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Volumn 287, Issue 23, 2012, Pages 19699-19714

Unusual spectroscopic and ligand binding properties of the cytochrome P450-flavodoxin fusion enzyme XplA

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BINDING MODES; COFACTORS; CYTOCHROME P450; EPR SPECTRA; EPR STUDIES; FLAVODOXIN; FUSION ENZYMES; HEME IRON; HIGH AFFINITY; LIGAND BINDING; LIGAND BINDING PROPERTIES; MONOMERIC ENZYMES; MORPHOLINES; RED-SHIFTED; RHODOCOCCUS RHODOCHROUS; SEMIQUINONES; SORET BANDS; SUBSTRATE-FREE; TRINITROBENZENE;

EID: 84861723942     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.319202     Document Type: Article
Times cited : (25)

References (71)
  • 2
    • 46049121122 scopus 로고    scopus 로고
    • Microbial transformation and degradation of polychlorinated biphenyls
    • DOI 10.1016/j.envpol.2007.10.016, PII S0269749107005088
    • Field, J. A., and Sierra-Alvarez, R. (2008) Microbial transformation and degradation of polychlorinated biphenyls. Environ. Pollut. 155, 1-12 (Pubitemid 351899238)
    • (2008) Environmental Pollution , vol.155 , Issue.1 , pp. 1-12
    • Field, J.A.1    Sierra-Alvarez, R.2
  • 3
    • 0034082905 scopus 로고    scopus 로고
    • Engineering dioxygenases for efficient degradation of environmental pollutants
    • Furukawa, K. (2000) Engineering dioxygenases for efficient degradation of environmental pollutants. Curr. Opin. Biotechnol. 11, 244-249
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 244-249
    • Furukawa, K.1
  • 4
    • 0035544054 scopus 로고    scopus 로고
    • Identification of a microorganism that links its growth to the reductive dechlorination of 2,3,5,6-chlorobiphenyl
    • DOI 10.1046/j.1462-2920.2001.00246.x
    • Cutter, L. A., Watts, J. E., Sowers, K. R., and May, H. D. (2001) Identification of a microorganism that links its growth to the reductive dechlorination of 2,3,5,6-chlorobiphenyl. Environ. Microbiol. 3, 699-709 (Pubitemid 34054301)
    • (2001) Environmental Microbiology , vol.3 , Issue.11 , pp. 699-709
    • Cutter, L.A.1    Watts, J.E.M.2    Sowers, K.R.3    May, H.D.4
  • 5
    • 0034881143 scopus 로고    scopus 로고
    • Purification, cloning, and sequencing of an enzyme mediating the reductive dechlorination of tetrachloroethylene (PCE) from Clostridium bifermentans DPH-1
    • DOI 10.1139/cjm-47-5-448
    • Okeke, B. C., Chang, Y. C., Hatsu, M., Suzuki, T., and Takamizawa, K. (2001) Purification, cloning, and sequencing of an enzyme mediating the reductive dechlorination of tetrachloroethylene (PCE) from Clostridium bifermentans DPH-1. Can. J. Microbiol. 47, 448-456 (Pubitemid 32745012)
    • (2001) Canadian Journal of Microbiology , vol.47 , Issue.5 , pp. 448-456
    • Okeke, B.C.1    Chang, Y.C.2    Hatsu, M.3    Suzuki, T.4    Takamizawa, K.5
  • 6
    • 0015057899 scopus 로고
    • Induction specificity and catabolite repression of the early enzymes in camphor degradation by Pseudomonas putida
    • Hartline, R. A., and Gunsalus, I. C. (1971) Induction specificity and catabolite repression of the early enzymes in camphor degradation by Pseudomonas putida. J. Bacteriol. 106, 468-478
    • (1971) J. Bacteriol. , vol.106 , pp. 468-478
    • Hartline, R.A.1    Gunsalus, I.C.2
  • 7
    • 0030033702 scopus 로고    scopus 로고
    • Characterization of the expression of the thcB gene, coding for a pesticide-degrading cytochrome P-450 in Rhodococcus strains
