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Volumn 417, Issue 1, 2009, Pages 65-76

Novel haem co-ordination variants of flavocytochrome P450 BM3

Author keywords

Cytochrome P450; Electron paramagnetic resonance (EPR); Haem co ordination; Magnetic circular dichroism (MCD); P450 BM3

Indexed keywords

CYTOCHROME P450; ELECTRON PARAMAGNETIC RESONANCE (EPR); HAEM CO-ORDINATION; MAGNETIC CIRCULAR DICHROISM (MCD); P450 BM3;

EID: 58249083277     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20081133     Document Type: Article
Times cited : (29)

References (52)
  • 1
    • 0030009067 scopus 로고    scopus 로고
    • Bacterial cytochromes P450
    • Munro, A. W. and Lindsay, J. G. (1996) Bacterial cytochromes P450. Mol. Microbiol. 20, 1115-1125
    • (1996) Mol. Microbiol , vol.20 , pp. 1115-1125
    • Munro, A.W.1    Lindsay, J.G.2
  • 2
    • 33846483860 scopus 로고    scopus 로고
    • Complex reactions catalyzed by cytochrome P450 enzymes
    • Isin, E. M. and Guengerich, F. P. (2007) Complex reactions catalyzed by cytochrome P450 enzymes. Biochim. Biophys. Acta 1770, 314-329
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 314-329
    • Isin, E.M.1    Guengerich, F.P.2
  • 3
    • 34249819058 scopus 로고    scopus 로고
    • Variations on a (t)heme: Novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamily
    • Munro, A. W., Girvan, H. M. and McLean, K. J. (2007) Variations on a (t)heme: novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamily. Nat. Prod. Rep. 24, 585-609
    • (2007) Nat. Prod. Rep , vol.24 , pp. 585-609
    • Munro, A.W.1    Girvan, H.M.2    McLean, K.J.3
  • 5
    • 33645892004 scopus 로고    scopus 로고
    • The status of high-valent metal oxo complexes in the P450 cytochromes
    • Makris, T. M., von Koenig, K., Schlichting, I. and Sligar, S. G. (2006) The status of high-valent metal oxo complexes in the P450 cytochromes. J. Inorg. Biochem. 100, 507-518
    • (2006) J. Inorg. Biochem , vol.100 , pp. 507-518
    • Makris, T.M.1    von Koenig, K.2    Schlichting, I.3    Sligar, S.G.4
  • 7
    • 13444266016 scopus 로고    scopus 로고
    • Substrate modulation of the properties and reactivity of the oxy-ferrous and hydroperoxo-ferric intermediates of cytochrome P450cam as shown by cryoreduction-EPR/ENDOR spectroscopy
    • Davydov, R., Perera, R., Jin, S., Yang, T. C., Bryson, T. A., Sono, M., Dawson, J. H. and Hoffman, B. M. (2005) Substrate modulation of the properties and reactivity of the oxy-ferrous and hydroperoxo-ferric intermediates of cytochrome P450cam as shown by cryoreduction-EPR/ENDOR spectroscopy. J. Am. Chem. Soc. 127, 1403-1413
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 1403-1413
    • Davydov, R.1    Perera, R.2    Jin, S.3    Yang, T.C.4    Bryson, T.A.5    Sono, M.6    Dawson, J.H.7    Hoffman, B.M.8
  • 8
    • 0030873316 scopus 로고    scopus 로고
    • Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN-and FAD-containing enzymes
    • Wang, M., Roberts, D. L., Paschke, R., Shea, T. M., Masters, B. S. and Kim, J. J. (1997) Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN-and FAD-containing enzymes. Proc. Natl. Acad. Sci. U.S.A. 94, 8411-8416
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 8411-8416
    • Wang, M.1    Roberts, D.L.2    Paschke, R.3    Shea, T.M.4    Masters, B.S.5    Kim, J.J.6
  • 9
