메뉴 건너뛰기




Volumn 44, Issue 49, 2005, Pages 16266-16274

Characterization of functional heme domains from soluble guanylate cyclase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; HEMODYNAMICS; MOLECULAR STRUCTURE; OXIDATION;

EID: 28944448524     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051601b     Document Type: Article
Times cited : (69)

References (42)
  • 1
    • 0031472326 scopus 로고    scopus 로고
    • Localization of the heme binding region of soluble guanylate cyclase
    • Zhao, Y., and Marletta, M. A. (1997) Localization of the heme binding region of soluble guanylate cyclase, Biochemistry 36, 15959-15964.
    • (1997) Biochemistry , vol.36 , pp. 15959-15964
    • Zhao, Y.1    Marletta, M.A.2
  • 2
    • 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
  • 4
    • 9144261238 scopus 로고    scopus 로고
    • Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins
    • Iyer, L. M., Anantharaman, V., and Aravind, L. (2003) Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins, BMC Genomics 6, 490-497.
    • (2003) BMC Genomics , vol.6 , pp. 490-497
    • Iyer, L.M.1    Anantharaman, V.2    Aravind, L.3
  • 5
    • 4444333687 scopus 로고    scopus 로고
    • Crystal structure of an oxygen binding H-NOX domain related to soluble guanylate cyclases
    • Pellicena, P., Karow, D. S., Boon, E. M., Marletta, M. A., and Kuriyan, J. (2004) Crystal structure of an oxygen binding H-NOX domain related to soluble guanylate cyclases, Proc. Natl. Acad. Sci. U.S.A. 101, 12854-12859.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 12854-12859
    • Pellicena, P.1    Karow, D.S.2    Boon, E.M.3    Marletta, M.A.4    Kuriyan, J.5
  • 6
    • 3543102591 scopus 로고    scopus 로고
    • Spectroscopic characterization of the sGC-like heme domains from Vibrio cholerae and Thermoanaerobacter tengcongensis
    • Karow, D. S., Pan, D., Tran, R., Pellicena, P., Presley, A., Mathies, R. A., and Marletta, M. A. (2004) Spectroscopic characterization of the sGC-like heme domains from Vibrio cholerae and Thermoanaerobacter tengcongensis, Biochemistry 43, 10203-10211.
    • (2004) Biochemistry , vol.43 , 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
  • 7
    • 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., Babcock, G. T., and Marletta, 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.2    Babcock, G.T.3    Marletta, M.A.4
  • 8
    • 0025614438 scopus 로고
    • A new form of guanylyl cyclase is preferentially expressed in rat kidney
    • Yuen, P. S. T., Potter, L. R., and Garbers, D. L. (1990) A new form of guanylyl cyclase is preferentially expressed in rat kidney, Biochemistry 29, 10872-10878.
    • (1990) Biochemistry , vol.29 , pp. 10872-10878
    • Yuen, P.S.T.1    Potter, L.R.2    Garbers, D.L.3
  • 9
    • 0034728793 scopus 로고    scopus 로고
    • The β2 subunit of soluble guanylyl cyclase contains a human-specific frameshift and is expressed in gastric carcinoma
    • Behrends, S., and Vehse, K. (2000) The β2 subunit of soluble guanylyl cyclase contains a human-specific frameshift and is expressed in gastric carcinoma, Biochem. Biophys. Res. Commun. 271, 64-69.
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 64-69
    • Behrends, S.1    Vehse, K.2
  • 10
    • 0035903155 scopus 로고    scopus 로고
    • Nitric oxide activates the β2 subunit of soluble guanylyl cyclase in the absence of a second subunit
    • Koglin, M., Vehse, K., Budaeus, L., Scholz, H., and Behrends, S. (2001) Nitric oxide activates the β2 subunit of soluble guanylyl cyclase in the absence of a second subunit, J. Biol. Chem. 276, 30737-30743.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30737-30743
    • Koglin, M.1    Vehse, K.2    Budaeus, L.3    Scholz, H.4    Behrends, S.5
  • 11
    • 0037961228 scopus 로고    scopus 로고
    • Properties of NO-activated guanylyl cyclases expressed in cells
    • Gibb, B. J., Wykes, V., and Garthwaite, J. (2003) Properties of NO-activated guanylyl cyclases expressed in cells, Br. J. Pharmacol. 139, 1032-1040.