    • Shao, Z. Q., and Behki, R. (1996) Characterization of the expression of the thcB gene, coding for a pesticide-degrading cytochrome P-450 in Rhodococcus strains. Appl. Environ. Microbiol. 62, 403-407 (Pubitemid 26051565)
    • (1996) Applied and Environmental Microbiology , vol.62 , Issue.2 , pp. 403-407
    • Shao, Z.Q.1    Behki, R.2
  • 8
    • 34249819058 scopus 로고    scopus 로고
    • Variations on a (t)heme - Novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamily
    • DOI 10.1039/b604190f
    • 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 (Pubitemid 46848711)
    • (2007) Natural Product Reports , vol.24 , Issue.3 , pp. 585-609
    • Munro, A.W.1    Girvan, H.M.2    McLean, K.J.3
  • 9
    • 77951621289 scopus 로고    scopus 로고
    • Application of advanced oxidation processes for TNT removal. A review
    • Ayoub, K., van Hullebusch, E. D., Cassir, M., and Bermond, A. (2010) Application of advanced oxidation processes for TNT removal. A review. J. Hazard. Mater. 178, 10-28
    • (2010) J. Hazard. Mater. , vol.178 , pp. 10-28
    • Ayoub, K.1    Van Hullebusch, E.D.2    Cassir, M.3    Bermond, A.4
  • 10
    • 65549109101 scopus 로고    scopus 로고
    • Transgenic plants for enhanced phytoremediation of toxic explosives
    • Van Aken, B. (2009) Transgenic plants for enhanced phytoremediation of toxic explosives. Curr. Opin. Biotechnol. 20, 231-236
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 231-236
    • Van Aken, B.1
  • 13
    • 0032937445 scopus 로고    scopus 로고
    • Biodegradation of explosives by transgenic plants expressing pentaerythritol tetranitrate reductase
    • DOI 10.1038/8673
    • French, C. E., Rosser, S. J., Davies, G. J., Nicklin, S., and Bruce, N. C. (1999) Biodegradation of explosives by transgenic plants expressing pentaerythritol tetranitrate reductase. Nat. Biotechnol. 17, 491-494 (Pubitemid 29217904)
    • (1999) Nature Biotechnology , vol.17 , Issue.5 , pp. 491-494
    • French, C.E.1    Rosser, S.J.2    Davies, G.J.3    Nicklin, S.4    Bruce, N.C.5
  • 15
    • 32344440055 scopus 로고    scopus 로고
    • An explosive-degrading cytochrome P450 activity and its targeted application for the phytoremediation of RDX
    • DOI 10.1038/nbt1184, PII NBT1184
    • Rylott, E. L., Jackson, R. G., Edwards, J., Womack, G. L., Seth-Smith, H. M., Rathbone, D. A., Strand, S. E., and Bruce, N. C. (2006) An explosivedegrading cytochrome P450 activity and its targeted application for the phytoremediation of RDX. Nat. Biotechnol. 24, 216-219 (Pubitemid 43221707)
    • (2006) Nature Biotechnology , vol.24 , Issue.2 , pp. 216-219
    • Rylott, E.L.1    Jackson, R.G.2    Edwards, J.3    Womack, G.L.4    Seth-Smith, H.M.B.5    Rathbone, D.A.6    Strand, S.E.7    Bruce, N.C.8
  • 16
    • 21844434930 scopus 로고    scopus 로고
    • Structure and chemistry of cytochrome P450
    • DOI 10.1021/cr0307143
    • Denisov, I. G., Makris, T. M., Sligar, S. G., and Schlichting, I. (2005) Structure and chemistry of cytochrome P450. Chem. Rev. 105, 2253-2277 (Pubitemid 40951784)
    • (2005) Chemical Reviews , vol.105 , Issue.6 , pp. 2253-2277
    • Denisov, I.G.1    Makris, T.M.2    Sligar, S.G.3    Schlichting, I.4
  • 17
    • 0030009067 scopus 로고    scopus 로고
    • Bacterial cytochromes P-450
    • DOI 10.1111/j.1365-2958.1996.tb02632.x
    • Munro, A. W., and Lindsay, J. G. (1996) Bacterial cytochromes P-450. Mol. Microbiol. 20, 1115-1125 (Pubitemid 26225422)
