메뉴 건너뛰기




Volumn , Issue , 2007, Pages 123-153

Cytochrome P450 Redox Partner Systems: Biodiversity and Biotechnological Implications

Author keywords

Artificial P450 redox partner fusion enzymes; Biocatalytic potential; Biodiversity; Biotechnological implications; Coenzyme issues; Cytochrome P450 redox partner systems; Diverse ferredoxins; Enzyme stability; Flavodoxins; Increasing P450 redox partner complexity; Modern biooxidation; Natural P450 redox partner fusion enzymes; P450 catalytic function; P450 redox partners

Indexed keywords


EID: 77955964576     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527611522.ch5     Document Type: Chapter
Times cited : (5)

References (147)
  • 1
    • 33745177792 scopus 로고    scopus 로고
    • Cytochrome P450 nomenclature, 2004
    • Nelson, D.R. Cytochrome P450 nomenclature, 2004. Methods Mol Biol 2006, 320, 1-10.
    • (2006) Methods Mol Biol , vol.320 , pp. 1-10
    • Nelson, D.R.1
  • 2
    • 0030009067 scopus 로고    scopus 로고
    • Bacterial cytochromes P450
    • Munro, A.W., Lindsay, J.G. Bacterial cytochromes P450. Mol Microbiol 1996, 20, 1115-1125.
    • (1996) Mol Microbiol , vol.20 , pp. 1115-1125
    • Munro, A.W.1    Lindsay, J.G.2
  • 3
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsoms. I. Evidence for its hemoprotein nature
    • Omura. T., Sato, R. The carbon monoxide-binding pigment of liver microsoms. I. Evidence for its hemoprotein nature. J Biol Chem 1964, 239, 2370-2378.
    • (1964) J Biol Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 4
    • 0024974060 scopus 로고
    • Crystal structure of the carbon monoxide-substratecytochrome P-450cam ternary complex
    • Raag, R., Poulos, T.L. Crystal structure of the carbon monoxide-substratecytochrome P-450cam ternary complex. Biochemistry 1989, 28, 7586-7592.
    • (1989) Biochemistry , vol.28 , pp. 7586-7592
    • Raag, R.1    Poulos, T.L.2
  • 5
    • 0022919721 scopus 로고
    • Crystal structure of substrate-free Pseudomonas putida cytochrome P-450
    • Poulos, T.L., Finzel, B.C., Howard, A.J. Crystal structure of substrate-free Pseudomonas putida cytochrome P-450. Biochemistry 1986, 25, 5314-5322.
    • (1986) Biochemistry , vol.25 , pp. 5314-5322
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 6
    • 0018820633 scopus 로고
    • NADPH cytochrome P450 reductase and its role in the mixed function oxidase reaction
    • Strobel, H.W., Dignam, J.D., Gunn, J.R. NADPH cytochrome P450 reductase and its role in the mixed function oxidase reaction. Pharmacol Ther 1980, 8, 525-537.
    • (1980) Pharmacol Ther , vol.8 , pp. 525-537
    • Strobel, H.W.1    Dignam, J.D.2    Gunn, J.R.3
  • 7
    • 0014429758 scopus 로고
    • A soluble cytochrome P-450 functional in methylene hydroxylation
    • Katagiri, M., Ganguli, B.N., Gunsalus, I.C. A soluble cytochrome P-450 functional in methylene hydroxylation. J Biol Chem 1968, 243, 3543-3564.
    • (1968) J Biol Chem , vol.243 , pp. 3543-3564
    • Katagiri, M.1    Ganguli, B.N.2    Gunsalus, I.C.3
  • 8
    • 0000350777 scopus 로고
    • Twenty-fi ve years of P450cam research
    • In: Ortiz de Montellano, P.R. (ed.), 2nd edn. New York: Plenum Press
    • Mueller, E.J., Loida, P.J., Sligar, S.G. Twenty-fi ve years of P450cam research. In: Ortiz de Montellano, P.R. (ed.) Cytochrome P450: Structure, Mechanism and Biochemistry, 2nd edn. New York: Plenum Press, 1995, pp. 83-124.
    • (1995) Cytochrome P450: Structure, Mechanism and Biochemistry , pp. 83-124
    • Mueller, E.J.1    Loida, P.J.2    Sligar, S.G.3
  • 9
    • 0141869098 scopus 로고    scopus 로고
    • Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida
    • Sevrioukova, I.F., Garcia, C., Li, H., Bhaskar, B., Poulos, T.L. Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida. J Mol Biol 2003, 333, 377-392.
    • (2003) J Mol Biol , vol.333 , pp. 377-392
    • Sevrioukova, I.F.1    Garcia, C.2    Li, H.3    Bhaskar, B.4    Poulos, T.L.5
  • 10
    • 1042264042 scopus 로고    scopus 로고
    • Crystal structure of putidaredoxin reductase from Pseudomonas putida, the fi nal structural component of the cytochrome P450cam monooxygenase
    • Sevrioukova, I.F., Li, H., Poulos, T.L. Crystal structure of putidaredoxin reductase from Pseudomonas putida, the fi nal structural component of the cytochrome P450cam monooxygenase. J Mol Biol 2004, 336, 889-902.
    • (2004) J Mol Biol , vol.336 , pp. 889-902
    • Sevrioukova, I.F.1    Li, H.2    Poulos, T.L.3
  • 11
    • 42449157733 scopus 로고
    • Models and mechanisms of cytochrome P450 action
    • In: Ortiz de Montellano, P.R. (ed.), 2nd edn. New York: Plenum Press
    • Groves, J.T. Models and mechanisms of cytochrome P450 action. In: Ortiz de Montellano, P.R. (ed.) Cytochrome P450: Structure, Mechanism and Biochemistry, 2nd edn. New York: Plenum Press, 1995, pp. 1-43.
    • (1995) Cytochrome P450: Structure, Mechanism and Biochemistry , pp. 1-43
    • Groves, J.T.1
  • 12
    • 0017170343 scopus 로고
    • Control of spin, substrate and redox equilibria in cytochrome P-450
    • Sligar, S.G. Control of spin, substrate and redox equilibria in cytochrome P-450. Biochemistry 1976, 15, 5399-5406.
    • (1976) Biochemistry , vol.15 , pp. 5399-5406
    • Sligar, S.G.1
  • 16
    • 2442552990 scopus 로고    scopus 로고
    • Expression, purifi cation and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: fl avocytochrome homologues of P450 BM3 from Bacillus megaterium
    • Gustafsson, M.C., Roitel, O., Marshall, K.R., Noble, M.A., Chapman, S.K., Pessegueiro, A., Fulco, A.J., Cheesman, M.R., Von Wachenfeldt, C., Munro, A.W. Expression, purifi cation and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: fl avocytochrome homologues of P450 BM3 from Bacillus megaterium. Biochemistry 2004, 43, 5474-5487.
    • (2004) Biochemistry , vol.43 , pp. 5474-5487
    • Gustafsson, M.C.1    Roitel, O.2    Marshall, K.R.3    Noble, M.A.4    Chapman, S.K.5    Pessegueiro, A.6    Fulco, A.J.7    Cheesman, M.R.8    Von Wachenfeldt, C.9    Munro, A.W.10
  • 17
    • 0037432069 scopus 로고    scopus 로고
    • Role of glutamic acid 216 in cytochrome P450 2D6 substrate binding and catalysis
    • Guengerich, F.P., Hanna, I.H., Martin, M.V., Gillam, E.M.J. Role of glutamic acid 216 in cytochrome P450 2D6 substrate binding and catalysis, Biochemistry 2003, 42, 1245-1253.
    • (2003) Biochemistry , vol.42 , pp. 1245-1253
    • Guengerich, F.P.1    Hanna, I.H.2    Martin, M.V.3    Gillam, E.M.J.4
  • 19
    • 27544483600 scopus 로고    scopus 로고
    • Thirty years of microbial P450 monooxygenase research: peroxo-heme intermediates-the central bus station in heme oxygenase catalysis
    • Sligar, S.G, Makris, T.M., Denisov, I.G. Thirty years of microbial P450 monooxygenase research: peroxo-heme intermediates-the central bus station in heme oxygenase catalysis. Biochem Biophys Res Commun 2005, 338, 346-354.
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 346-354
    • Sligar, S.G.1    Makris, T.M.2    Denisov, I.G.3
  • 20
    • 0023645035 scopus 로고
    • High-resolution crystal structure of cytochrome P450cam
    • Poulos, T.L., Finzel, B.C., Howard, A.J. High-resolution crystal structure of cytochrome P450cam. J Mol Biol 1987, 195, 687-700.
