Selected references on P450_BM-3

Last modified: Thu Apr 15 13:26:20 BST 2004

• Bec, N., Anzenbacher, P., Anzenbacherova, E., Gorren, A.C.F., Munro, A.W. and Lange, R. (1999) Spectral properties of the oxyferrous complex of the heme domain of cytochrome P450 BM-3 (CYP102). Biochem. Biophys. Res. Commun. 266, 187-189.
• Besse, P., Modi, S., Boyle, J.M., Roberts, G.C.K. and Primrose, W.U. (1997) Redox cycling by cytochrome P-450. Biochem. Soc. Trans. 25, S579.
• Black, S.D. (1994) On the domain structure of cytochrome P450 102 (BM-3): Isolation and properties of a 45-kDa FAD/NADP domain. Biochem. Biophys. Res. Commun. 203, 162-168.
• Black, S.D. and Martin, S.T. (1994) Evidence for conformational dynamics and molecular aggregation in cytochrome P450 102 (BM-3). Biochemistry 33, 12056-12062.
• Black, S.D., Linger, M.H., Freck, L.C., Kazemi, S. and Galbraith, J.A. (1994) Affinity isolation and characterization of cytochrome P450 102 (BM-3) from barbiturate-induced Bacillus megaterium. Arch. Biochem. Biophys. 310, 126-133.
• Boddupalli, S.S., Estabrook, R.W. and Peterson, J.A. (1990) Fatty acid monooxygenation by cytochrome P-450BM-3. J. Biol. Chem. 265, 4233-4239.
• Boddupalli, S.S., Pramanik, B.C., Slaughter, C.A., Estabrook, R.W. and Peterson, J.A. (1992a) Fatty acid monooxygenation by P450BM-3: product identification and proposed mechanisms for the sequential hydroxylation reactions. Arch. Biochem. Biophys. 292, 20-28.
• Boddupalli, S.S., Oster, T., Estabrook, R.W. and Peterson, J.A. (1992b) Reconstitution of the fatty acid hydroxylation function of cytochrome P-450_BM-3 utilizing its individual recombinant hemo- and flavoprotein domains. J. Biol. Chem. 267, 10375-10380.
• Boddupalli, S.S., Hasemann, C.A., Ravichandran, K.G., Lu, J.Y., Goldsmith, E.J., Deisenhofer, J. and Peterson, J.A. (1992c) Crystallization and preliminary X-ray diffraction analysis of P450terp and the hemoprotein domain of P450_BM-3, enzymes belonging to two distinct classes of the cytochrome P450 superfamily. Proc. Natl. Acad. Sci. USA 89, 5567-5571.
• Capdevila, J.H., Wei, S., Helvig, C., Falck, J.R., Belosludtsev, Y., Truan, G., Graham-Lorence, S.E. and Peterson, J.A. (1996) The highly stereoselective oxidation of polyunsaturated fatty acids by cytochrome P450BM-3. J. Biol. Chem. 271, 22663-22671.
• Carmichael, A.B. and Wong, L.-L. (2001) Protein engineering of Bacillus megaterium CYP102. The oxidation of polycyclic aromatic hydrocarbons. Eur. J. Biochem. 268, 3117-3125.
• Chapman, S.K., Welsh, F., Moysey, R., Mowat, C., Doherty, M.K., Turner, K.L., Munro, A.W. and Reid, G.A. (1999) Flavocytochromes: transceivers and relays in biological electron transfer. Biochem. Soc. Trans. 27, 185-189.
• Chen, J.-K., Wang, D.-W., Falck, J.R., Capdevila, J. and Harris, R.C. (1999) Transfection of an active cytochrome P450 arachidonic acid epoxygenase indicates that 14,15-epoxyeicosatrienoic acid functions as an intracellular second messenger in response to epidermal growth factor. J. Biol. Chem. 274, 4764-4769.
• 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.
• Daiber, A., Herold, S., Schöneich, C., Namgaladze, D., Peterson, J.A. and Ullrich, V. (2000) Nitration and inactivation of cytochrome P450_BM-3 by peroxynitrite: Stopped-flow measurements prove ferryl intermediates. Eur. J. Biochem. 267, 6729-6739.
• Darwish, K., Li, H. and Poulos, T.L. (1991) Engineering proteins, subcloning and hyperexpressing oxidoreductase genes. Protein Engineering 4, 701-708 [published erratum Protein Engineering 4, 851 (1991)].