    • (1996) Molecular Microbiology , vol.20 , Issue.6 , pp. 1115-1125
    • Munro, A.W.1    Lindsay, J.G.2
  • 18
    • 33846473252 scopus 로고    scopus 로고
    • Cytochrome P450 systems-biological variations of electron transport chains
    • DOI 10.1016/j.bbagen.2006.07.017, PII S0304416506002133
    • Hannemann, F., Bichet, A., Ewen, K. M., and Bernhardt, R. (2007) Cytochrome P450 systems. Biological variations of electron transport chains. Biochim. Biophys. Acta 1770, 330-344 (Pubitemid 46157074)
    • (2007) Biochimica et Biophysica Acta - General Subjects , vol.1770 , Issue.3 , pp. 330-344
    • Hannemann, F.1    Bichet, A.2    Ewen, K.M.3    Bernhardt, R.4
  • 20
    • 0037032543 scopus 로고    scopus 로고
    • A novel sterol 14α-demethylase/ferredoxin fusion protein (MCCYP51FX) from Methylococcus capsulatus represents a new class of the cytochrome P450 superfamily
    • DOI 10.1074/jbc.M203523200
    • Jackson, C. J., Lamb, D. C., Marczylo, T. H., Warrilow, A. G., Manning, N. J., Lowe, D. J., Kelly, D. E., and Kelly, S. L. (2002) A novel sterol 14α-demethylase/ferredoxin fusion protein (MCCYP51FX) from Methylococcus capsulatus represents a new class of the cytochrome P450 superfamily. J. Biol. Chem. 277, 46959-46965 (Pubitemid 36159200)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.49 , pp. 46959-46965
    • Jackson, C.J.1    Lamb, D.C.2    Marczylo, T.H.3    Warrilow, A.G.S.4    Manning, N.J.5    Lowe, D.J.6    Kelly, D.E.7    Kelly, S.L.8
  • 23
    • 0036795043 scopus 로고    scopus 로고
    • Cloning, sequencing, and characterization of the hexahydro-1,3,5- trinitro-1,3,5-triazine degradation gene cluster from Rhodococcus rhodochrous
    • DOI 10.1128/AEM.68.10.4764-4771.2002
    • Seth-Smith, H. M., Rosser, S. J., Basran, A., Travis, E. R., Dabbs, E. R., Nicklin, S., and Bruce, N. C. (2002) Cloning, sequencing, and characterization of the hexahydro-1,3,5-trinitro-1,3,5-triazine degradation gene cluster from Rhodococcus rhodochrous. Appl. Environ. Microbiol. 68, 4764-4771 (Pubitemid 35154779)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.10 , pp. 4764-4771
    • Seth-Smith, H.M.B.1    Rosser, S.J.2    Basran, A.3    Travis, E.R.4    Dabbs, E.R.5    Nicklin, S.6    Bruce, N.C.7
  • 24
    • 70350509061 scopus 로고    scopus 로고
    • The 1.5-Å structure of XplA-heme, an unusual cytochrome P450 heme domain that catalyzes reductive biotransformation of royal demolition explosive
    • Sabbadin, F., Jackson, R., Haider, K., Tampi, G., Turkenburg, J. P., Hart, S., Bruce, N. C., and Grogan, G. (2009) The 1.5-Å structure of XplA-heme, an unusual cytochrome P450 heme domain that catalyzes reductive biotransformation of royal demolition explosive. J. Biol. Chem. 284, 28467-28475
    • (2009) J. Biol. Chem. , vol.284 , pp. 28467-28475
    • Sabbadin, F.1    Jackson, R.2    Haider, K.3    Tampi, G.4    Turkenburg, J.P.5    Hart, S.6    Bruce, N.C.7    Grogan, G.8
  • 25
    • 0345184329 scopus 로고    scopus 로고
    • Biotransformation of hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) by a rabbit liver cytochrome P450: Insight into the mechanism of RDX biodegradation by Rhodococcus sp. strain DN22
    • DOI 10.1128/AEM.69.3.1347-1351.2003