    • (2003) Br. J. Pharmacol. , vol.139 , pp. 1032-1040
    • Gibb, B.J.1    Wykes, V.2    Garthwaite, J.3
  • 12
    • 0032400370 scopus 로고    scopus 로고
    • Regeneration of the ferrous heme of soluble guanylate cyclase from the nitric oxide complex: Acceleration by thiols and oxyhemoglobin
    • Brandish, P. E., Buechler, W., and Marletta, M. A. (1998) Regeneration of the ferrous heme of soluble guanylate cyclase from the nitric oxide complex: Acceleration by thiols and oxyhemoglobin. Biochemistry 37, 16898-16907.
    • (1998) Biochemistry , vol.37 , pp. 16898-16907
    • Brandish, P.E.1    Buechler, W.2    Marletta, M.A.3
  • 13
    • 0347383758 scopus 로고    scopus 로고
    • Modeller: Generation and refinement of homology-based protein structure models
    • Fiser, A., and Sali, A. (2003) Modeller: Generation and refinement of homology-based protein structure models. Methods Enzymol. 374, 461-491.
    • (2003) Methods Enzymol , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 14
    • 0036570054 scopus 로고    scopus 로고
    • Time-resolved resonance Raman analysis of chromophore structural changes in the formation and decay of rhodopsin's BSI intermediate
    • Pan, D., Ganim, Z., Kim, J. E., Verhoeven, M. A., Lugtenburg, J., and Mathies, R. A. (2002) Time-resolved resonance Raman analysis of chromophore structural changes in the formation and decay of rhodopsin's BSI intermediate, J. Am. Chem. Soc. 124, 4857-4864.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4857-4864
    • Pan, D.1    Ganim, Z.2    Kim, J.E.3    Verhoeven, M.A.4    Lugtenburg, J.5    Mathies, R.A.6
  • 15
    • 0019739893 scopus 로고
    • Preparation of derivatives of ferrous and ferric hemoglobin
    • (Antonini, E., Rossi-Bernardi, L., and Chiancone, E., Eds.) Academic Press, New York
    • Di Iorio, E. E. (1981) Preparation of derivatives of ferrous and ferric hemoglobin, in Hemoglobins (Antonini, E., Rossi-Bernardi, L., and Chiancone, E., Eds.) pp 57-71, Academic Press, New York.
    • (1981) Hemoglobins , pp. 57-71
    • Di Iorio, E.E.1
  • 16
    • 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 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.
    • (1996) Biochemistry , vol.35 , pp. 1540-1547
    • Deinum, G.1    Stone, J.R.2    Babcock, G.T.3    Marletta, M.A.4
  • 17
    • 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 Kitigawa, 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    Kitigawa, T.5
  • 18
    • 2842546487 scopus 로고
    • Structural correlations and vinyl influences in resonance Raman spectra of protoheme complexes and proteins
    • Choi, S., Spiro, T. G., Langry, K. C., Smith, K. M., Budd, D. L., and La Mar, G. N. (1982) Structural correlations and vinyl influences in resonance Raman spectra of protoheme complexes and proteins, J. Am. Chem. Soc. 104, 4345-4351.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4345-4351
    • Choi, S.1    Spiro, T.G.2    Langry, K.C.3    Smith, K.M.4    Budd, D.L.5    La Mar, G.N.6
  • 19
    • 0020484829 scopus 로고
    • Resonance Raman investigation of nitric oxide bonding in nitrosylhemoglobin a and -myoglobin: Detection of bound N-O stretching and Fe-NO stretching vibrations from the hexacoordinated NO-heme complex
    • Tsubaki, M., and Yu, N. T. (1982) Resonance Raman investigation of nitric oxide bonding in nitrosylhemoglobin A and -myoglobin: Detection of bound N-O stretching and Fe-NO stretching vibrations from the hexacoordinated NO-heme complex, Biochemistry 21, 1140-1144.