    • 84892304480 scopus 로고    scopus 로고
    • Paine, M. J. I., Scrutton, N. S., Munro, A. W., Gutierrez, A., Roberts, G. C. K. and Wolf, C. R. (2005) Electron transfer partners of cytochrome P450. In Cytochrome P450 Structure, Mechanism and Biochemistry (Ortiz de Montellano, P. R., ed.), pp. 115-148, Kluwer Academic/Plenum Publishers, New York
    • Paine, M. J. I., Scrutton, N. S., Munro, A. W., Gutierrez, A., Roberts, G. C. K. and Wolf, C. R. (2005) Electron transfer partners of cytochrome P450. In Cytochrome P450 Structure, Mechanism and Biochemistry (Ortiz de Montellano, P. R., ed.), pp. 115-148, Kluwer Academic/Plenum Publishers, New York
  • 10
    • 0037202185 scopus 로고    scopus 로고
    • CYP119 plus a Sulfolobus tokodaii strain 7 ferredoxin and 2-oxoacid:ferredoxin oxidoreductase constitute a high-temperature cytochrome P450 catalytic system
    • Puchkaev, A. V., Wakagi, T. and Oriz de Montellano, P. R. (2002) CYP119 plus a Sulfolobus tokodaii strain 7 ferredoxin and 2-oxoacid:ferredoxin oxidoreductase constitute a high-temperature cytochrome P450 catalytic system. J. Am. Chem. Soc. 124, 12682-12683
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 12682-12683
    • Puchkaev, A.V.1    Wakagi, T.2    Oriz de Montellano, P.R.3
  • 12
    • 0042819974 scopus 로고    scopus 로고
    • Electron transfer in flavocytochrome P450 BM3: Kinetics of flavin reduction and oxidation, the role of cysteine 999, and relationships with mammalian cytochrome P450 reductase
    • Roitel, O., Scrutton, N. S. and Munro, A. W. (2003) Electron transfer in flavocytochrome P450 BM3: kinetics of flavin reduction and oxidation, the role of cysteine 999, and relationships with mammalian cytochrome P450 reductase. Biochemistry 42, 10809-10821
    • (2003) Biochemistry , vol.42 , pp. 10809-10821
    • Roitel, O.1    Scrutton, N.S.2    Munro, A.W.3
  • 14
    • 0026452788 scopus 로고
    • Domains of the catalytically self-sufficient cytochrome P-450 BM-3: Genetic construction, overexpression, purification and spectroscopic characterization
    • Miles, J. S., Munro, A. W., Rospendowski, B. N., Smith, W. E., McKnight, J. and Thomson, A. J. (1992) Domains of the catalytically self-sufficient cytochrome P-450 BM-3: genetic construction, overexpression, purification and spectroscopic characterization. Biochem. J. 288, 503-509
    • (1992) Biochem. J , vol.288 , pp. 503-509
    • Miles, J.S.1    Munro, A.W.2    Rospendowski, B.N.3    Smith, W.E.4    McKnight, J.5    Thomson, A.J.6
  • 15
    • 0028205462 scopus 로고
    • Structural and enzymological analysis of the interaction of isolated domains of cytochrome P-450 BM3
    • Munro, A. W., Lindsay, J. G., Coggins, J. R., Kelly, S. M. and Price, N. C. (1994) Structural and enzymological analysis of the interaction of isolated domains of cytochrome P-450 BM3. FEBS Lett. 343, 70-74
    • (1994) FEBS Lett , vol.343 , pp. 70-74
    • Munro, A.W.1    Lindsay, J.G.2    Coggins, J.R.3    Kelly, S.M.4    Price, N.C.5
  • 16
    • 0242330792 scopus 로고    scopus 로고
    • Regio- and enantioselective alkane hydroxylation with engineered cytochromes P450 BM-3
    • Peters, M. W., Meinhold, P., Glieder, A. and Arnold, F. H. (2003) Regio- and enantioselective alkane hydroxylation with engineered cytochromes P450 BM-3. J. Am. Chem. Soc. 125, 13442-134540