    • Bhushan, B., Trott, S., Spain, J. C., Halasz, A., Paquet, L., and Hawari, J. (2003) Biotransformation of hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) by a rabbit liver cytochrome P450. Insight into the mechanism of RDX biodegradation by Rhodococcus sp. strain DN22. Appl. Environ. Microbiol. 69, 1347-1351 (Pubitemid 36314267)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.3 , pp. 1347-1351
    • Bhushan, B.1    Trott, S.2    Spain, J.C.3    Halasz, A.4    Paquet, L.5    Hawari, J.6
  • 26
    • 0026352457 scopus 로고
    • Crystal structure of the cytochrome P-450CAM active site mutant Thr252Ala
    • Raag, R., Martinis, S. A., Sligar, S. G., and Poulos, T. L. (1991) Crystal structure of the cytochrome P-450CAM active site mutant Thr252Ala. Biochemistry 30, 11420-11429
    • (1991) Biochemistry , vol.30 , pp. 11420-11429
    • Raag, R.1    Martinis, S.A.2    Sligar, S.G.3    Poulos, T.L.4
  • 28
    • 78651165715 scopus 로고
    • The Carbon Monoxide-binding Pigment of Liver Microsomes. I. Evidence for Its Hemoprotein Nature
    • Omura, T., and Sato, R. (1964) The Carbon Monoxide-binding Pigment of Liver Microsomes. I. Evidence for Its Hemoprotein Nature. J. Biol. Chem. 239, 2370-2378
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 29
    • 26844563342 scopus 로고    scopus 로고
    • Field-flow fractionation coupled to multi-angle laser light scattering detectors: Applicability and analytical benefits for the analysis of environmental colloids
    • DOI 10.1016/j.aca.2005.07.049, PII S0003267005012900
    • Kammera, F. V., Baborowski, M., and Friese, K. (2005) Field flow fractionation coupled to multi-angle laser light scattering detectors: Applicability and analytical benefits for the analysis of environmental colloids. Anal. Chim. Acta 552, 166-174 (Pubitemid 41460521)
    • (2005) Analytica Chimica Acta , vol.552 , Issue.1-2 , pp. 166-174
    • Kammer, F.V.D.1    Baborowski, M.2    Friese, K.3
  • 30
    • 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
    • 0030666084 scopus 로고    scopus 로고
    • Redox control of the catalytic cycle of flavocytochrome P-450 BM3
    • DOI 10.1021/bi971085s
    • Daff, S. N., Chapman, S. K., Turner, K. L., Holt, R. A., Govindaraj, S., Poulos, T. L., and Munro, A. W. (1997) Redox control of the catalytic cycle of flavocytochrome P-450 BM3. Biochemistry 36, 13816-13823 (Pubitemid 27494887)
    • (1997) Biochemistry , vol.36 , Issue.45 , pp. 13816-13823
    • Daff, S.N.1    Chapman, S.K.2    Turner, K.L.3    Holt, R.A.4    Govindaraj, S.5    Poulos, T.L.6    Munro, A.W.7
  • 33
    • 0032612239 scopus 로고    scopus 로고
    • Identifying and quantitating FAD and FMN in simple and in iron-sulfur-containing flavoproteins
    • Aliverti, A., Curti, B., and Vanoni, M. A. (1999) Identifying and quantitating FAD and FMN in simple and in iron-sulfur-containing flavoproteins. Methods Mol. Biol. 131, 9-23
    • (1999) Methods Mol. Biol. , vol.131 , pp. 9-23
    • Aliverti, A.1    Curti, B.2    Vanoni, M.A.3
  • 35
    • 84861723266 scopus 로고
    • Pergamon Press, Oxford, UK
    • Cargill, R. (ed) (1990) Carbon Monoxide, Vol. 43, pp. 5-30, Pergamon Press, Oxford, UK
    • (1990) Carbon Monoxide , vol.43 , pp. 5-30
    • Cargill, R.1
  • 36
    • 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
  • 37
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch, W. (1988) Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallogr. 21, 916-924
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 38
    • 0028103275 scopus 로고