    • (1987) J Mol Biol , vol.195 , pp. 687-700
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 21
    • 0023583624 scopus 로고
    • Crystal structures of metyrapone-and phenylimidazole-inhibited complexes of cytochrome P-450cam
    • Poulos, T.L., Howard, A.J. Crystal structures of metyrapone-and phenylimidazole-inhibited complexes of cytochrome P-450cam. J Mol Biol 1987, 26, 8165-8174.
    • (1987) J Mol Biol , vol.26 , pp. 8165-8174
    • Poulos, T.L.1    Howard, A.J.2
  • 22
    • 0001127948 scopus 로고
    • A thermodynamic model of regulation: modulation of redox equilibria in camphor monoxygenase
    • Sligar, S.G., Gunsalus, I.C. A thermodynamic model of regulation: modulation of redox equilibria in camphor monoxygenase. Proc Natl Acad Sci USA 1976, 73, 1078-1082.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 1078-1082
    • Sligar, S.G.1    Gunsalus, I.C.2
  • 23
    • 0017170343 scopus 로고
    • Coupling of spin, substrate, and redox equilibria in cytochrome P450
    • Sligar, S.G. Coupling of spin, substrate, and redox equilibria in cytochrome P450. Biochemistry 1976, 15, 5399-5406.
    • (1976) Biochemistry , vol.15 , pp. 5399-5406
    • Sligar, S.G.1
  • 24
    • 0023867587 scopus 로고
    • Single turnover kinetics of the reaction between oxycytochrome P-450cam and reduced putidaredoxin
    • Brewer, J.A., Peterson, J.A. Single turnover kinetics of the reaction between oxycytochrome P-450cam and reduced putidaredoxin. J Biol Chem 1988, 263, 791-798.
    • (1988) J Biol Chem , vol.263 , pp. 791-798
    • Brewer, J.A.1    Peterson, J.A.2
  • 25
    • 0022930461 scopus 로고
    • The involvement of carboxylate groups of putidaredoxin in the reaction with putidaredoxin reductase
    • Geren, L., Tuls, J., O'Brien, P., Millett, F., Peterson, J.A. The involvement of carboxylate groups of putidaredoxin in the reaction with putidaredoxin reductase. J Biol Chem 1986, 261, 15491-15495.
    • (1986) J Biol Chem , vol.261 , pp. 15491-15495
    • Geren, L.1    Tuls, J.2    O'Brien, P.3    Millett, F.4    Peterson, J.A.5
  • 26
    • 0021351056 scopus 로고
    • Identifi cation of specifi c carboxylate groups on adrenodoxin that are involved in the interactin with adrenodoxin reductase
    • Geren, L.M., O'Brien, P., Stonehuerner, J., Millett, F. Identifi cation of specifi c carboxylate groups on adrenodoxin that are involved in the interactin with adrenodoxin reductase. J Biol Chem 1984, 259, 2155-2160.
    • (1984) J Biol Chem , vol.259 , pp. 2155-2160
    • Geren, L.M.1    O'Brien, P.2    Stonehuerner, J.3    Millett, F.4
  • 27
    • 0024468304 scopus 로고
    • Putidaredoxin competitively inhibits cytochrome b5-cytochrome P-450cam association: A proposed molecular model for a cytochrome P-450cam electron-transfer complex
    • Stayton, P.S., Poulos, T.L., Sligar, S.G. Putidaredoxin competitively inhibits cytochrome b5-cytochrome P-450cam association: A proposed molecular model for a cytochrome P-450cam electron-transfer complex. Biochemistry 1989, 28, 8201-8205.
    • (1989) Biochemistry , vol.28 , pp. 8201-8205
    • Stayton, P.S.1    Poulos, T.L.2    Sligar, S.G.3
  • 28
    • 0025195188 scopus 로고
    • The cytochrome P-450cam binding surface as defi ned by site-directed mutagenesis and electrostatic modelling
    • Stayton, P.S., Sligar, S.G. The cytochrome P-450cam binding surface as defi ned by site-directed mutagenesis and electrostatic modelling. Biochemistry 1990, 29, 7381-7386.
    • (1990) Biochemistry , vol.29 , pp. 7381-7386
    • Stayton, P.S.1    Sligar, S.G.2
  • 29
    • 0029054788 scopus 로고
    • Modulation of the activity of human 17 alphahydroxylase-17,20-lyase (CYP17) by cytochrome b5: endocrinological and mechanistic implications
    • Lee-Robichaud, P., Wright, J.N., Akhtar, M.E., Akhtar, M. Modulation of the activity of human 17 alphahydroxylase-17,20-lyase (CYP17) by cytochrome b5: endocrinological and mechanistic implications. Biochem J 1995, 308, 901-908.
    • (1995) Biochem J , vol.308 , pp. 901-908
    • Lee-Robichaud, P.1    Wright, J.N.2    Akhtar, M.E.3    Akhtar, M.4
  • 31
    • 0039621987 scopus 로고
    • A role for putidaredoxin COOH-terminus in P-450cam (cytochrome m) hydroxylations
    • USA
    • Sligar, S.G., Debrunner, P.G., Lipscomb, J.D., Namtvedt, M.J., Gunsalus, I.C. A role for putidaredoxin COOH-terminus in P-450cam (cytochrome m) hydroxylations. Proc Natl Acad Sci USA 1974, 71, 3906-3910.
    • (1974) , vol.71 , pp. 3906-3910
    • Sligar, S.G.1    Debrunner, P.G.2    Lipscomb, J.D.3    Namtvedt, M.J.4    Gunsalus, I.C.5
  • 32
    • 0025049895 scopus 로고
    • Putidaredoxin's reduction of cytochrome P-450cam: Dependence of electron transfer on the identity of putidaredoxin's C-terminal amino acid
    • Davies, M.D., Qin, L., Beck, J.L., Suslick, K.S., Koga, H., Horiuchi, T., Sligar, S.G. Putidaredoxin's reduction of cytochrome P-450cam: Dependence of electron transfer on the identity of putidaredoxin's C-terminal amino acid. J Am Chem Soc 1990, 112, 7396-7398.
    • (1990) J Am Chem Soc , vol.112 , pp. 7396-7398
    • Davies, M.D.1    Qin, L.2    Beck, J.L.3    Suslick, K.S.4    Koga, H.5    Horiuchi, T.6    Sligar, S.G.7
  • 33
    • 0026442895 scopus 로고
    • Genetic variants in the putidaredoxincytochrome P-450cam electron transfer complex: Identifi cation of the residue responsible for redox-state-dependent conformers
    • Davies. M.D., Sligar, S.G. Genetic variants in the putidaredoxincytochrome P-450cam electron transfer complex: Identifi cation of the residue responsible for redox-state-dependent conformers. Biochemistry 1992, 31, 11383-11389.
    • (1992) Biochemistry , vol.31 , pp. 11383-11389
    • Davies, M.D.1    Sligar, S.G.2
  • 34
    • 0024974060 scopus 로고
    • Crystal structure of the carbon monoxide-substratecytochrome P-450cam ternary complex
    • Raag, R., Poulos, T.L. Crystal structure of the carbon monoxide-substratecytochrome P-450cam ternary complex. Biochemistry 1989, 28, 7586-7592.
    • (1989) Biochemistry , vol.28 , pp. 7586-7592
    • Raag, R.1    Poulos, T.L.2
  • 35
    • 14744286132 scopus 로고    scopus 로고
    • Redox-dependent structural reorganization in putidaredoxin, a vertebrate-type [2Fe-2S] ferredoxin from Pseudomonas putida
    • Sevrioukova, I.F. Redox-dependent structural reorganization in putidaredoxin, a vertebrate-type [2Fe-2S] ferredoxin from Pseudomonas putida. J Mol Biol 2005, 347, 607-621.
    • (2005) J Mol Biol , vol.347 , pp. 607-621
    • Sevrioukova, I.F.1
  • 36
    • 18144391863 scopus 로고    scopus 로고
    • The putidaredoxin reductaseputidaredoxin electron transfer complex: theoretical and experimental studies
    • Kuznetzov, V.Y., Blair, E., Farmer, P.J., Poulos, T.L., Pifferitti, A., Sevriouokova I.F. The putidaredoxin reductaseputidaredoxin electron transfer complex: theoretical and experimental studies. J Biol Chem 2005, 280, 16135-16142.