• Davis, S.C., Sui, Z., Peterson, J.A. and Ortiz de Montellano, P.R. (1996) Oxidation of -oxo fatty acids by cytochrome P450_BM-3 (CYP102). Arch. Biochem. Biophys. 328, 35-42.
• Davydov, D.R., Hui Bon Hoa, G. and Peterson, J.A. (1999) Dynamics of protein­bound water in the heme domain of P450BM3 studied by high­pressure spectroscopy: Comparison with P450cam and P450 2B4. Biochemistry 38, 751-761.
• Davydov, D.R., Kariakin, A.A., Petushkova, N.A. and Peterson, J.A. (2000) Association of cytochromes P450 with their reductases: Opposite sign of the electrostatic interactions in P450BM-3 as compared with the microsomal 2B4 system. Biochemistry 39, 6489-6497.
• Deng, T.­j., Proniewicz, L.M., Kincaid, J.R., Yeom, H., Macdonald, I.D.G. and Sligar, S.G. (1999) Resonance Raman studies of cytochrome P450BM3 and its complexes with exogenous ligands. Biochemistry 38, 13699-13706.
• English, N.T. and Rankin, L.C. (1997) Antioxidant-mediated attenuation of the induction of cytochrome P450BM-3 (CYP102) by ibuprofen in Bacillus megaterium ATCC 14581. Biochem. Pharmacol. 54, 443-450.
• English, N.T., Hughes, V. and Wolf, C.R. (1996) Induction of cytochrome P-450_BM-3 (CYP 102) by non-steroidal anti-inflammatory drugs in Bacillus megaterium. Biochem. J. 316, 279-283.
• English, N.T., Palmer, C.N.A., Alworth, W.L., Kang, L., Hughes, V. and Wolf, C.R. (1997) Fatty acid signals in Bacillus megaterium are attenuated by cytochrome P-450-mediated hydroxylation. Biochem. J. 327, 363-368.
• Fang, X. and Halpert, J.R. (1996) Dithionite-supported hydroxylation of palmitic acid by cytochrome P450BM-3. Drug Metab. Dispos. 24, 1282-1285.
• Fulco, A.J. (1991) P450_BM-3 and other inducible bacterial P450 cytochromes: biochemistry and regulation. Annu. Rev. Pharmacol. Toxicol. 31, 177-203.
• Gonvindaraj, S., Li, H. and Poulos, T.L. (1994) Flavin supported fatty acid oxidation by the heme domain of Bacillus megaterium cytochrome P450_BM-3. Biochem. Biophys. Res. Commun. 203, 1745-1749.
• Gonvindaraj, S. and Poulos, T.L. (1995) Role of the linker region connecting the reductase and heme domains in cytochrome P450_BM-3. Biochemistry 34, 11221-11226.
• Gonvindaraj, S. and Poulos, T.L. (1996) Probing the structure of the linker connecting the reductase and heme domains of cytochrome P450_BM-3 using site-directed mutagenesis. Protein Science 5, 1389-1393.
• Gonvindaraj, S. and Poulos, T.L. (1997) The domain architecture of cytochrome P450_BM-3. J. Biol. Chem. 272, 7915-7921.
• Graham-Lorence, S., Truan, G., Peterson, J.A., Falck, J.R., Wei, S., Helvig, C. and Capdevila, J.H. (1997) An active site substitution, F87V, converts cytochrome P450 BM-3 into a regio- and stereoselective (14S,15R)-arachidonic acid epoxygenase. J. Biol. Chem. 272, 1127-1135.
• Haines, D.C., Sevrioukova, I.F. and Peterson, J.A. (2000) The FMN-binding domain of cytochrome P450BM-3: resolution, reconstitution, and flavin analogue substitution. Biochemistry 39, 9419-9429.
• Hazzard, J.T., Gonvindaraj, S., Poulos, T.L. and Tollin, G. (1997) Electron transfer between the FMN and heme domains of cytochrome P450_BM-3. Effects of substrate and CO. J. Biol. Chem. 272, 7922-7926.
• Hudecek, J., Baumruk, V., Anzenbacher, P. and Munro, A.W. (1998) Catalytically self­sufficient P450 CYP102 (cytochrome P450 BM­3): resonance Raman spectral characterization of the heme domain and of the holoenzyme. Biochem. Biophys. Res. Commun. 243, 811-815.