    • The CCP4 suite. Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite. Programs for protein crystallography. Acta Crystallogr.DBiol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr.DBiol. Crystallogr. , vol.50 , pp. 760-763
  • 40
    • 0036842594 scopus 로고    scopus 로고
    • Laboratory evolution of a soluble, self-sufficient, highly active alkane hydroxylase
    • DOI 10.1038/nbt744
    • Glieder, A., Farinas, E. T., and Arnold, F. H. (2002) Laboratory evolution of a soluble, self-sufficient, highly active alkane hydroxylase. Nat. Biotechnol. 20, 1135-1139 (Pubitemid 35285443)
    • (2002) Nature Biotechnology , vol.20 , Issue.11 , pp. 1135-1139
    • Glieder, A.1    Farinas, E.T.2    Arnold, F.H.3
  • 42
    • 0017170343 scopus 로고
    • Coupling of spin, substrate, and redox equilibria in cytochrome P450
    • Sligar, S. G. (1976) Coupling of spin, substrate, and redox equilibria in cytochrome P450. Biochemistry 15, 5399-5406
    • (1976) Biochemistry , vol.15 , pp. 5399-5406
    • Sligar, S.G.1
  • 43
    • 0032506159 scopus 로고    scopus 로고
    • Imidazolyl carboxylic acids as mechanistic probes of flavocytochrome P- 450 BM3
    • DOI 10.1021/bi980462d
    • Noble, M. A., Quaroni, L., Chumanov, G. D., Turner, K. L., Chapman, S. K., Hanzlik, R. P., and Munro, A. W. (1998) Imidazolyl carboxylic acids as mechanistic probes of flavocytochrome P-450 BM3. Biochemistry 37, 15799-15807 (Pubitemid 28524751)
    • (1998) Biochemistry , vol.37 , Issue.45 , pp. 15799-15807
    • Noble, M.A.1    Quaroni, L.2    Chumanov, G.D.3    Turner, K.L.4    Chapman, S.K.5    Hanzlik, R.P.6    Munro, A.W.7
  • 44
    • 77952213251 scopus 로고    scopus 로고
    • Cloning, expression, and purification of cindoxin, an unusual Fmn-containing cytochrome p450 redox partner
    • Hawkes, D. B., Slessor, K. E., Bernhardt, P. V., and De Voss, J. J. (2010) Cloning, expression, and purification of cindoxin, an unusual Fmn-containing cytochrome p450 redox partner. Chembiochem 11, 1107-1114
    • (2010) Chembiochem , vol.11 , pp. 1107-1114
    • Hawkes, D.B.1    Slessor, K.E.2    Bernhardt, P.V.3    De Voss, J.J.4
  • 45
    • 0033152446 scopus 로고    scopus 로고
    • The midpoint potentials for the oxidized-semiquinone couple for Gly-57 mutants of the Clostridium beijerinckii flavodoxin correlate with changes in the hydrogen-bonding interaction with the proton on N(5) of the reduced flavin mononucleotide cofactor as measured by NMR chemical shift temperature dependencies
    • Chang, F. C., and Swenson, R. P. (1999) The midpoint potentials for the oxidized-semiquinone couple for Gly-57 mutants of the Clostridium beijerinckii flavodoxin correlate with changes in the hydrogen-bonding interaction with the proton on N(5) of the reduced flavin mononucleotide cofactor as measured by NMR chemical shift temperature dependencies. Biochemistry 38, 7168-7176
    • (1999) Biochemistry , vol.38 , pp. 7168-7176
    • Chang, F.C.1    Swenson, R.P.2
  • 46
    • 4744337841 scopus 로고    scopus 로고
    • Expression and characterization of the two flavodoxin proteins of Bacillus subtilis, YkuN and YkuP: Biophysical properties and interactions with cytochrome P450 bioI
    • DOI 10.1021/bi049131t
    • Lawson, R. J., von Wachenfeldt, C., Haq, I., Perkins, J., and Munro, A. W. (2004) Expression and characterization of the two flavodoxin proteins of Bacillus subtilis, YkuN and YkuP. Biophysical properties and interactions with cytochrome P450 BioI. Biochemistry 43, 12390-12409 (Pubitemid 39314702)