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 13442-134540
    • Peters, M.W.1    Meinhold, P.2    Glieder, A.3    Arnold, F.H.4
  • 17
    • 33747885449 scopus 로고    scopus 로고
    • A screening system for the directed evolution of epoxygenases: Importance of position 184 in P450 BM3 for stereoselective styrene epoxidation
    • Tee, K. L. and Schwaneberg, U. (2006) A screening system for the directed evolution of epoxygenases: importance of position 184 in P450 BM3 for stereoselective styrene epoxidation. Angew. Chem. Int. Ed. 45, 5380-5383
    • (2006) Angew. Chem. Int. Ed , vol.45 , pp. 5380-5383
    • Tee, K.L.1    Schwaneberg, U.2
  • 18
    • 0030570979 scopus 로고    scopus 로고
    • Analysis of the structural stability of the multidomain enzyme flavocytochrome P-450 BM3
    • Munro, A. W., Lindsay, J. G., Coggins, J. R., Kelly, S. M. and Price, N. C. (1996) Analysis of the structural stability of the multidomain enzyme flavocytochrome P-450 BM3. Biochim. Biophys. Acta 1296, 127-137
    • (1996) Biochim. Biophys. Acta , vol.1296 , pp. 127-137
    • Munro, A.W.1    Lindsay, J.G.2    Coggins, J.R.3    Kelly, S.M.4    Price, N.C.5
  • 19
    • 0037035545 scopus 로고    scopus 로고
    • Covalent attachment of the heme prosthetic group in the CYP4F cytochrome P450 family
    • LeBrun, L. A., Xu, F., Kroetz, D. L. and Ortiz de Montellano, P. R. (2002) Covalent attachment of the heme prosthetic group in the CYP4F cytochrome P450 family. Biochemistry 41, 5931-5937
    • (2002) Biochemistry , vol.41 , pp. 5931-5937
    • LeBrun, L.A.1    Xu, F.2    Kroetz, D.L.3    Ortiz de Montellano, P.R.4
  • 21
    • 14844354133 scopus 로고    scopus 로고
    • The P450cam G248E mutant covalently binds its prosthetic heme group
    • Limburg, J., LeBrun, L. A. and Ortiz de Montellano, P. R. (2005) The P450cam G248E mutant covalently binds its prosthetic heme group. Biochemistry 44, 4091-4099
    • (2005) Biochemistry , vol.44 , pp. 4091-4099
    • Limburg, J.1    LeBrun, L.A.2    Ortiz de Montellano, P.R.3
  • 23
    • 2542439885 scopus 로고    scopus 로고
    • A single mutation in cytochrome P450 BM3 induces the conformational rearrangement seen upon substrate binding in the wild-type enzyme
    • Joyce, M. G., Girvan, H. M., Munro, A. W. and Leys, D. (2004) A single mutation in cytochrome P450 BM3 induces the conformational rearrangement seen upon substrate binding in the wild-type enzyme. J. Biol. Chem. 279, 23287-23293
    • (2004) J. Biol. Chem , vol.279 , pp. 23287-23293
    • Joyce, M.G.1    Girvan, H.M.2    Munro, A.W.3    Leys, D.4
  • 24
    • 33846958772 scopus 로고    scopus 로고
    • Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets: New heme ligation states influence conformational equilibria in P450 BM3
    • Girvan, H. M., Seward, H. E., Toogood, H. S., Cheesman, M. R., Leys, D. and Munro, A. W. (2007) Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets: new heme ligation states influence conformational equilibria in P450 BM3. J. Biol. Chem. 282, 564-572
    • (2007) J. Biol. Chem , vol.282 , pp. 564-572
    • Girvan, H.M.1    Seward, H.E.2    Toogood, H.S.3    Cheesman, M.R.4    Leys, D.5    Munro, A.W.6
  • 25
    • 23844434591 scopus 로고    scopus 로고
    • Switching pyridine nucleotide specificity in P450 BM3: Mechanistic analysis of the W1046H and W1046A enzymes