• Khan, K.K., Mazumdar, S., Modi, S., Sutcliffe, M.J., Roberts, G.C.K. and Mitra, S. (1997) Steady-state and picosecond-time-resolved fluorescence studies on the recombinant heme domain of Bacillus megaterium cytochrome P-450. Eur. J. Biochem. 244, 361-370.
• Klein, M.L. and Fulco, A.J. (1993) Critical residues involved in FMN binding and catalytic activity in cytochrome P450_BM-3. J. Biol. Chem. 268, 7553-7561.
• Li, H. and Poulos, T.L. (1996) Conformational dynamics in cytochrome P450-substrate interactions. Biochimie 78, 695-699.
• Li, H. and Poulos, T.L. (1997) The structure of the cytochrome P450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid. Nature Struct. Biol. 4, 140-146.
• Li, H. and Poulos, T.L. (1999) Fatty acid metabolism, conformational change, and electron transfer in cytochrome P-450_BM-3. Biochim. Biophys. Acta 1441, 141-149.
• Li, H., Darwish, K. and Poulos, T.L. (1991) Characterization of recombinant Bacillus megaterium cytochrome P-450_BM-3 and its two functional domains. J. Biol. Chem. 266, 11909-11914.
• Li, Q.-S., Schwaneberg, U., Fischer, P. and Schmid, R.D. (2000) Directed evolution of the fatty-acid hydroxylase P450 BM-3 into an indole-hydroxylating catalyst. Chem. Eur. J. 6, 1531-1536.
• Macdonald, I.D.G., Smith, W.E. and Munro, A.W. (1996) Inhibitor/fatty acid interactions with cytochrome P-450 BM3. FEBS Lett. 396, 196-200.
• Macdonald, I.D.G., Munro, A.W. and Smith, W.E. (1998) Fatty acid-induced alteration of the porphyrin macrocycle of cytochrome P450 BM3. Biophys. J. 74, 3241-3249.
• McLean, M.A., Yeom, H. and Sligar, S.G. (1996) Carbon monoxide binding to cytochrome P450_BM-3: Evidence for a substrate-dependent conformational change. Biochimie 78, 700-705.
• Maves, S.A., Yeom, H., McLean, M.A. and Sligar, S.G. (1997) Decreased substrate affinity upon alteration of the substrate-docking region in cytochrome P450_BM-3. FEBS Lett. 414, 213-218.
• 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.
• Modi, S., Primrose, W.U., Boyle, J.M., Gibson, C.F., Lian, L.-Y. and Roberts, G.C.K. (1995a) NMR studies of substrate binding to cytochrome P450_BM-3: Comparisons to cytochrome P450cam. Biochemistry 34, 8982-8988.
• Modi, S., Primrose, W.U., Lian, L.-Y. and Roberts, G.C.K. (1995b) Effect of replacement of ferriprotoporphyrin IX in the haem domain of cytochrome P-450 BM-3 on substrate binding and catalytic activity. Biochem. J. 310, 939-943.
• Modi, S., Sutcliffe, M.J., Primrose, W.U., Lian, L.-Y. and Roberts, G.C.K. (1996) The catalytic mechanism of cytochrome P450 BM-3 involves a 6 Å movement of the bound substrate on reduction. Nature Struct. Biol. 3, 414-417.
• Munro, A.W. (1993) Purification schemes for the constituent domains of cytochrome P450 BM3 in E. coli. Biochem. Soc. Trans. 21, 316S.
• Munro, A.W., Malarkey, K. and Miles, J.S. (1993a) Investigating the function of cytochrome P450 BM-3: a role for the phylogenetically conserved tryptophan residue? Biochem. Soc. Trans. 21, 66S.
• Munro, A.W., Coggins, J.R. and Lindsay, J.G. (1993b) Regional saturation mutagenesis as an approach to identification of substrate specificity determinants in cytochrome P450 BM3. Biochem. Soc. Trans. 21, 409S.
• Munro, A.W., Coggins, J.R. and Lindsay, J.G. (1993c) A novel inhibitor of cytochrome P450 BM3. Biochem. Soc. Trans. 21, 411S.
• Munro, A.W., Lindsay, J.G. and Coggins, J.R. (1993d) Alkane metabolism by cytochrome P450 BM3. Biochem. Soc. Trans. 21, 412S.
