial toxins
    • Tomita, T., Tsuyama, S., Imai, Y., and Kitagawa, T. (1997) Purification of bovine soluble guanylate cyclase and ADP-ribosylation on its small subunit by bacterial toxins, J. Biochem. 122, 531-536.
    • (1997) J. Biochem. , vol.122 , pp. 531-536
    • Tomita, T.1    Tsuyama, S.2    Imai, Y.3    Kitagawa, T.4
  • 37
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 38
    • 0037687336 scopus 로고    scopus 로고
    • YC-1 facilitates release of the proximal His residue in the NO and CO complexes of soluble guanylate cyclase
    • Makino, R., Obayashi, E., Homma, N., Shiro, Y., and Hori, H. (2003) YC-1 facilitates release of the proximal His residue in the NO and CO complexes of soluble guanylate cyclase, J. Biol. Chem. 278, 11130-11137.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11130-11137
    • Makino, R.1    Obayashi, E.2    Homma, N.3    Shiro, Y.4    Hori, H.5
  • 39
    • 0033578443 scopus 로고    scopus 로고
    • Kinetics and equilibria of soluble guanylate cyclase ligation by CO: Effect of YC-1
    • Kharitonov, V. G., Sharma, V. S., Magde, D., and Koesling, D. (1999) Kinetics and equilibria of soluble guanylate cyclase ligation by CO: effect of YC-1, Biochemistry 38, 10699-10706.
    • (1999) Biochemistry , vol.38 , pp. 10699-10706
    • Kharitonov, V.G.1    Sharma, V.S.2    Magde, D.3    Koesling, D.4
  • 40
    • 2342606948 scopus 로고    scopus 로고
    • Resonance Raman study on synergistic activation of soluble guanylate cyclase by imidazole, YC-1 and GTP
    • Pal, B., Li, Z., Ohta, T., Takenaka, S., Tsuyama, S., and Kitagawa, T. (2004) Resonance Raman study on synergistic activation of soluble guanylate cyclase by imidazole, YC-1 and GTP, J. Inorg. Biochem. 98, 824-832.
    • (2004) J. Inorg. Biochem. , vol.98 , pp. 824-832
    • Pal, B.1    Li, Z.2    Ohta, T.3    Takenaka, S.4    Tsuyama, S.5    Kitagawa, T.6
  • 41
    • 0021102431 scopus 로고
    • Resonance Raman detection of Fe-CO stretching and Fe-C-O bending vibrations in sterically hindered carbonmonoxy "strapped hemes". A structural probe of Fe-C-O distortion
    • Yu, N. T., Kerr, E. A., Ward, B., and Chang, C. K. (1983) Resonance Raman detection of Fe-CO stretching and Fe-C-O bending vibrations in sterically hindered carbonmonoxy "strapped hemes". A structural probe of Fe-C-O distortion, Biochemistry 22, 4534-4540.
    • (1983) Biochemistry , vol.22 , pp. 4534-4540
    • Yu, N.T.1    Kerr, E.A.2    Ward, B.3    Chang, C.K.4
  • 42
    • 0025776927 scopus 로고
    • Unusual CO bonding geometry in abnormal subunits of hemoglobin M Boston and hemoglobin M Saskatoon
    • Nagai, M., Yoneyama, Y., and Kitagawa, T. (1991) Unusual CO 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
  • 43
    • 0001640211 scopus 로고
    • Vibrational assignments of the FeCO unit of CO-Bound heme proteins revisited: Observation of a new CO-Isotope-Sensitive Raman band assignable to the FeCO bending fundamental
    • Hirota, S., Ogura, T., Shinzawa-Itoh, K., Yoshikawa, S., Nagai, M., and Kitagawa, T. (1994) Vibrational Assignments of the FeCO Unit of CO-Bound Heme Proteins Revisited: Observation of a New CO-Isotope-Sensitive Raman Band Assignable to the FeCO Bending Fundamental, J. Phys. Chem. 98, 6652-6660.
    • (1994) J. Phys. Chem. , vol.98 , pp. 6652-6660
    • Hirota, S.1    Ogura, T.2    Shinzawa-Itoh, K.3    Yoshikawa, S.4    Nagai, M.5    Kitagawa, T.6
  • 44
    • 0029152608 scopus 로고
    • 2 and Fe-CO vibrations and potentioal anharmonicities for oxyhemoglobin and carbon monoxyhemoglobin. Evidences supporting a new assignment of the Fe-C-O bending fundamental
    • 2 and Fe-CO Vibrations and Potentioal Anharmonicities for Oxyhemoglobin and Carbon monoxyhemoglobin. Evidences Supporting a New Assignment of the Fe-C-O Bending Fundamental, J. Am. Chem. Soc. 117, 821-822.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 821-822
    • Hirota, S.1    Ogura, T.2    Kitagawa, T.3
  • 45
    • 0032578154 scopus 로고    scopus 로고
    • Resonance Raman studies of hemoglobin with selectively deuterated hemes. A new perspective on the controversial assignment of the references. Fe-CO bending mode
    • Rajani, C., and Kincaid, J. R. (1998) Resonance Raman Studies of Hemoglobin with Selectively Deuterated Hemes. A New Perspective on the Controversial Assignment of the references. Fe-CO Bending Mode, J. Am. Chem. Soc. 120, 7278-7285.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7278-7285
    • Rajani, C.1    Kincaid, J.R.2
  • 47
    • 1642576030 scopus 로고    scopus 로고
    • Identification of residues crucially involved in the binding of the heme moiety of soluble guanylate cyclase
    • Schmidt, P. M., Schramm, M., Schroder, H., Wunder, F., and Stasch, J.-P. (2004) Identification of residues crucially involved in the binding of the heme moiety of soluble guanylate cyclase, J. Biol. Chem. 279, 3025-3032.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3025-3032
    • Schmidt, P.M.1    Schramm, M.2    Schroder, H.3    Wunder, F.4    Stasch, J.-P.5
  • 48
    • 0033576311 scopus 로고    scopus 로고
    • A point-mutated guanylyl cyclase with features of the YC-1-stimulated enzyme: Implications for the YC-1 binding site?
    • Friebe, A., Russwurm, M., Mergia, E., and Koesling, D. (1999) A point-mutated guanylyl cyclase with features of the YC-1-stimulated enzyme: implications for the YC-1 binding site? Biochemistry 38, 15253-15257.
    • (1999) Biochemistry , vol.38 , pp. 15253-15257
    • Friebe, A.1    Russwurm, M.2    Mergia, E.3    Koesling, D.4
  • 49
    • 1542638765 scopus 로고    scopus 로고
    • Functional characterization of nitric oxide and YC-1 activation of soluble guanylyl cyclase: Structural implication for the YC-1 binding site?
    • Lamothe, M., Chang, F.-J., Balashova, N., Shirokov, R., and Beuve, A. (2004) Functional Characterization of Nitric Oxide and YC-1 Activation of Soluble Guanylyl Cyclase: Structural Implication for the YC-1 Binding Site? Biochemistry 43, 3039-3048.
    • (2004) Biochemistry , vol.43 , pp. 3039-3048
    • Lamothe, M.1    Chang, F.-J.2    Balashova, N.3    Shirokov, R.4    Beuve, A.5
  • 50
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.