    • (1982) Biochemistry , vol.21 , pp. 1140-1144
    • Tsubaki, M.1    Yu, N.T.2
  • 20
    • 0000506287 scopus 로고
    • Resonance Raman spectra of the nitric oxide adducts of ferrous cytochrome P450cam in the presence of various substrates
    • Hu, S., and Kincaid, J. R. (1991) Resonance Raman spectra of the nitric oxide adducts of ferrous cytochrome P450cam in the presence of various substrates, J. Am. Chem. Soc. 113, 9760-9766.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9760-9766
    • Hu, S.1    Kincaid, J.R.2
  • 21
    • 0020484765 scopus 로고
    • Resonance Raman investigation of carbon monoxide bonding in (carbon monoxy)hemoglobin and -myoglobin: Detection of Fe-CO stretching and Fe-C-O 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 Fe-CO stretching and Fe-C-O 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
  • 22
    • 0035846626 scopus 로고    scopus 로고
    • FTIR and resonance Raman studies of nitric oxide binding to H93G cavity mutants of myoglobin
    • Thomas, M. R., Brown, D., Franzen, S., and Boxer, S. G. (2001) FTIR and resonance Raman studies of nitric oxide binding to H93G cavity mutants of myoglobin, Biochemistry 40, 15047-15056.
    • (2001) Biochemistry , vol.40 , pp. 15047-15056
    • Thomas, M.R.1    Brown, D.2    Franzen, S.3    Boxer, S.G.4
  • 23
    • 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., 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.2    Spiro, T.G.3    Dierks, E.A.4    Yu, A.E.5    Burstyn, J.N.6
  • 24
    • 0037117726 scopus 로고    scopus 로고
    • A comparative resonance Raman analysis of heme-binding PAS domains: Heme iron coordination structures of the BjFixL, AxPDEA1, EcDos, and MtDos proteins
    • Tomita, T., Gonzalez, G., Chang, A. L., Ikeda-Saito, M., and Gilles-Gonzalez, M. A. (2002) A comparative resonance Raman analysis of heme-binding PAS domains: Heme iron coordination structures of the BjFixL, AxPDEA1, EcDos, and MtDos proteins, Biochemistry 41, 4819-4826.
    • (2002) Biochemistry , vol.41 , pp. 4819-4826
    • Tomita, T.1    Gonzalez, G.2    Chang, A.L.3    Ikeda-Saito, M.4    Gilles-Gonzalez, M.A.5
  • 25
    • 0032542021 scopus 로고    scopus 로고
    • Resonance Raman characterization of the heme domain of soluble guanylate cyclase
    • Schelvis, J. P., Zhao, Y., Marletta, 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.1    Zhao, Y.2    Marletta, M.A.3    Babcock, G.T.4
  • 26
    • 0030942247 scopus 로고    scopus 로고
    • Characterization of ferrous FixL-nitric oxide adducts by resonance Raman spectroscopy
    • Lukat-Rodgers, G. S., and Rodgers, K. R. (1997) Characterization of ferrous FixL-nitric oxide adducts by resonance Raman spectroscopy, Biochemistry 36, 4178-4187.
    • (1997) Biochemistry , vol.36 , pp. 4178-4187
    • Lukat-Rodgers, G.S.1    Rodgers, K.R.2
  • 27
    • 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
  • 28
    • 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
  • 29
    • 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
  • 30
    • 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
  • 31
    • 0002179084 scopus 로고
    • Resonance Raman spectroscopy of metalloporphyrins
    • (Spiro, T. G., Ed.) John Wiley and Sons, New York
    • Spiro, T. G., and Li, X.-Y. (1988) Resonance Raman spectroscopy of metalloporphyrins, in Biological Applications of Raman Spectroscopy (Spiro, T. G., Ed.) pp 1-37, John Wiley and Sons, New York.
    • (1988) Biological Applications of Raman Spectroscopy , pp. 1-37
    • Spiro, T.G.1    Li, X.-Y.2
  • 32
    • 0002052550 scopus 로고
    • Heme protein structure and the iron-histidine stretching mode
    • (Spiro, T. G., Ed.) John Wiley and Sons, New York
    • Kitagawa, T. (1988) Heme protein structure and the iron-histidine stretching mode, in Biological Applications of Raman Spectroscopy (Spiro, T. G., Ed.) pp 97-131, John Wiley and Sons, New York.