    • Neeli, R., Roitel, O., Scrutton, N. S. and Munro, A. W. (2005) Switching pyridine nucleotide specificity in P450 BM3: mechanistic analysis of the W1046H and W1046A enzymes. J. Biol. Chem. 280, 17634-17644
    • (2005) J. Biol. Chem , vol.280 , pp. 17634-17644
    • Neeli, R.1    Roitel, O.2    Scrutton, N.S.3    Munro, A.W.4
  • 26
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • Berry, E. A. and Trumpower, B. L. (1987) Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra. Anal. Biochem. 161, 1-15
    • (1987) Anal. Biochem , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 27
    • 26844498754 scopus 로고    scopus 로고
    • The dimeric form of flavocytochrome P450 BM3 is catalytically functional as a fatty acid hydroxylase
    • Neeli, R., Girvan, H. M., Lawrence, A., Warren, M. J., Leys, D., Scrutton, N. S. and Munro, A. W. (2005) The dimeric form of flavocytochrome P450 BM3 is catalytically functional as a fatty acid hydroxylase. FEBS Lett. 579, 5582-5588
    • (2005) FEBS Lett , vol.579 , pp. 5582-5588
    • Neeli, R.1    Girvan, H.M.2    Lawrence, A.3    Warren, M.J.4    Leys, D.5    Scrutton, N.S.6    Munro, A.W.7
  • 29
    • 0018115502 scopus 로고
    • Redox potentiometry: Determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems
    • Dutton, P. L. (1978) Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems. Methods Enzymol. 54, 411-435
    • (1978) Methods Enzymol , vol.54 , pp. 411-435
    • Dutton, P.L.1
  • 31
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D Biol. Crystallogr. 50, 760-763
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D Biol. Crystallogr. 50, 760-763
  • 34
    • 33745832316 scopus 로고    scopus 로고
    • Biophysical characterization of the sterol demethylase P450 from Mycobacterium tuberculosis, its cognate ferredoxin, and their interactions
    • McLean, K. J., Warman, A. J., Seward, H. E., Marshall, K. R., Girvan, H. M., Cheesman, M. R., Waterman, M. R. and Munro, A. W. (2006) Biophysical characterization of the sterol demethylase P450 from Mycobacterium tuberculosis, its cognate ferredoxin, and their interactions. Biochemistry 45, 8427-8443
    • (2006) Biochemistry , vol.45 , pp. 8427-8443
    • McLean, K.J.1    Warman, A.J.2    Seward, H.E.3    Marshall, K.R.4    Girvan, H.M.5    Cheesman, M.R.6    Waterman, M.R.7    Munro, A.W.8
  • 35
    • 0037390012 scopus 로고    scopus 로고
    • Neutral thiol as a proximal ligand to ferrous heme iron: Implications for heme proteins that lose cysteine thiolate ligation on reduction
    • Perera, R., Sono, M., Sigman, J. A., Pfister, T. D., Lu, Y. and Dawson, J. H. (2003) Neutral thiol as a proximal ligand to ferrous heme iron: implications for heme proteins that lose cysteine thiolate ligation on reduction. Proc. Natl. Acad. Sci. U.S.A. 100, 3641-3646
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 3641-3646
    • Perera, R.1    Sono, M.2    Sigman, J.A.3    Pfister, T.D.4    Lu, Y.5    Dawson, J.H.6
  • 36
    • 34548329954 scopus 로고    scopus 로고
    • Rapid P450 heme iron reduction by laser photoexcitation of Mycobacterium tuberculosis CYP121 and CYP51B1: Analysis of CO complexation reactions and reversibility of the P450/P420 equilibrium