• Munro, A.W., Lindsay, J.G., Coggins, J.R., Kelly, S.M. and Price, N.C. (1994a) Structural and enzymological analysis of the interaction of isolated domains of cytochrome P-450 BM3. FEBS Lett. 343, 70-74.
• Munro, A.W., Lindsay, J.G., Coggins, J.R., Macdonald, I.D.G., Smith, W.E. and Rospendowski, B.N. (1994b) Resonance Raman spectroscopic studies on intact cytochrome P450 BM3. Biochem. Soc. Trans. 22, 54S.
• Munro, A.W., Malarkey, K., McKnight, J., Thomson, A.J., Kelly, S.M., Price, N.C., Lindsay, J.G., Coggins, J.R. and Miles, J.S. (1994c) The role of tryptophan 97 of cytochrome P-450 BM3 from Bacillus megaterium in catalytic function. Evidence against the 'covalent switching' hypothesis of P-450 electron transfer. Biochem. J. 303, 423-428.
• Munro, A.W., Lindsay, J.G., Coggins, J.R., Kelly, S.M. and Price, N.C. (1995) NADPH oxidase activity of cytochrome P-450 BM3 and its constituent reductase domain. Biochim. Biophys. Acta 1231, 255-264.
• Munro, A.W., Coggins, J.R. and Lindsay, J.G. (1996a) Inhibition of flavin reoxidation in P450 BM3 by diphenyliodonium chloride. Biochem. Soc. Trans. 24, 17S.
• Munro, A.W., Coggins, J.R., Lindsay, J.G., Daff, S.N. and Chapman, S.K. (1996b) Formation of flavin semiquinone during the reduction of P450 BM3 reductase domain with NADPH. Biochem. Soc. Trans. 24, 18S.
• Munro, A.W., Coggins, J.R., Lindsay, J.G., Kelly, S.M. and Price, N.C. (1996c) Deflavination of cytochrome P450 BM3 by treatment with guanidinium chloride. Biochem. Soc. Trans. 24, 19S.
• Munro, A.W., Daff, S.N., Coggins, J.R., Lindsay, J.G. and Chapman, S.K. (1996d) Probing electron transfer in flavocytochrome P-450 BM3 and its component domains. Eur. J. Biochem. 239, 403-409.
• Munro, A.W., Lindsay, J.G., Coggins, J.R., Kelly, S.M. and Price, N.C. (1996e) Analysis of the structural stability of the multidomain enzyme flavocytochrome P-450 BM3. Biochim. Biophys. Acta 1296, 127-137.
• Munro, A.W., Daff, S.N., Turner, K.L. and Chapman, S.K. (1997a) Redox characterisation of flavocytochrome P-450 BM3 from Bacillus megaterium. Biochem. Soc. Trans. 25, S628.
• Munro, A.W., Daff, S.N., Turner, K.L. and Chapman, S.K. (1997b) Probing inter-domain electron transfer in a model flavocytochrome P-450. Biochem. Soc. Trans. 25, S629.
• Munro, A.W., Noble, M.A., Turner, K.L. and Chapman, S.K. (1998) The interaction of eukaryotic cytochrome b₅ with flavocytochrome P-450 BM3 from Bacillus megaterium. Biochem. Soc. Trans. 26, S212.
• Munro, A.W., Noble, M.A., Miles, C.S., Daff, S.N., Green, A.J., Quaroni, L., Rivers, S., Ost, T.W.B., Reid, G.A. and Chapman, S.K. (1999) Flavocytochrome P-450 BM3: a paradigm for the analysis of electron transfer and its control in the P-450s. Biochem. Soc. Trans. 27, 190-196.
• Munro, A.W., Noble, M.A., Ost, T.W.B., Green, A.J., McLean, K.J., Robledo, L., Miles, C.S., Murdoch, J. and Chapman, S.K. (2000) Flavocytochrome P450 BM3 substrate selectivity and electron transfer in a model cytochrome P450. Subcell. Biochem. 35, 297-315.
• Murataliev, M.B. and Feyereisen, R. (1996) Functional interactions in cytochrome P450BM3. Fatty acid substrate binding alters electron-transfer properties of the flavoprotein domain. Biochemistry 35, 15029-15037.
• Murataliev, M.B. and Feyereisen, R. (2000) Functional interactions in cytochrome P450_BM3. Evidence that NADP(H) binding controls redox potentials of the flavin cofactors. Biochemistry 39, 12699-12707.