    • (1988) Biological Applications of Raman Spectroscopy , pp. 97-131
    • Kitagawa, T.1
  • 33
    • 25144432064 scopus 로고    scopus 로고
    • A molecular basis for NO selectivity in soluble guanylate cyclase
    • Boon, E. M., Huang, S. H., and Marletta, M. A. (2005) A molecular 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
  • 34
    • 0029823461 scopus 로고    scopus 로고
    • Distal pocket polarity in the unusual ligand binding site of soluble guanylate cyclase: Implications for control of ·NO binding
    • Kim, S., Deinum, G., Gardner, M. T., Marletta, M. A., and Babcock, G. T. (1996) Distal pocket polarity in the unusual ligand binding site of soluble guanylate cyclase: Implications for control of ·NO binding, J. Am. Chem. Soc. 118, 8769-8770.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8769-8770
    • Kim, S.1    Deinum, G.2    Gardner, M.T.3    Marletta, M.A.4    Babcock, G.T.5
  • 35
    • 0027768729 scopus 로고
    • Distal pocket polarity in ligand binding to myoglobin: Deoxy and carbonmonoxy forms of a threonine68(E11) mutant investigated by X-ray crystallography and infrared spectroscopy
    • Cameron, A. D., Smerdon, S. J., Wilkinson, A. J., Habash, J., Helliwell, J. R., Li, T., and Olson, J. S. (1993) Distal pocket polarity in ligand binding to myoglobin: Deoxy and carbonmonoxy forms of a threonine68(E11) mutant investigated by X-ray crystallography and infrared spectroscopy, Biochemistry 32, 13061-13070.
    • (1993) Biochemistry , vol.32 , pp. 13061-13070
    • Cameron, A.D.1    Smerdon, S.J.2    Wilkinson, A.J.3    Habash, J.4    Helliwell, J.R.5    Li, T.6    Olson, J.S.7
  • 36
    • 0028328331 scopus 로고
    • Structural determinants of the stretching frequency of CO bound to myoglobin
    • Li, T., Quillin, M. L., Phillips, G. N., Jr., and Olson, J. S. (1994) Structural determinants of the stretching frequency of CO bound to myoglobin, Biochemistry 33, 1433-1446.
    • (1994) Biochemistry , vol.33 , pp. 1433-1446
    • Li, T.1    Quillin, M.L.2    Phillips Jr., G.N.3    Olson, J.S.4
  • 37
    • 0002429122 scopus 로고
    • (Hester, R. E., and Girling, R. B., Eds.) Royal Society of Chemistry, Cambridge, U.K.
    • Biram, D., Garratt, C. J., and Hester, R. E. (1991) in Spectroscopy of Biological Molecules (Hester, R. E., and Girling, R. B., Eds.) pp 433-434, Royal Society of Chemistry, Cambridge, U.K.
    • (1991) Spectroscopy of Biological Molecules , pp. 433-434
    • Biram, D.1    Garratt, C.J.2    Hester, R.E.3
  • 39
    • 0032493819 scopus 로고    scopus 로고
    • Heme environmental structure of CooA is modulated by the target DNA binding. Evidence from resonance Raman spectroscopy and CO rebinding kinetics
    • Uchida, T., Ishikawa, H., Takahashi, S., Ishimori, K., Morishima, I., Ohkubo, K., Nakajima, H., and Aono, S, (1998) Heme environmental structure of CooA is modulated by the target DNA binding. Evidence from resonance Raman spectroscopy and CO rebinding kinetics, J. Biol. Chem. 273, 19988-19992.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19988-19992
    • Uchida, T.1    Ishikawa, H.2    Takahashi, S.3    Ishimori, K.4    Morishima, I.5    Ohkubo, K.6    Nakajima, H.7    Aono, S.8
  • 40
    • 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
  • 41
    • 0000582319 scopus 로고
    • Oxygen-bound heme-heme oxygenase complex: Evidence for a highly bent structure of the coordinated oxygen
    • Takahashi, S., Ishikawa, K., Takeuchi, N., Ikeda-Saito, M., Yoshida, T., and Rousseau, D. L. (1995) Oxygen-bound heme-heme oxygenase complex: Evidence for a highly bent structure of the coordinated oxygen, J. Am. Chem. Soc. 117, 6002-6006.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6002-6006
    • Takahashi, S.1    Ishikawa, K.2    Takeuchi, N.3    Ikeda-Saito, M.4    Yoshida, T.5    Rousseau, D.L.6
  • 42
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.