    • (2005) J Biol Chem , vol.280 , pp. 16135-16142
    • Kuznetzov, V.Y.1    Blair, E.2    Farmer, P.J.3    Poulos, T.L.4    Pifferitti, A.5    Sevriouokova, I.F.6
  • 38
    • 0021254794 scopus 로고
    • Discriminatory processing of the precursor forms of cytochrome P-450scc and adrenodoxin by adrenocortical and heart mitochondria
    • Matocha, M.F., Waterman, M.R. Discriminatory processing of the precursor forms of cytochrome P-450scc and adrenodoxin by adrenocortical and heart mitochondria. J Biol Chem 1984, 259, 8672-8678.
    • (1984) J Biol Chem , vol.259 , pp. 8672-8678
    • Matocha, M.F.1    Waterman, M.R.2
  • 39
    • 0032520951 scopus 로고    scopus 로고
    • New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108)
    • Müller, A., Müller, J.J., Müller, Y.A., Uhlmann, H., Bernhardt, R., Heinemann, U. New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108). Structure 1998, 6, 269-280.
    • (1998) Structure , vol.6 , pp. 269-280
    • Müller, A.1    Müller, J.J.2    Müller, Y.A.3    Uhlmann, H.4    Bernhardt, R.5    Heinemann, U.6
  • 40
    • 0033979988 scopus 로고    scopus 로고
    • The tertiary structure of full-length bovine adrenodoxin suggests functional dimers
    • Pikuleva, I.A., Tesh, K., Waterman, M.R., Kim, Y. The tertiary structure of full-length bovine adrenodoxin suggests functional dimers. Arch Biochem Biophys 2000, 373, 44-55.
    • (2000) Arch Biochem Biophys , vol.373 , pp. 44-55
    • Pikuleva, I.A.1    Tesh, K.2    Waterman, M.R.3    Kim, Y.4
  • 41
    • 0033057396 scopus 로고    scopus 로고
    • The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis
    • Ziegler, G.A., Vonrhein, C., Hanukoglu, I., Schulz, G.E. The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis. J Mol Biol 1999, 289, 981-990.
    • (1999) J Mol Biol , vol.289 , pp. 981-990
    • Ziegler, G.A.1    Vonrhein, C.2    Hanukoglu, I.3    Schulz, G.E.4
  • 42
    • 0031022337 scopus 로고    scopus 로고
    • Molecular recognition and electron transfer in the mitochondrial steroid hydroxylase system
    • Vickery, L.E. Molecular recognition and electron transfer in the mitochondrial steroid hydroxylase system. Steroids 1997, 62, 124-127.
    • (1997) Steroids , vol.62 , pp. 124-127
    • Vickery, L.E.1
  • 43
    • 0018291970 scopus 로고
    • Ionic effects on adrenal steroidogenic electron transport
    • Lambeth, J.D., Seybert, D.W., Kamin, H. Ionic effects on adrenal steroidogenic electron transport. J Biol Chem 1979, 254, 7255-7264.
    • (1979) J Biol Chem , vol.254 , pp. 7255-7264
    • Lambeth, J.D.1    Seybert, D.W.2    Kamin, H.3
  • 44
    • 0035951779 scopus 로고    scopus 로고
    • Adrenodxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis
    • Müller, J., Lapko, A., Bourenkov, G., Ruckpaul, K., Heinemann, U. Adrenodxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis. J Biol Chem 2001, 276, 2786-2789.
    • (2001) J Biol Chem , vol.276 , pp. 2786-2789
    • Müller, J.1    Lapko, A.2    Bourenkov, G.3    Ruckpaul, K.4    Heinemann, U.5
  • 46
    • 0025976756 scopus 로고
    • An unusual yet strongly conserved fl avoprotein reductase in bacteria and mammals
    • Porter, T.D. An unusual yet strongly conserved fl avoprotein reductase in bacteria and mammals. Trends Biochem Sci 1991, 16, 154-158.
    • (1991) Trends Biochem Sci , vol.16 , pp. 154-158
    • Porter, T.D.1
  • 47
    • 0034719132 scopus 로고    scopus 로고
    • Trp-676 facilitates nicotinamide coenzyme exchange in the reductive half-reaction of human cytochrome P450 reductase: properties of the soluble W676H and W676A mutant reductases
    • Gutierrez, A., Doehr, O., Paine, M., Wolf, C.R., Scrutton, N.S., Roberts, G.C. Trp-676 facilitates nicotinamide coenzyme exchange in the reductive half-reaction of human cytochrome P450 reductase: properties of the soluble W676H and W676A mutant reductases. Biochemistry 2000, 39, 15990-15999.
    • (2000) Biochemistry , vol.39 , pp. 15990-15999
    • Gutierrez, A.1    Doehr, O.2    Paine, M.3    Wolf, C.R.4    Scrutton, N.S.5    Roberts, G.C.6
  • 48
    • 0030873316 scopus 로고    scopus 로고
    • Three dimensional structure of NADPHcytochrome P450 reductase-prototype for FAD-and FMN-containing enzymes
    • USA
    • Wang, M., Roberts, D.L., Paschke, R., Shea, T.M., Masters, B.S.S., Kim, J.-J.P. Three dimensional structure of NADPHcytochrome P450 reductase-prototype for FAD-and FMN-containing enzymes. Proc Natl Acad Sci USA 1997, 94, 9411-9416.
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 9411-9416
    • Wang, M.1    Roberts, D.L.2    Paschke, R.3    Shea, T.M.4    Masters, B.S.S.5    Kim, J.-J.P.6
  • 49
    • 0028106174 scopus 로고
    • Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains
    • USA
    • Smith, G.C., Tew, D.G., Wolf, C.R. Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains. Proc Natl Acad Sci USA1994, 91, 8710-8714.
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 8710-8714
    • Smith, G.C.1    Tew, D.G.2    Wolf, C.R.3
  • 50
    • 0035916295 scopus 로고    scopus 로고
    • Determination of the redox properties of human NADPH-cytochrome P450 reductase
    • Munro, A.W., Noble, M.A., Robledo, L., Daff, S.N., Chapman, S.K. Determination of the redox properties of human NADPH-cytochrome P450 reductase. Biochemistry 2001, 40, 1956-1963.
    • (2001) Biochemistry , vol.40 , pp. 1956-1963
    • Munro, A.W.1    Noble, M.A.2    Robledo, L.3    Daff, S.N.4    Chapman, S.K.5
  • 52
    • 0035800760 scopus 로고    scopus 로고
    • NADPHcytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer
    • Hubbard, P.A., Shen, A.L., Paschke, R., Kasper, C.B., Kim, J.-J. NADPHcytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer. J Biol Chem 2001, 276, 29163-29170.
    • (2001) J Biol Chem , vol.276 , pp. 29163-29170
    • Hubbard, P.A.1    Shen, A.L.2    Paschke, R.3    Kasper, C.B.4    Kim, J.-J.5
  • 53
    • 0017801794 scopus 로고
    • Purifi ed liver microsomal NADPH-cytochrome P-450 reductase. Spectral characterization of oxidation-reduction states
    • Vermillion, J.L., Coon, M.J. Purifi ed liver microsomal NADPH-cytochrome P-450 reductase. Spectral characterization of oxidation-reduction states. J Biol Chem 1978, 253, 2694-2704.
    • (1978) J Biol Chem , vol.253 , pp. 2694-2704
    • Vermillion, J.L.1    Coon, M.J.2
  • 54
    • 0033605237 scopus 로고    scopus 로고
    • Mechanistic studies on the reductive half-reaction of NADPH-cytochrome P450 oxidoreductase
    • Shen, A.L., Sem, D.S., Kasper, C.B. Mechanistic studies on the reductive half-reaction of NADPH-cytochrome P450 oxidoreductase. J Biol Chem 1999, 274, 5391-5398.
    • (1999) J Biol Chem , vol.274 , pp. 5391-5398
    • Shen, A.L.1    Sem, D.S.2    Kasper, C.B.3
  • 55
    • 0347093470 scopus 로고    scopus 로고
    • Electron transfer in human methionine synthase reductase studied by stopped-fl ow spectrophotometry
    • Wolthers, K.R., Scrutton, N.S. Electron transfer in human methionine synthase reductase studied by stopped-fl ow spectrophotometry. Biochemistry 2004, 43, 490-500.
    • (2004) Biochemistry , vol.43 , pp. 490-500
    • Wolthers, K.R.1    Scrutton, N.S.2
  • 58
    • 0345505668 scopus 로고    scopus 로고
    • Determination of the redox potentials and electron transfer properties of the FAD-and FMNbinding domains of the human oxidoreductase NR1
    • Finn, R.D., Basran, J., Roitel, O., Wolf, C.R., Munro, A.W., Paine, M.J., Scrutton, N.S. Determination of the redox potentials and electron transfer properties of the FAD-and FMNbinding domains of the human oxidoreductase NR1. Eur J Biochem 2003, 270, 1164-1175.