    • Dunford, A. J., McLean, K. J., Sabri, M., Seward, H. E., Heyes, D. J., Scrutton, N. S. and Munro, A. W. (2007) Rapid P450 heme iron reduction by laser photoexcitation of Mycobacterium tuberculosis CYP121 and CYP51B1: analysis of CO complexation reactions and reversibility of the P450/P420 equilibrium. J. Biol. Chem. 282, 24816-24824
    • (2007) J. Biol. Chem , vol.282 , pp. 24816-24824
    • Dunford, A.J.1    McLean, K.J.2    Sabri, M.3    Seward, H.E.4    Heyes, D.J.5    Scrutton, N.S.6    Munro, A.W.7
  • 39
    • 0035856564 scopus 로고    scopus 로고
    • Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3
    • Ost, T. W., Miles, C. S., Munro, A. W., Murdoch, J., Reid, G. A. and Chapman, S. K. (2001) Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3. Biochemistry 40, 13421-13429
    • (2001) Biochemistry , vol.40 , pp. 13421-13429
    • Ost, T.W.1    Miles, C.S.2    Munro, A.W.3    Murdoch, J.4    Reid, G.A.5    Chapman, S.K.6
  • 40
    • 0020490891 scopus 로고
    • Sulfur donor ligand binding to ferric cytochrome P450cam and myoglobin: Ultraviolet-visible absorption, magnetic circular dichroism, and electron paramagnetic resonance spectroscopic investigations of the complexes
    • Sono, M., Andersson, L. A. and Dawson, J. H. (1982) Sulfur donor ligand binding to ferric cytochrome P450cam and myoglobin: ultraviolet-visible absorption, magnetic circular dichroism, and electron paramagnetic resonance spectroscopic investigations of the complexes. J. Biol. Chem. 257, 8308-8320
    • (1982) J. Biol. Chem , vol.257 , pp. 8308-8320
    • Sono, M.1    Andersson, L.A.2    Dawson, J.H.3
  • 41
    • 0025766549 scopus 로고
    • Electron paramagnetic resonance investigations of exogenous ligand complexes of low-spin ferric chloroperoxidase: Further support for endogenous thiolate ligation to the heme iron
    • Sono, M., Hager, L. P. and Dawson, J. H. (1991) Electron paramagnetic resonance investigations of exogenous ligand complexes of low-spin ferric chloroperoxidase: further support for endogenous thiolate ligation to the heme iron. Biochim. Biophys. Acta 1078, 351-359
    • (1991) Biochim. Biophys. Acta , vol.1078 , pp. 351-359
    • Sono, M.1    Hager, L.P.2    Dawson, J.H.3
  • 42
    • 0035807062 scopus 로고    scopus 로고
    • Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation: EPR and MCD of SoxAX from Rhodovulum sulfidophilum
    • Cheesman, M. R., Little, P. J. and Berks, B. C. (2001) Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation: EPR and MCD of SoxAX from Rhodovulum sulfidophilum. Biochemistry 40, 10562-10569
    • (2001) Biochemistry , vol.40 , pp. 10562-10569
    • Cheesman, M.R.1    Little, P.J.2    Berks, B.C.3
  • 43
    • 0025025649 scopus 로고
    • Bis-methionine axial ligation of haem in bacterioferritin from Pseudomonas aeruginosa
    • Cheesman, M. R., Thomson, A. J., Greenwood, C., Moore, G. R. and Kadir, F. (1990) Bis-methionine axial ligation of haem in bacterioferritin from Pseudomonas aeruginosa. Nature 346, 771-773
    • (1990) Nature , vol.346 , pp. 771-773
    • Cheesman, M.R.1    Thomson, A.J.2    Greenwood, C.3    Moore, G.R.4    Kadir, F.5
  • 44
    • 0027298183 scopus 로고
    • Identification of charge-transfer transitions in the optical spectrum of low-spin ferric cytochrome P-450 Bacillus megaterium
    • McKnight, J., Cheesman, M. R., Thomson, A. J., Miles, J. S. and Munro, A. W. (1993) Identification of charge-transfer transitions in the optical spectrum of low-spin ferric cytochrome P-450 Bacillus megaterium. Eur. J. Biochem. 213, 683-687