• Murataliev, M.B., Klein, M., Fulco, A. and Feyereisen, R. (1997) Functional interactions in cytochrome P450BM3: flavin semiquinone intermediates, role of NADP(H), and mechanism of electron transfer by the flavoprotein domain. Biochemistry 36, 8401-8412.
• Narhi, L.O. and Fulco, A.J. (1987) Identification and characterization of two functional domains in cytochrome P-450_BM-3, a catalytically self-sufficient monooxygenase induced by barbiturates in Bacillus megaterium. J. Biol. Chem. 262, 6683-6690.
• Narhi, L.O., Wen, L.P. and Fulco, A.J. (1988) Characterization of the protein expressed in Escherichia coli by a recombinant plasmid containing the Bacillus megaterium cytochrome P-450_BM-3 gene. Mol. Cell Biochem. 79, 63-71.
• Noble, M.A., Turner, K.L., Chapman, S.K. and Munro, A.W. (1998a) Mechanistic probes of flavocytochrome P-450 BM3. Biochem. Soc. Trans. 26, S213.
• Noble, M.A., Quaroni, L., Chumanov, G.D., Turner, K.L., Chapman, S.K., Hanzlik, R.P. and Munro, A.W. (1998b) Imidazolyl carboxylic acids as mechanistic probes of flavocytochrome P-450 BM3. Biochemistry 37, 15799-15807.
• Noble, M.A., Miles, C.S., Chapman, S.K., Lysek, D.A., Mackay, A.C., Reid, G.A., Hanzlik, R.P. and Munro, A.W. (1999) Roles of key active-site residues in flavocytochrome P450 BM3. Biochem. J. 339, 371-379.
• Oliver, C.F., Modi, S., Sutcliffe, M.J., Primrose, W.U., Lian, L.-Y. and Roberts, G.C.K. (1997a) A single mutation in cytochrome P450 BM3 changes substrate orientation in a catalytic intermediate and the regiospecificity of hydroxylation. Biochemistry 36, 1567-1572.
• Oliver, C.F., Modi, S., Primrose, W.U., Lian, L.-Y. and Roberts, G.C.K. (1997b) Engineering the substrate specificity of Bacillus megaterium cytochrome P-450 BM3: hydroxylation of alkyl trimethylammonium compounds. Biochem. J. 327, 537-544.
• Ost, T.W.B., Miles, C.S., Murdoch, J., Cheung, Y., Reid, G.A., Chapman, S.K. and Munro, A.W. (2000) Rational re-design of the substrate binding site of flavocytochrome P450 BM3. FEBS Lett. 486, 173-177.
• Ost, T.W.B., Miles, C.S., Munro, A.W., Murdoch, J., Reid, G.A. and Chapman, S.K. (2001a) Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3. Biochemistry 40, 13421-13429.
• Ost, T.W.B., Munro, A.W., Mowat, C.G., Taylor, P.R., Pesseguiero, A., Fulco, A.J., Cho, A.K., Cheesman, M.A., Walkinshaw, M.D. and Chapman, S.K. (2001b) Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3. Biochemistry 40, 13430-13438.
• Palmer, C.N., Gustafsson, M.C., Dobson, H., von Wachenfeldt, C. and Wolf, C.R. (1999) Adaptive responses to fatty acids are mediated by the regulated expression of cytochromes P450. Biochem. Soc. Trans. 27, 374-378.
• Peterson, J.A. and Boddupalli, S.S. (1992) P450_BM-3: reduction by NADPH and sodium dithionite. Arch. Biochem. Biophys. 294, 654-661.
• Peterson, J.A., Sevrioukova, I., Truan, G. and Graham-Lorence, S.E. (1997) P450BM­3: A tale of two domains - or is it three? Steroids 62, 117-123.
• Poulos, T.L. (1996) Ligands and electrons and haem proteins. Nature Struct. Biol. 3, 401-403.
• Ravichandran, K.G., Boddupalli, S.S., Hasemann, C.A., Peterson, J.A. and Deisenhofer, J. (1993) Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's. Science 261, 731-736.
• Ruettinger, R.T., Wen, L.P. and Fulco, A.J. (1989) Coding nucleotide, 5´ regulatory, and deduced amino acid sequences of P-450_BM-3, a single peptide cytochrome P-450:NADPH-P-450 reductase from Bacillus megaterium. J. Biol. Chem. 264, 10987-10995.