    • (2003) Eur J Biochem , vol.270 , pp. 1164-1175
    • Finn, R.D.1    Basran, J.2    Roitel, O.3    Wolf, C.R.4    Munro, A.W.5    Paine, M.J.6    Scrutton, N.S.7
  • 59
    • 0035793117 scopus 로고    scopus 로고
    • Engineering of a functional human NADHdependent cytochrome P450 system
    • USA
    • Dohr, O., Paine, M.J., Friedberg, T., Roberts, G.C., Wolf, C.R. Engineering of a functional human NADHdependent cytochrome P450 system. Proc Natl Acad Sci USA 2001, 98, 81-86.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 81-86
    • Dohr, O.1    Paine, M.J.2    Friedberg, T.3    Roberts, G.C.4    Wolf, C.R.5
  • 61
    • 0025755694 scopus 로고
    • Probing the roles of lysines and arginines in the catalytic function of cytochrome-P450d by sitedirected mutagenesis-interaction with NADPH-cytochrome-P450 reductase
    • Shimizu, T., Tateishi, T., Hatano, M., Fujiikuriyama, Y. Probing the roles of lysines and arginines in the catalytic function of cytochrome-P450d by sitedirected mutagenesis-interaction with NADPH-cytochrome-P450 reductase. J Biol Chem 1991, 266, 3372-3375.
    • (1991) J Biol Chem , vol.266 , pp. 3372-3375
    • Shimizu, T.1    Tateishi, T.2    Hatano, M.3    Fujiikuriyama, Y.4
  • 62
    • 0027216444 scopus 로고
    • Role of lysine and arginine residues of cytochrome P450 in the interaction between cytochrome P4502B1 and NADPHcytochrome P450 reductase
    • Shen, S., Strobel, H.W. Role of lysine and arginine residues of cytochrome P450 in the interaction between cytochrome P4502B1 and NADPHcytochrome P450 reductase. Arch Biochem Biophys 1993, 304, 257-265.
    • (1993) Arch Biochem Biophys , vol.304 , pp. 257-265
    • Shen, S.1    Strobel, H.W.2
  • 63
    • 0032479307 scopus 로고    scopus 로고
    • Identifi cation of the binding site on cytochrome P450 2B4 for cytochrome b5 and cytochrome P450 reductase
    • Bridges, A., Gruenke, L., Chang, Y.T., Vasker, I.A., Loew, G., Waskell, L. Identifi cation of the binding site on cytochrome P450 2B4 for cytochrome b5 and cytochrome P450 reductase. J Biol Chem 1998, 273, 17036-17049.
    • (1998) J Biol Chem , vol.273 , pp. 17036-17049
    • Bridges, A.1    Gruenke, L.2    Chang, Y.T.3    Vasker, I.A.4    Loew, G.5    Waskell, L.6
  • 64
    • 0025939628 scopus 로고
    • Identifi cation and characterization of an NADPH-cytochrome P450 reductase derived peptide involved in binding to cytochrome P450
    • Nadler, S.G., Strobel, H.W. Identifi cation and characterization of an NADPH-cytochrome P450 reductase derived peptide involved in binding to cytochrome P450. Arch Biochem Biophys 1991, 290, 277-284.
    • (1991) Arch Biochem Biophys , vol.290 , pp. 277-284
    • Nadler, S.G.1    Strobel, H.W.2
  • 65
    • 0028352320 scopus 로고
    • Quantitative analyses of electrostatic interactions between NADPHcytochrome P450 reductase and cytochrome P450 enzymes
    • Voznesensky, A.I., Schenkman, J.B. Quantitative analyses of electrostatic interactions between NADPHcytochrome P450 reductase and cytochrome P450 enzymes. J Biol Chem 1994, 269, 15724-15731.
    • (1994) J Biol Chem , vol.269 , pp. 15724-15731
    • Voznesensky, A.I.1    Schenkman, J.B.2
  • 66
    • 0026718792 scopus 로고
    • The cytochrome P450 2B4-NADPH cytochrome P450 reductase electron transfer complex is not formed by charge-pairing
    • Voznesensky, A.I., Schenkman, J.B. The cytochrome P450 2B4-NADPH cytochrome P450 reductase electron transfer complex is not formed by charge-pairing. J Biol Chem 1992, 267, 1466-14676.
    • (1992) J Biol Chem , vol.267 , pp. 1466-14676
    • Voznesensky, A.I.1    Schenkman, J.B.2
  • 67
    • 0028172287 scopus 로고
    • Infl uence of ionic strength on the P450 monooxygenase reaction and role of cytochrome b5 in the process
    • Voznesensky, A.I., Schenkman, J.B. Infl uence of ionic strength on the P450 monooxygenase reaction and role of cytochrome b5 in the process. Arch Biochem Biophys 1994, 314, 234-241.
    • (1994) Arch Biochem Biophys , vol.314 , pp. 234-241
    • Voznesensky, A.I.1    Schenkman, J.B.2
  • 68
    • 0025922972 scopus 로고
    • P450BM-3 and other inducible bacterial P450 cytochromes: biochemistry and regulation
    • Fulco, A.J. P450BM-3 and other inducible bacterial P450 cytochromes: biochemistry and regulation. Annu Rev Pharmacol Toxicol 1991, 31, 177-203.
    • (1991) Annu Rev Pharmacol Toxicol , vol.31 , pp. 177-203
    • Fulco, A.J.1
  • 69
    • 0022878676 scopus 로고
    • Characterization of a catalytically self-suffi cient 119,000-dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium
    • Narhi, L.O., Fulco, A.J. Characterization of a catalytically self-suffi cient 119,000-dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium. J Biol Chem 1986, 261, 7160-7169.
    • (1986) J Biol Chem , vol.261 , pp. 7160-7169
    • Narhi, L.O.1    Fulco, A.J.2
  • 70
    • 0023654954 scopus 로고
    • Identifi cation and characterization of two functional domains in cytochrome P-450BM-3, a catalytically self-suffi cient monooxygenase induced by barbiturates in Bacillus megaterium
    • Narhi, L.O., Fulco, A.J. Identifi cation and characterization of two functional domains in cytochrome P-450BM-3, a catalytically self-suffi cient monooxygenase induced by barbiturates in Bacillus megaterium. J Biol Chem 1987, 262, 6683-6690.
    • (1987) J Biol Chem , vol.262 , pp. 6683-6690
    • Narhi, L.O.1    Fulco, A.J.2
  • 72
    • 0030057886 scopus 로고    scopus 로고
    • Probing electron transfer in fl avocytochrome P-450 BM3 and its component domains
    • Munro, A.W., Daff, S., Coggins, J.R., Lindsay, J.G., Chapman, S.K. Probing electron transfer in fl avocytochrome P-450 BM3 and its component domains. Eur J Biochem 1996, 239, 403-409.
    • (1996) Eur J Biochem , vol.239 , pp. 403-409
    • Munro, A.W.1    Daff, S.2    Coggins, J.R.3    Lindsay, J.G.4    Chapman, S.K.5
  • 73
    • 0016738181 scopus 로고
    • Omega-1, omega-2 and omega-3 hydroxylation of long-chain fatty acids, amides and alcohols by a soluble enzyme system from Bacillus megaterium
    • Miura, Y., Fulco, A.J. Omega-1, omega-2 and omega-3 hydroxylation of long-chain fatty acids, amides and alcohols by a soluble enzyme system from Bacillus megaterium. Biochim Biophys Acta 1975, 388, 305-317.
    • (1975) Biochim Biophys Acta , vol.388 , pp. 305-317
    • Miura, Y.1    Fulco, A.J.2
  • 74
    • 0031021585 scopus 로고    scopus 로고
    • An active site substitution, F87V, converts cytochrome P450 BM-3 into a regioand stereoselective (14S,15R)-arachidonic acid epoxygenase
    • Graham-Lorence, S., Truan, G., Peterson, J.A., Falck, J.R., Wei, S., Helvig, C., Capdevila, J.H. An active site substitution, F87V, converts cytochrome P450 BM-3 into a regioand stereoselective (14S,15R)-arachidonic acid epoxygenase. J Biol Chem 1997, 272, 1127-1135.
    • (1997) J Biol Chem , vol.272 , pp. 1127-1135
    • Graham-Lorence, S.1    Truan, G.2    Peterson, J.A.3    Falck, J.R.4    Wei, S.5    Helvig, C.6    Capdevila, J.H.7
  • 75
    • 0028861062 scopus 로고
    • The role of Thr268 in oxygen activation of cytochrome P450BM-3
    • Yeom, H., Sligar, S.G., Li, H., Poulos, T.L., Fulco, A.J. The role of Thr268 in oxygen activation of cytochrome P450BM-3. Biochemistry 1995, 34, 14733-14740.