    • (2004) Biochemistry , vol.43 , Issue.39 , pp. 12390-12409
    • Lawson, R.J.1    Von Wachenfeldt, C.2    Haq, I.3    Perkins, J.4    Munro, A.W.5
  • 47
    • 33745832316 scopus 로고    scopus 로고
    • Biophysical characterization of the sterol demethylase P450 from Mycobacterium tuberculosis, its cognate ferredoxin, and their interactions
    • DOI 10.1021/bi0601609
    • 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 tu-berculosis, its cognate ferredoxin, and their interactions. Biochemistry 45, 8427-8443 (Pubitemid 44036548)
    • (2006) Biochemistry , vol.45 , Issue.27 , 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
  • 50
    • 0020490891 scopus 로고
    • Sulfur donor ligand binding to ferric cytochrome P-450-CAM and myoglobin. Ultravioletvisible absorption, magnetic circular dichroism, and electron paramagnetic resonance spectroscopic investigation of the complexes
    • Sono, M., Andersson, L. A., and Dawson, J. H. (1982) Sulfur donor ligand binding to ferric cytochrome P-450-CAM and myoglobin. Ultravioletvisible absorption, magnetic circular dichroism, and electron paramagnetic resonance spectroscopic investigation 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
  • 52
    • 77951241302 scopus 로고    scopus 로고
    • Glutamate-haem ester bond formation is disfavored in flavocytochrome P450 BM3. Characterization of glutamate substitution mutants at the heme site of P450 BM3
    • Girvan, H. M., Levy, C. W., Williams, P., Fisher, K., Cheesman, M. R., Rigby, S. E., Leys, D., and Munro, A. W. (2010) Glutamate-haem ester bond formation is disfavored in flavocytochrome P450 BM3. Characterization of glutamate substitution mutants at the heme site of P450 BM3. Biochem. J. 427, 455-466
    • (2010) Biochem. J. , vol.427 , pp. 455-466
    • Girvan, H.M.1    Levy, C.W.2    Williams, P.3    Fisher, K.4    Cheesman, M.R.5    Rigby, S.E.6    Leys, D.7    Munro, A.W.8
  • 53
    • 0030445739 scopus 로고    scopus 로고
    • Probing the heme iron coordination structure of pressure-induced cytochrome P420cam
    • Martinis, S. A., Blanke, S. R., Hager, L. P., and Sligar, S. G. (1996) Probing the heme iron coordination structure of pressure-induced cytochrome P420cam. Biochemistry 35, 14530-14536
    • (1996) Biochemistry , vol.35 , pp. 14530-14536
    • Martinis, S.A.1    Blanke, S.R.2    Hager, L.P.3    Sligar, S.G.4
  • 54
    • 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
  • 55
    • 0020490659 scopus 로고
    • Formation of low spin complexes of ferric cytochrome P-450-CAM with anionic ligands. Spin state and ligand affinity comparison with myoglobin
    • Sono, M., and Dawson, J. H. (1982) Formation of low spin complexes of ferric cytochrome P-450-CAM with anionic ligands. Spin state and ligand affinity comparison with myoglobin. J. Biol. Chem. 257, 5496-5502
    • (1982) J. Biol. Chem. , vol.257 , pp. 5496-5502
    • Sono, M.1    Dawson, J.H.2
  • 56
    • 49349133018 scopus 로고
    • Analysis of low-spin ESR spectra of ferric heme proteins. A reexamination
    • Bohan, T. L. (1977) Analysis of low-spin ESR spectra of ferric heme proteins. A reexamination. J. Magn. Reson. 26, 109-118
    • (1977) J. Magn. Reson. , vol.26 , pp. 109-118
    • Bohan, T.L.1
  • 58
    • 0025894901 scopus 로고
    • Magnetic circular dichroism spectroscopy as a probe of axial heme ligand replacement in semisynthetic mutants of cytochrome c