    • (1993) Eur. J. Biochem , vol.213 , pp. 683-687
    • McKnight, J.1    Cheesman, M.R.2    Thomson, A.J.3    Miles, J.S.4    Munro, A.W.5
  • 45
    • 0021777960 scopus 로고
    • Resonance Raman spectroscopy as a probe of heme-protein structure and dynamics
    • Spiro, T. G. (1985) Resonance Raman spectroscopy as a probe of heme-protein structure and dynamics. Adv. Prot. Chem. 37, 111-159
    • (1985) Adv. Prot. Chem , vol.37 , pp. 111-159
    • Spiro, T.G.1
  • 46
    • 0001098626 scopus 로고
    • 15N-substituted derivatives. II. Normal coordinate analysis
    • 15N-substituted derivatives. II. Normal coordinate analysis. J. Chem. Phys. 69, 4526-4534
    • (1978) J. Chem. Phys , vol.69 , pp. 4526-4534
    • Abe, M.1    Kitagawa, T.2    Kyogoku, Y.3
  • 47
    • 0346220023 scopus 로고    scopus 로고
    • Resonance Raman scattering of cytochrome P450 BM3 and effect of imidazole inhibitors
    • Smith, S. J., Munro, A. W. and Smith, W. E. (2003) Resonance Raman scattering of cytochrome P450 BM3 and effect of imidazole inhibitors. Biopolymers 70, 620-627
    • (2003) Biopolymers , vol.70 , pp. 620-627
    • Smith, S.J.1    Munro, A.W.2    Smith, W.E.3
  • 48
    • 0024852008 scopus 로고
    • Resonance Raman study on the structure of the active sites of microsomal cytochrome P-450 isozymes LM2 and LM4
    • Hildebrandt, P., Greinert, R., Stier, A. and Taniguchi, H. (1989) Resonance Raman study on the structure of the active sites of microsomal cytochrome P-450 isozymes LM2 and LM4. Eur. J. Biochem. 186, 291-302
    • (1989) Eur. J. Biochem , vol.186 , pp. 291-302
    • Hildebrandt, P.1    Greinert, R.2    Stier, A.3    Taniguchi, H.4
  • 49
    • 0037646516 scopus 로고    scopus 로고
    • Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis: Crystallographic, spectroscopic, and mutational studies
    • Lee, D. S., Yamada, A., Sugimoto, H., Matsunaga, I., Ogura, H., Ichihara, K., Adachi, S., Park, S. Y. and Shiro, Y. (2003) Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis: crystallographic, spectroscopic, and mutational studies. J. Biol. Chem. 278, 9761-9767
    • (2003) J. Biol. Chem , vol.278 , pp. 9761-9767
    • Lee, D.S.1    Yamada, A.2    Sugimoto, H.3    Matsunaga, I.4    Ogura, H.5    Ichihara, K.6    Adachi, S.7    Park, S.Y.8    Shiro, Y.9
  • 50
    • 0031013972 scopus 로고    scopus 로고
    • The structure of the cytochrome P450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid
    • Li, H. Y. and Poulos, T. L. (1997) The structure of the cytochrome P450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid. Nat. Struct. Biol. 4, 140-146
    • (1997) Nat. Struct. Biol , vol.4 , pp. 140-146
    • Li, H.Y.1    Poulos, T.L.2
  • 51
    • 0000833558 scopus 로고
    • Crystal structure and preliminary functional analysis of the cytochrome c peroxidase His175Gln proximal ligand mutant
    • Sundaramoorthy, M., Choudhury, K., Edwards, S. L. and Poulos, T. L. (1991) Crystal structure and preliminary functional analysis of the cytochrome c peroxidase His175Gln proximal ligand mutant. J. Am. Chem. Soc. 113, 7755-7757
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 7755-7757
    • Sundaramoorthy, M.1    Choudhury, K.2    Edwards, S.L.3    Poulos, T.L.4
  • 52


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