    • (1995) Biochemistry , vol.34 , pp. 14733-14740
    • Yeom, H.1    Sligar, S.G.2    Li, H.3    Poulos, T.L.4    Fulco, A.J.5
  • 77
    • 0035856564 scopus 로고    scopus 로고
    • Phenylalanine 393 exerts thermodynamic control over the heme of fl avocytochrome P450 BM3
    • Ost, T.W., Miles, C.S., Munro, A.W., Murdoch, J., Reid, G.A., Chapman, S. K. Phenylalanine 393 exerts thermodynamic control over the heme of fl avocytochrome P450 BM3. Biochemistry 2001, 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
  • 78
    • 0042819974 scopus 로고    scopus 로고
    • Electron transfer in fl avocytochrome P450 BM3: kinetics of fl avin reduction and oxidation, the role of cysteine 999, and relationships with mammalian cytochrome P450 reductase
    • Roitel, O., Scrutton, N.S., Munro, A.W. Electron transfer in fl avocytochrome P450 BM3: kinetics of fl avin reduction and oxidation, the role of cysteine 999, and relationships with mammalian cytochrome P450 reductase, Biochemistry 2003, 42, 10809-10821.
    • (2003) Biochemistry , vol.42 , pp. 10809-10821
    • Roitel, O.1    Scrutton, N.S.2    Munro, A.W.3
  • 79
    • 0030960888 scopus 로고    scopus 로고
    • The domain architecture of cytochrome P450BM-3
    • Govindaraj, S., Poulos, T.L. The domain architecture of cytochrome P450BM-3. J Biol Chem 1997, 272, 7915-7921.
    • (1997) J Biol Chem , vol.272 , pp. 7915-7921
    • Govindaraj, S.1    Poulos, T.L.2
  • 80
    • 0026452788 scopus 로고
    • Domains of the catalytically self-suffi cient cytochrome P-450 BM-3. Genetic construction, overexpression, purifi cation and spectroscopic characterization
    • Miles, J.S., Munro, A.W., Rospendowski, B.N., Smith, W.E., McKnight, J., Thomson, A.J. Domains of the catalytically self-suffi cient cytochrome P-450 BM-3. Genetic construction, overexpression, purifi cation and spectroscopic characterization. Biochem J 1992, 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
  • 82
    • 0031013972 scopus 로고    scopus 로고
    • The structure of the cytochrome P450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid
    • Li, H., Poulos, T.L. The structure of the cytochrome P450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid. Nat Struct Biol 1997, 4, 140-146.
    • (1997) Nat Struct Biol , vol.4 , pp. 140-146
    • Li, H.1    Poulos, T.L.2
  • 84
    • 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., Leys, D. A single mutation in cytochrome P450 BM3 induces the conformational rearrangement seen upon substrate binding in the wild-type enzyme. J Biol Chem 2004, 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
  • 85
    • 0033514990 scopus 로고    scopus 로고
    • Structure of a cytochrome P450-redox partner electron-transfer complex
    • USA
    • Sevrioukova, I.F., Li, H., Zhang, H., Peterson, J.A., Poulos, T.L. Structure of a cytochrome P450-redox partner electron-transfer complex, Proc Natl Acad Sci USA 1999, 96, 1863-1888.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 1863-1888
    • Sevrioukova, I.F.1    Li, H.2    Zhang, H.3    Peterson, J.A.4    Poulos, T.L.5
  • 86
    • 0034680319 scopus 로고    scopus 로고
    • Functional interactions in cytochrome P450 BM3: Evidence that NADP(H) binding controls redox potentials of the fl avin cofactors
    • Murataliev, M.B., Feyereisen, R. Functional interactions in cytochrome P450 BM3: Evidence that NADP(H) binding controls redox potentials of the fl avin cofactors. Biochemistry 2000, 39, 12699-12707.
    • (2000) Biochemistry , vol.39 , pp. 12699-12707
    • Murataliev, M.B.1    Feyereisen, R.2
  • 87
    • 8844239344 scopus 로고    scopus 로고
    • The unusual redox properties of fl avocytochrome P450 BM3 fl avodoxin domain
    • Hanley, S.C., Daff, S. The unusual redox properties of fl avocytochrome P450 BM3 fl avodoxin domain. Biochem Biophys Res Commun 2004, 325, 1418-1423.
    • (2004) Biochem Biophys Res Commun , vol.325 , pp. 1418-1423
    • Hanley, S.C.1    Daff, S.2
  • 88
    • 26844498754 scopus 로고    scopus 로고
    • The dimeric form of fl avocytochrome 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., Munro, A.W. The dimeric form of fl avocytochrome P450 BM3 is catalytically functional as a fatty acid hydroxylase. FEBS Lett 2005, 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
  • 89
    • 32344437281 scopus 로고    scopus 로고
    • Altering the regioselectivity of cytochrome P450 CYP102A3 of Bacillus subtilis by using a new versatile assay system
    • Lentz, O., Feenstra, A., Habicher, T., Hauer, B., Schmid, R.D., Urlacher, V.B. Altering the regioselectivity of cytochrome P450 CYP102A3 of Bacillus subtilis by using a new versatile assay system. ChemBiochem 2006, 7, 345-350.
    • (2006) ChemBiochem , vol.7 , pp. 345-350
    • Lentz, O.1    Feenstra, A.2    Habicher, T.3    Hauer, B.4    Schmid, R.D.5    Urlacher, V.B.6
  • 90
    • 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., Shiro, Y. Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies, J Biol Chem 2003, 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
  • 91
    • 0035573747 scopus 로고    scopus 로고
    • Characterization of four clustered and coregulated genes associated with fumonisin biosynthesis in Fusarium verticillioides
    • Seo, J.A., Proctor, R.H., Plattner, R.D. Characterization of four clustered and coregulated genes associated with fumonisin biosynthesis in Fusarium verticillioides. Fungal Genet Biol 2001, 34, 155-165.
    • (2001) Fungal Genet Biol , vol.34 , pp. 155-165
    • Seo, J.A.1    Proctor, R.H.2    Plattner, R.D.3
  • 92
    • 0028792364 scopus 로고
    • Structure and mechanism of the ironsulfur fl avoprotein phthalate dioxygenase reductase
    • Gassner, G.T., Ludwig, M.L., Gatti, D.L., Correll, C.C., Ballou, D.P. Structure and mechanism of the ironsulfur fl avoprotein phthalate dioxygenase reductase. FASEB J 1995, 9, 1411-1418.
    • (1995) FASEB J , vol.9 , pp. 1411-1418
    • Gassner, G.T.1    Ludwig, M.L.2    Gatti, D.L.3    Correll, C.C.4    Ballou, D.P.5
  • 93
    • 17644402801 scopus 로고    scopus 로고
    • Chemistry of the catalytic conversion of phthalate into its cis-dihydrodiol during the reaction of oxygen with the reduced form of phthalate dioxygenase
    • Tarasev, M., Ballou, D.P. Chemistry of the catalytic conversion of phthalate into its cis-dihydrodiol during the reaction of oxygen with the reduced form of phthalate dioxygenase. Biochemistry 2005, 44, 6197-6207.
    • (2005) Biochemistry , vol.44 , pp. 6197-6207
    • Tarasev, M.1    Ballou, D.P.2
  • 94
    • 4944224145 scopus 로고    scopus 로고
    • Rates of the phthalate dioxygenase reaction with oxygen are dramatically increased by interactions with phthalate and phthalate oxygenase reductase
    • Tarasev, M., Rhames, F., Ballou, D.P. Rates of the phthalate dioxygenase reaction with oxygen are dramatically increased by interactions with phthalate and phthalate oxygenase reductase. Biochemistry 2004, 43, 12799-12808.
    • (2004) Biochemistry , vol.43 , pp. 12799-12808
    • Tarasev, M.1    Rhames, F.2    Ballou, D.P.3
  • 95
    • 0027093793 scopus 로고
    • Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotide to [2Fe-2S]
    • Correll, C.C., Batie, C.J., Ballou, D.P., Ludwig, M.L. Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotide to [2Fe-2S]. Science 1992, 258, 1604-1610.
    • (1992) Science , vol.258 , pp. 1604-1610
    • Correll, C.C.1    Batie, C.J.2    Ballou, D.P.3    Ludwig, M.L.4
  • 96
    • 0036844477 scopus 로고    scopus 로고
    • A novel class of self-suffi cient cytochrome P450 mono-oxygenases in prokaryotes
    • De Mot, R., Parret, A.H.A. A novel class of self-suffi cient cytochrome P450 mono-oxygenases in prokaryotes. Trends Microbiol 2002, 10, 502-508.