    • Rux, J. J., and Dawson, J. H. (1991) Magnetic circular dichroism spectroscopy as a probe of axial heme ligand replacement in semisynthetic mutants of cytochrome c. FEBS Lett. 290, 49-51
    • (1991) FEBS Lett. , vol.290 , pp. 49-51
    • Rux, J.J.1    Dawson, J.H.2
  • 59
    • 33846015513 scopus 로고    scopus 로고
    • Crystal structure of the Mycobacterium tuberculosis P450 CYP121-fluconazole complex reveals new azole drug-P450 binding mode
    • DOI 10.1074/jbc.M607665200
    • Seward, H. E., Roujeinikova, A., McLean, K. J., Munro, A. W., and Leys, D. (2006) Crystal structure of the Mycobacterium tuberculosis P450 CYP121-fluconazole complex reveals new azole drug-P450 binding mode. J. Biol. Chem. 281, 39437-39443 (Pubitemid 46041903)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.51 , pp. 39437-39443
    • Seward, H.E.1    Roujeinikova, A.2    McLean, K.J.3    Munro, A.W.4    Leys, D.5
  • 61
    • 47749127412 scopus 로고    scopus 로고
    • The explosive-degrading cytochrome P450 system is highly conserved among strains of Rhodococcus spp.
    • DOI 10.1128/AEM.00391-08
    • Seth-Smith, H. M., Edwards, J., Rosser, S. J., Rathbone, D. A., and Bruce, N. C. (2008) The explosive-degrading cytochrome P450 system is highly conserved among strains of Rhodococcus spp. Appl. Environ. Microbiol. 74, 4550-4552 (Pubitemid 352031039)
    • (2008) Applied and Environmental Microbiology , vol.74 , Issue.14 , pp. 4550-4552
    • Seth-Smith, H.M.B.1    Edwards, J.2    Rosser, S.J.3    Rathbone, D.A.4    Bruce, N.C.5
  • 62
    • 29144448087 scopus 로고    scopus 로고
    • Mineralization of the cyclic nitramine explosive hexahydro-1,3,5- trinitro- 1,3,5-triazine by Gordonia and Williamsia spp.
    • DOI 10.1128/AEM.71.12.8265-8272.2005
    • Thompson, K. T., Crocker, F. H., and Fredrickson, H. L. (2005) Mineralization of the cyclic nitramine explosive hexahydro-1,3,5-trinitro-1,3,5- triazine by Gordonia and Williamsia spp. Appl. Environ. Microbiol. 71, 8265-8272 (Pubitemid 41803953)
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.12 , pp. 8265-8272
    • Thompson, K.T.1    Crocker, F.H.2    Fredrickson, H.L.3
  • 63
    • 66249124277 scopus 로고    scopus 로고
    • Lateral transfer of genes for hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) degradation
    • Andeer, P. F., Stahl, D. A., Bruce, N. C., and Strand, S. E. (2009) Lateral transfer of genes for hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) degradation. Appl. Environ. Microbiol. 75, 3258-3262
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 3258-3262
    • Andeer, P.F.1    Stahl, D.A.2    Bruce, N.C.3    Strand, S.E.4
  • 64
    • 0035856564 scopus 로고    scopus 로고
    • Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3
    • DOI 10.1021/bi010716m
    • 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 (Pubitemid 33130769)
    • (2001) Biochemistry , vol.40 , Issue.45 , pp. 13421-13429
    • Ost, T.W.B.1    Miles, C.S.2    Munro, A.W.3    Murdoch, J.4    Reid, G.A.5    Chapman, S.K.6
  • 66
    • 0036712117 scopus 로고    scopus 로고
    • Crystallographic investigation of the role of aspartate 95 in the modulation of the redox potentials of Desulfovibrio vulgaris flavodoxin
    • DOI 10.1021/bi020225h