• Schneider, S., Wubbolts, M.G., Sanglard, D. and Witholt, B. (1998) Biocatalyst engineering by assembly of fatty acid transport and oxidation activities for in vivo application of cytochrome P-450_BM-3 monooxygenase. Appl. Environ. Microbiol. 64, 3784-3790.
• Schwaneberg, U., Sprauer, A., Schmidt-Dannert, C. and Schmid, R.D. (1999a) P450 monooxygenase in biotechnology. I. Single-step, large-scale purification method for cytochrome P450 BM-3 by anion-exchange chromatography. J. Chromatogr. A 848, 149-159.
• Schwaneberg, U., Schmidt-Dannert, C., Schmitt, J. and Schmid, R.D. (1999b) A continuous spectrophotometric assay for P450 BM-3, a fatty acid hydroxylating enzyme, and its mutant F87A. Anal. Biochem. 269, 359-366.
• Sevrioukova, I.F. and Peterson, J.A. (1995) Reaction of carbon monoxide and molecular oxygen with P450terp (CYP108) and P450_BM-3 (CYP102). Arch. Biochem. Biophys. 317, 397-404.
• Sevrioukova, I.F. and Peterson, J.A. (1996) Domain-domain interaction in cytochrome P450BM-3. Biochimie 78, 744-751.
• Sevrioukova, I.F., Shaffer, C., Ballou, D.P. and Peterson, J.A. (1996a) Equilibrium and transient state spectrophotometric studies of the mechanism of reduction of the flavoprotein domain of P450BM-3. Biochemistry 35, 7058-7068.
• Sevrioukova, I.F., Truan, G. and Peterson, J.A. (1996b) The flavoprotein domain of P450BM-3: expression, purification, and properties of the flavin adenine dinucleotide- and flavin mononucleotide-binding subdomains. Biochemistry 35, 7528-7535.
• Sevrioukova, I.F., Truan, G. and Peterson, J.A. (1997) Reconstitution of the fatty acid hydroxylase activity of cytochrome P450BM-3 utilizing its functional domains. Arch. Biochem. Biophys. 340, 231-238.
• Sevrioukova, I.F., Li, H., Zhang, H., Peterson, J.A. and Poulos, T.L. (1999a) Structure of a cytochrome P450-redox partner electron-transfer complex. Proc. Natl. Acad. Sci. USA 96, 1863-1868.
• Sevrioukova, I.F., Hazzard, J.T., Tollin, G. and Poulos, T.L. (1999b) The FMN to heme electron transfer in cytochrome P450BM-3. Effect of chemical modification of cysteines engineered at the FMN-heme domain interaction site. J. Biol. Chem. 274, 36097-36106.
• Sharp, R.E. and Chapman, S.K. (1999) Mechanisms for regulating electron transfer in multi-centre redox proteins. Biochim. Biophys. Acta 1432, 143-158.
• Shirane, N., Sui, Z., Peterson, J.A. and Ortiz de Montellano, P.R. (1993) Cytochrome P450_BM-3 (CYP102): regiospecificity of oxidation of -unsaturated fatty acids and mechanism-based inactivation. Biochemistry 32, 13732-13741.
• Truan, G. and Peterson, J.A. (1998) Thr268 in substrate binding and catalysis in P450BM-3. Arch. Biochem. Biophys. 349, 53-64.
• Truan, G., Komandla, M.R., Falck, J.R. and Peterson, J.A. (1999) P450BM-3: absolute configuration of the primary metabolites of palmitic acid. Arch. Biochem. Biophys. 366, 192-198.
• Tuck, S.F., Peterson, J.A. and Ortiz de Montellano, P.R. (1992) Active site topologies of bacterial cytochromes P450101 (P450cam), P450108 (P450terp), and P450102 (P450_BM-3). In situ rearrangement of their phenyl-iron complexes. J. Biol. Chem. 267, 5614-5620.
• Yeom, H. and Sligar, S.G. (1997) Oxygen activation by cytochrome P450_BM-3: Effects of mutating an active site acidic residue. Arch. Biochem. Biophys. 337, 209-216.
• Yeom, H., Sligar, S.G., Li, H., Poulos, T.L. and Fulco, A.J. (1995) The role of Thr268 in oxygen activation of cytochrome P450_BM-3. Biochemistry 34, 14733-14740.

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