    • (2002) Trends Microbiol , vol.10 , pp. 502-508
    • De Mot, R.1    Parret, A.H.A.2
  • 97
    • 1542571790 scopus 로고    scopus 로고
    • A selfsuffi cient cytochrome P450 with a primary structural organization that includes a fl avin domain and a [2Fe-2S] center
    • Roberts, G.A., Celik, A., Hunter, D.J., Ost, T.W., White, J.H., Chapman, S.K., Turner, N.J., Flitsch, S.L. A selfsuffi cient cytochrome P450 with a primary structural organization that includes a fl avin domain and a [2Fe-2S] center. J Biol Chem 2003, 278, 48914-48920.
    • (2003) J Biol Chem , vol.278 , pp. 48914-48920
    • Roberts, G.A.1    Celik, A.2    Hunter, D.J.3    Ost, T.W.4    White, J.H.5    Chapman, S.K.6    Turner, N.J.7    Flitsch, S.L.8
  • 98
    • 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., Behki, R. Characterization of the expression of the thcB gene, coding for a pesticide-degrading cytochrome P-450 in Rhodococcus strains. Appl Environ Microbiol 1996, 62, 403-407.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 403-407
    • Shao, Z.Q.1    Behki, R.2
  • 99
    • 0037245378 scopus 로고    scopus 로고
    • Expression, purifi cation and characterisation of a Bacillus subtilis ferredoxin: a potential electron transfer donor to cytochrome P450 BioI
    • Green, A.J., Munro. A.W., Cheesman, M.R., Reid, G.A., Von Wachenfeldt, C., Chapman, S.K. Expression, purifi cation and characterisation of a Bacillus subtilis ferredoxin: a potential electron transfer donor to cytochrome P450 BioI. J Inorg Biochem 2003, 93, 92-99.
    • (2003) J Inorg Biochem , vol.93 , pp. 92-99
    • Green, A.J.1    Munro, A.W.2    Cheesman, M.R.3    Reid, G.A.4    Von Wachenfeldt, C.5    Chapman, S.K.6
  • 100
    • 0034846763 scopus 로고    scopus 로고
    • Expression, purifi cation and characterization of cytochrome P450 Biol: a novel P450 involved in biotin synthesis in Bacillus subtilis
    • Green, A.J., Rivers, S.L., Cheesman, M., Reid, G.A., Quaroni, L.G., Macdonald, I.D., Chapman, S.K., Munro, A.W. Expression, purifi cation and characterization of cytochrome P450 Biol: a novel P450 involved in biotin synthesis in Bacillus subtilis. J Biol Inorg Chem 2001, 6, 523-533.
    • (2001) J Biol Inorg Chem , vol.6 , pp. 523-533
    • Green, A.J.1    Rivers, S.L.2    Cheesman, M.3    Reid, G.A.4    Quaroni, L.G.5    Macdonald, I.D.6    Chapman, S.K.7    Munro, A.W.8
  • 101
    • 0033529797 scopus 로고    scopus 로고
    • Characterization and catalytic properties of the sterol 14α-demethylase from Mycobacterium tuberculosis
    • USA
    • Bellamine, A., Mangla, A.T., Nes, W.D., Waterman, M.R. Characterization and catalytic properties of the sterol 14α-demethylase from Mycobacterium tuberculosis. Proc Natl Acad Sci USA 1999, 96, 8937-8942.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 8937-8942
    • Bellamine, A.1    Mangla, A.T.2    Nes, W.D.3    Waterman, M.R.4
  • 102
    • 33745832316 scopus 로고    scopus 로고
    • Characterization of the Mycobacterium tuberculosis ferredoxin (Fdx) and interactions with its cognate redox partner: the sterol demethylase P450 CYP51
    • McLean, K.J., Warman, A.J., Seward, H.E, Marshall, K.R., Cheesman, M.R., Waterman, M.R., Munro, A.W. Characterization of the Mycobacterium tuberculosis ferredoxin (Fdx) and interactions with its cognate redox partner: the sterol demethylase P450 CYP51, Biochemistry 2006, 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    Cheesman, M.R.5    Waterman, M.R.6    Munro, A.W.7
  • 103
    • 33646052947 scopus 로고    scopus 로고
    • Flavodoxins: sequence, folding, binding, function and beyond
    • Sancho, J. Flavodoxins: sequence, folding, binding, function and beyond. Cell Mol Life Sci 2006, 63, 855-864.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 855-864
    • Sancho, J.1
  • 104
    • 0033047656 scopus 로고    scopus 로고
    • Flavodoxin as a model for the P450-interacting domain of NADPH cytochrome P450 reductase
    • Jenkins, C.M., Waterman, M.R. Flavodoxin as a model for the P450-interacting domain of NADPH cytochrome P450 reductase. Drug Metab Rev 1999, 31, 195-203.
    • (1999) Drug Metab Rev , vol.31 , pp. 195-203
    • Jenkins, C.M.1    Waterman, M.R.2
  • 105
    • 0032211496 scopus 로고    scopus 로고
    • Characterisation of fl avodoxin NADP+ oxidoreductase and fl avodoxin; key components of electron transfer in Escherichia coli
    • McIver, L., Leadbeater, C., Campopiano, D.J., Baxter, R.L., Daff, S.N., Chapman, S.K., Munro, A.W. Characterisation of fl avodoxin NADP+ oxidoreductase and fl avodoxin; key components of electron transfer in Escherichia coli. Eur J Biochem 1998, 257, 577-585.
    • (1998) Eur J Biochem , vol.257 , pp. 577-585
    • McIver, L.1    Leadbeater, C.2    Campopiano, D.J.3    Baxter, R.L.4    Daff, S.N.5    Chapman, S.K.6    Munro, A.W.7
  • 106
    • 4744337841 scopus 로고    scopus 로고
    • Expression and characterization of the two fl avodoxin proteins of Bacillus subtilis, YkuN and YkuP: Biophysical properties and interactions with cytochrome P450 BioI
    • Lawson, R.J., Von Wachenfeldt, C., Haq, I., Perkins, J., Munro, A.W. Expression and characterization of the two fl avodoxin proteins of Bacillus subtilis, YkuN and YkuP: Biophysical properties and interactions with cytochrome P450 BioI. Biochemistry 2004, 43, 12390-12409.
    • (2004) Biochemistry , vol.43 , pp. 12390-12409
    • Lawson, R.J.1    Von Wachenfeldt, C.2    Haq, I.3    Perkins, J.4    Munro, A.W.5
  • 108
    • 0028104977 scopus 로고
    • Flavodoxin and NADPH-fl avodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities
    • Jenkins, C.M., Waterman, M.R. Flavodoxin and NADPH-fl avodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities. J Biol Chem 1994, 269, 27401-27408.
    • (1994) J Biol Chem , vol.269 , pp. 27401-27408
    • Jenkins, C.M.1    Waterman, M.R.2
  • 110
    • 33646806119 scopus 로고    scopus 로고
    • Selective hydroxylation of highly branched fatty acids and their derivatives by CYP102A1 from Bacillus megaterium
    • Budde, M., Morr, M., Schmid, R.D., Urlacher, V.B. Selective hydroxylation of highly branched fatty acids and their derivatives by CYP102A1 from Bacillus megaterium. ChemBiochem 2006, 7, 789-794.
    • (2006) ChemBiochem , vol.7 , pp. 789-794
    • Budde, M.1    Morr, M.2    Schmid, R.D.3    Urlacher, V.B.4
  • 111
    • 11844256914 scopus 로고    scopus 로고
    • Biotransformation of the sesquiterpene (C)-valencene by cytochrome P450cam and P450BM-3
    • Sowden, R.J., Yasmin, S, Rees, N.H., Bell, S.G and Wong, L.L. Biotransformation of the sesquiterpene (C)-valencene by cytochrome P450cam and P450BM-3. Org Biomol Chem 2005, 3, 57-64.
    • (2005) Org Biomol Chem , vol.3 , pp. 57-64
    • Sowden, R.J.1    Yasmin, S.2    Rees, N.H.3    Bell, S.G.4    Wong, L.L.5
  • 112
    • 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
    • Jackson, C.J., Lamb, D.C., Marczylo, T.M., Warrilow, A.J.S., Manning, N.J., Lowe, D.J., Kelly, D.E., Kelly, S.L. A novel sterol 14α-demethylase/ ferredoxin fusion protein (McCYP51FX) from Methylococcus capsulatus represents a new class of the cytochrome P450 superfamily. J Biol Chem 2002, 277, 46959-46965.