    • McCarthy, A. A., Walsh, M. A., Verma, C. S., O'Connell, D. P., Reinhold, M., Yalloway, G. N., D'Arcy, D., Higgins, T. M., Voordouw, G., and Mayhew, S. G. (2002) Crystallographic investigation of the role of aspartate 95 in the modulation of the redox potentials of Desulfovibrio vulgaris flavodoxin. Biochemistry 41, 10950-10962 (Pubitemid 35001208)
    • (2002) Biochemistry , vol.41 , Issue.36 , pp. 10950-10962
    • McCarthy, A.A.1    Walsh, M.A.2    Verma, C.S.3    O'Connell, D.P.4    Reinhold, M.5    Yalloway, G.N.6    D'Arcy, D.7    Higgins, T.M.8    Voordouw, G.9    Mayhew, S.G.10
  • 67
    • 26844498754 scopus 로고    scopus 로고
    • The dimeric form of flavocytochrome P450 BM3 is catalytically functional as a fatty acid hydroxylase
    • DOI 10.1016/j.febslet.2005.09.023, PII S0014579305011300
    • 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 (Pubitemid 41455634)
    • (2005) FEBS Letters , vol.579 , Issue.25 , 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
  • 68
    • 84860223425 scopus 로고    scopus 로고
    • Characterization of Cupriavidus metallidurans CYP116B1. A thiocarbamate herbicide oxygenating P450-phthalate dioxygenase reductase fusion protein
    • Warman, A. J., Robinson, J. W., Luciakova, D., Lawrence, A. D., Marshall, K. R., Warren, M. J., Cheesman, M. R., Rigby, S. E., Munro, A. W., and McLean, K. J. (2012) Characterization of Cupriavidus metallidurans CYP116B1. A thiocarbamate herbicide oxygenating P450-phthalate dioxygenase reductase fusion protein. FEBS J. 279, 1675-1693
    • (2012) FEBS J. , vol.279 , pp. 1675-1693
    • Warman, A.J.1    Robinson, J.W.2    Luciakova, D.3    Lawrence, A.D.4    Marshall, K.R.5    Warren, M.J.6    Cheesman, M.R.7    Rigby, S.E.8    Munro, A.W.9    McLean, K.J.10
  • 69
    • 84892193594 scopus 로고    scopus 로고
    • Substrate oxidation by P450 enzymes
    • 3rd Ed. (Ortiz de Montellano, P. R., ed) Kluwer Academic/ Plenum Press, New York
    • Ortiz de Montellano, P. R., and De Voss, J. J. (2005) Substrate oxidation by P450 enzymes. in Cytochrome P450: Structure, Mechanism and Biochemistry, 3rd Ed. (Ortiz de Montellano, P. R., ed) pp. 183-245, Kluwer Academic/ Plenum Press, New York
    • (2005) Cytochrome P450: Structure, Mechanism and Biochemistry , pp. 183-245
    • Ortiz De Montellano, P.R.1    De Voss, J.J.2
  • 70
    • 0029586252 scopus 로고
    • Structure of cytochrome P450eryF involved in erythromycin biosynthesis
    • DOI 10.1038/nsb0295-144
    • Cupp-Vickery, J. R., and Poulos, T. L. (1995) Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Nat. Struct. Biol. 2, 144-153 (Pubitemid 26040651)
    • (1995) Nature Structural Biology , vol.2 , Issue.2 , pp. 144-153
    • Cupp-Vickery, J.R.1    Poulos, T.L.2
  • 71
    • 78649649951 scopus 로고    scopus 로고
    • Structural and biochemical characterization of Mycobacterium tuberculosis CYP142. Evidence for multiple cholesterol 27-hydroxylase activities in a human pathogen
    • Driscoll, M. D., McLean, K. J., Levy, C., Mast, N., Pikuleva, I. A., Lafite, P., Rigby, S. E., Leys, D., and Munro, A. W. (2010) Structural and biochemical characterization of Mycobacterium tuberculosis CYP142. Evidence for multiple cholesterol 27-hydroxylase activities in a human pathogen. J. Biol. Chem. 285, 38270-38282
    • (2010) J. Biol. Chem. , vol.285 , pp. 38270-38282
    • Driscoll, M.D.1    McLean, K.J.2    Levy, C.3    Mast, N.4    Pikuleva, I.A.5    Lafite, P.6    Rigby, S.E.7    Leys, D.8    Munro, A.W.9


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