    • (2002) J Biol Chem , vol.277 , pp. 46959-46965
    • Jackson, C.J.1    Lamb, D.C.2    Marczylo, T.M.3    Warrilow, A.J.S.4    Manning, N.J.5    Lowe, D.J.6    Kelly, D.E.7    Kelly, S.L.8
  • 114
    • 4344566972 scopus 로고    scopus 로고
    • Update on mechanism and catalytic regulation in the NO synthases
    • Stuehr, D.J., Santolini, J., Wang, Z.Q., Wei, C.C., Adak, S. Update on mechanism and catalytic regulation in the NO synthases. J Biol Chem 2004, 279, 36167-36170.
    • (2004) J Biol Chem , vol.279 , pp. 36167-36170
    • Stuehr, D.J.1    Santolini, J.2    Wang, Z.Q.3    Wei, C.C.4    Adak, S.5
  • 115
    • 0032563106 scopus 로고    scopus 로고
    • Domain swapping in inducible nitricoxide synthase. Electron transfer occurs between fl avin and heme groups located on adjacent subunits in the dimer
    • Siddhanta, U., Presta, A., Fan, B., Wolan, D., Rousseau, D.L., Stuehr, D.J. Domain swapping in inducible nitricoxide synthase. Electron transfer occurs between fl avin and heme groups located on adjacent subunits in the dimer. J Biol Chem 1998, 273, 18950-18958.
    • (1998) J Biol Chem , vol.273 , pp. 18950-18958
    • Siddhanta, U.1    Presta, A.2    Fan, B.3    Wolan, D.4    Rousseau, D.L.5    Stuehr, D.J.6
  • 117
    • 0026485793 scopus 로고
    • High-level expression in Escherichia coli of enzymatically active fusion proteins containing the domains of mammalian cytochromes P450 and NADPH-P450 reductase fl avoprotein
    • USA
    • Fisher, C.W., Shet, M.S., Caudle, D.L., Martin-Wixtrom, C.A., Estabrook, R.W. High-level expression in Escherichia coli of enzymatically active fusion proteins containing the domains of mammalian cytochromes P450 and NADPH-P450 reductase fl avoprotein. Proc Natl Acad Sci USA 1992, 89, 10817-10821.
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 10817-10821
    • Fisher, C.W.1    Shet, M.S.2    Caudle, D.L.3    Martin-Wixtrom, C.A.4    Estabrook, R.W.5
  • 118
    • 0027146638 scopus 로고
    • Human cytochrome P450 3A4: enzymatic properties of a purifi ed recombinant fusion protein containing NADPH-P450 reductase
    • USA
    • Shet, M.S., Fisher, C.W., Holmans, P.L., Estabrook, R.W. Human cytochrome P450 3A4: enzymatic properties of a purifi ed recombinant fusion protein containing NADPH-P450 reductase. Proc Natl Acad Sci USA 1993, 90, 11748-11752.
    • (1993) Proc Natl Acad Sci , vol.90 , pp. 11748-11752
    • Shet, M.S.1    Fisher, C.W.2    Holmans, P.L.3    Estabrook, R.W.4
  • 119
    • 0029809775 scopus 로고    scopus 로고
    • Putidaredoxin reductase-putidaredoxin-cytochrome P450cam triple fusion protein
    • Sibbesen, O., de Voss, J.J., Ortiz de Montellano, P.R. Putidaredoxin reductase-putidaredoxin-cytochrome P450cam triple fusion protein. J Biol Chem 1996, 271, 22462-22469.
    • (1996) J Biol Chem , vol.271 , pp. 22462-22469
    • Sibbesen, O.1    de Voss, J.J.2    Ortiz De Montellano, P.R.3
  • 120
    • 84892305135 scopus 로고    scopus 로고
    • Activation of molecular oxygen by cytochrome P450
    • In: Ortiz de Montellano, P.R. (ed.), 3rd edn. New York: Kluwer Academic/ Plenum Press
    • Makris, T.M., Denisov, I., Schlichting, I., Sligar, S.G. Activation of molecular oxygen by cytochrome P450. In: Ortiz de Montellano, P.R. (ed.) Cytochrome P450: Structure, Mechanism and Biochemistry, 3rd edn. New York: Kluwer Academic/ Plenum Press, 2005, pp. 149-182.
    • (2005) Cytochrome P450: Structure, Mechanism and Biochemistry , pp. 149-182
    • Makris, T.M.1    Denisov, I.2    Schlichting, I.3    Sligar, S.G.4
  • 121
    • 0042522511 scopus 로고    scopus 로고
    • Global incorporation of norleucine in place of methionine in cytochrome P450 BM-3 heme domain increases peroxygenase activity
    • Cirino, P.C., Tang, Y., Takahashi, K., Tirrell, D.A., Arnold, F.H. Global incorporation of norleucine in place of methionine in cytochrome P450 BM-3 heme domain increases peroxygenase activity. Biotechnol Bioeng 2003, 83, 729-734.
    • (2003) Biotechnol Bioeng , vol.83 , pp. 729-734
    • Cirino, P.C.1    Tang, Y.2    Takahashi, K.3    Tirrell, D.A.4    Arnold, F.H.5
  • 122
    • 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., Shiro, Y. Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies. J Biol Chem 2003, 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
  • 123
    • 0033858391 scopus 로고    scopus 로고
    • Unique heme environment at the putative distal region of hydrogen peroxide-dependent fatty acid alpha-hydroxylase from Sphingomonas paucimobilis (peroxygenase P450SPα
    • Imai, Y., Matsunaga, I., Kusunose, E., Ichihara, K. Unique heme environment at the putative distal region of hydrogen peroxide-dependent fatty acid alpha-hydroxylase from Sphingomonas paucimobilis (peroxygenase P450SPα. J Biochem 2000, 128, 189-194.
    • (2000) J Biochem , vol.128 , pp. 189-194
    • Imai, Y.1    Matsunaga, I.2    Kusunose, E.3    Ichihara, K.4
  • 124
    • 0028979829 scopus 로고
    • Electrocatalytically driven omegahydroxylation of fatty acids using cytochrome P450 4A1
    • USA
    • Faulkner, K.M., Shet, M.S., Fisher, C.W., Estabrook, R.W. Electrocatalytically driven omegahydroxylation of fatty acids using cytochrome P450 4A1. Proc Natl Acad Sci USA 1995, 92, 7705-7709.
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 7705-7709
    • Faulkner, K.M.1    Shet, M.S.2    Fisher, C.W.3    Estabrook, R.W.4
  • 125
    • 1942489353 scopus 로고    scopus 로고
    • Direct electrochemistry of immobilized human cytochrome P450 2E1
    • Fantuzzi, A., Fairhead, M., Gilardi, G. Direct electrochemistry of immobilized human cytochrome P450 2E1. J Am Chem Soc 2004, 126, 5040-5041.
    • (2004) J Am Chem Soc , vol.126 , pp. 5040-5041
    • Fantuzzi, A.1    Fairhead, M.2    Gilardi, G.3
  • 127
    • 23844434591 scopus 로고    scopus 로고
    • Switching pyridine nucleotide specifi city in P450 BM3: mechanistic analysis of the W1046H and W1046A enzymes
    • Neeli, R., Roitel, O., Scrutton, N.S., Munro, A.W. Switching pyridine nucleotide specifi city in P450 BM3: mechanistic analysis of the W1046H and W1046A enzymes. J Biol Chem 2005, 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
  • 128
    • 10444284194 scopus 로고    scopus 로고
    • Nitric oxide reductase (P450nor) from Fusarium oxysporum
    • Daiber, A., Shoun, H., Ullrich, V. Nitric oxide reductase (P450nor) from Fusarium oxysporum. J Inorg Biochem 2005, 99, 185-193.
    • (2005) J Inorg Biochem , vol.99 , pp. 185-193
    • Daiber, A.1    Shoun, H.2    Ullrich, V.3
  • 129
    • 4143049187 scopus 로고    scopus 로고
    • Structural evidence for direct hydride transfer from NADH to cytochrome P450nor
    • Oshima, R., Fushinobu, S., Su, F., Zhang, L., Takaya, N., Shoun, H. Structural evidence for direct hydride transfer from NADH to cytochrome P450nor. J Mol Biol 2004, 342, 207-217.
    • (2004) J Mol Biol , vol.342 , pp. 207-217
    • Oshima, R.1    Fushinobu, S.2    Su, F.3    Zhang, L.4    Takaya, N.5    Shoun, H.6
  • 130
    • 0034079862 scopus 로고    scopus 로고
    • Free radicals and antioxidants in the year 2000. A historical look to the future
    • Gutteridge, J.M., Halliwell, B. Free radicals and antioxidants in the year 2000. A historical look to the future. Ann N Y Acad Sci 2000, 899, 136-147.
    • (2000) Ann N Y Acad Sci , vol.899 , pp. 136-147
    • Gutteridge, J.M.1    Halliwell, B.2
  • 131
    • 14744296960 scopus 로고    scopus 로고
    • The infl uence of substrate on the spectral properties of oxyferrous wild-type and T252A cytochrome P450-CAM
    • Sono, M., Perera, R., Jin, S., Makris, T.M., Sligar, S.G., Bryson, T.A., Dawson, J.H. The infl uence of substrate on the spectral properties of oxyferrous wild-type and T252A cytochrome P450-CAM. Arch Biochem Biophys 2005, 436, 40-49.
    • (2005) Arch Biochem Biophys , vol.436 , pp. 40-49
    • Sono, M.1    Perera, R.2    Jin, S.3    Makris, T.M.4    Sligar, S.G.5    Bryson, T.A.6    Dawson, J.H.7
  • 132
    • 33645990311 scopus 로고    scopus 로고
    • A literature review of enzyme kinetic parameters for CYP3A4-mediated metabolic reactions of 113 drugs in human liver microsomes: structure-kinetics relationship assessment
    • Bu, H.Z. A literature review of enzyme kinetic parameters for CYP3A4-mediated metabolic reactions of 113 drugs in human liver microsomes: structure-kinetics relationship assessment. Curr Drug Metab 2006, 7, 231-249.
    • (2006) Curr Drug Metab , vol.7 , pp. 231-249
    • Bu, H.Z.1
  • 133
    • 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., Ortiz de Montellano, P.R. 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 2002, 124, 12682-12683.
    • (2002) J Am Chem Soc , vol.124 , pp. 12682-12683
    • Puchkaev, A.V.1    Wakagi, T.2    Ortiz De Montellano, P.R.3
  • 134
  • 135
    • 21244475208 scopus 로고    scopus 로고
    • The heme monooxygenase cytochrome P450cam can be engineered to oxidize ethane to ethanol
    • Xu, F., Bell, S.G., Lednik, J., Insley, A., Rao, Z., Wong, L.L. The heme monooxygenase cytochrome P450cam can be engineered to oxidize ethane to ethanol. Angew Chem Int Ed 2005, 44, 4029-4032.
    • (2005) Angew Chem Int Ed , vol.44 , pp. 4029-4032
    • Xu, F.1    Bell, S.G.2    Lednik, J.3    Insley, A.4    Rao, Z.5    Wong, L.L.6
  • 136
    • 32544436092 scopus 로고    scopus 로고
    • Preparation of human metabolites of propranolol using laboratory-evolved bacterial cytochromes P450
    • Otey, C.R., Bandara, G., Lalonde, J., Takahashi, K., Arnold, F.H. Preparation of human metabolites of propranolol using laboratory-evolved bacterial cytochromes P450. Biotechnol Bioeng 2006, 93, 494-499.
    • (2006) Biotechnol Bioeng , vol.93 , pp. 494-499
    • Otey, C.R.1    Bandara, G.2    Lalonde, J.3    Takahashi, K.4    Arnold, F.H.5
  • 137
    • 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., Dawson, J.H. 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 USA 2003, 100, 3641-3646.
    • (2003) Proc Natl Acad Sci USA , 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
  • 138
    • 8744241642 scopus 로고    scopus 로고
    • EpoK, a cytochrome P450 involved in biosynthesis of the anticancer agents epothilones A and B. Substrate-mediated rescue of a P450 enzyme
    • Ogura, H., Nishida, C.R., Hoch, U.R., Perera, R., Dawson, J.H., Ortiz de Montellano, P.R. EpoK, a cytochrome P450 involved in biosynthesis of the anticancer agents epothilones A and B. Substrate-mediated rescue of a P450 enzyme. Biochemistry 2004, 43, 14712-14721.
    • (2004) Biochemistry , vol.43 , pp. 14712-14721
    • Ogura, H.1    Nishida, C.R.2    Hoch, U.R.3    Perera, R.4    Dawson, J.H.5    Ortiz De Montellano, P.R.6
  • 139
    • 0037066698 scopus 로고    scopus 로고
    • Autocatalytic mechanism and consequences of covalent heme attachment in the cytochrome P4504A family
    • LeBrun, L.A., Hoch, U., Ortiz de Montellano, P.R. Autocatalytic mechanism and consequences of covalent heme attachment in the cytochrome P4504A family. J Biol Chem 2002, 277, 12755-12761.
    • (2002) J Biol Chem , vol.277 , pp. 12755-12761
    • LeBrun, L.A.1    Hoch, U.2    Ortiz De Montellano, P.R.3
  • 141
    • 14844354133 scopus 로고    scopus 로고
    • The P450cam G248E mutant covalently binds its prosthetic heme group
    • Limburg, J., LeBrun, L.A., Ortiz de Montellano, P.R. The P450cam G248E mutant covalently binds its prosthetic heme group. Biochemistry 2005, 44, 4091-4099.
    • (2005) Biochemistry , vol.44 , pp. 4091-4099
    • Limburg, J.1    LeBrun, L.A.2    Ortiz De Montellano, P.R.3
  • 142
    • 0027522735 scopus 로고
    • Critical residues involved in FMN binding and catalytic activity in cytochrome P450BM-3
    • Klein, M.L., Fulco, A.J. Critical residues involved in FMN binding and catalytic activity in cytochrome P450BM-3. J Biol Chem 1993, 268, 7553-7561.
    • (1993) J Biol Chem , vol.268 , pp. 7553-7561
    • Klein, M.L.1    Fulco, A.J.2
  • 143
    • 0030570979 scopus 로고    scopus 로고
    • Analysis of the structural stability of the multidomain enzyme fl avocytochrome P-450 BM3
    • Munro, A.W., Lindsay, J.G., Coggins, J.R., Kelly, S.M., Price, N.C. Analysis of the structural stability of the multidomain enzyme fl avocytochrome P-450 BM3. Biochim Biophys Acta 1996, 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
  • 144
    • 0141460411 scopus 로고    scopus 로고
    • Thermostabilization of a cytochrome P450 peroxygenase
    • Salazar, O., Cirino, P.C., Arnold, F.H. Thermostabilization of a cytochrome P450 peroxygenase. ChemBiochem 2003, 4, 891-893.
    • (2003) ChemBiochem , vol.4 , pp. 891-893
    • Salazar, O.1    Cirino, P.C.2    Arnold, F.H.3
  • 145
    • 0035100923 scopus 로고    scopus 로고
    • Understanding thermostability in cytochrome P450 by combinatorial mutagenesis
    • Maves, S.A., Sligar, S.G. Understanding thermostability in cytochrome P450 by combinatorial mutagenesis. Protein Sci 2001, 10, 161-168.
    • (2001) Protein Sci , vol.10 , pp. 161-168
    • Maves, S.A.1    Sligar, S.G.2
  • 146
    • 0042573727 scopus 로고    scopus 로고
    • Structure of mammalian cytochrome P450 2C5 complexed with diclofenac at 2.1 Å resolution: evidence for an induced fi t model of substrate binding
    • Wester, M.R., Johnson, E.F., Marques-Soares, C., Dijols, S., Dansette, P.M., Mansuy, D., Stout, C.D. Structure of mammalian cytochrome P450 2C5 complexed with diclofenac at 2.1 Å resolution: evidence for an induced fi t model of substrate binding. Biochemistry 2003, 42, 9335-9345.
    • (2003) Biochemistry , vol.42 , pp. 9335-9345
    • Wester, M.R.1    Johnson, E.F.2    Marques-Soares, C.3    Dijols, S.4    Dansette, P.M.5    Mansuy, D.6    Stout, C.D.7
  • 147
    • 0033571213 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase: role of the N-terminal betahairpin hook and pterin-binding segment in dimerization and tetrahydrobiopterin interaction
    • Ghosh, D.K., Crane, B.R., Ghosh, S., Wolan, D., Gachhui, R., Crooks, C., Presta, A., Tainer, J.A., Getzoff, E.D., Stuehr, D.J. Inducible nitric oxide synthase: role of the N-terminal betahairpin hook and pterin-binding segment in dimerization and tetrahydrobiopterin interaction. EMBO J 1999, 18, 6260-6270.
    • (1999) EMBO J , vol.18 , pp. 6260-6270
    • Ghosh, D.K.1    Crane, B.R.2    Ghosh, S.3    Wolan, D.4    Gachhui, R.5    Crooks, C.6    Presta, A.7    Tainer, J.A.8    Getzoff, E.D.9    Stuehr, D.J.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.