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Volumn 8, Issue 3, 1997, Pages 274-278

Engineering cytochrome P450s for bioremediation

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450 REDUCTASE; TOXIC SUBSTANCE;

EID: 0030918730     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(97)80003-1     Document Type: Article
Times cited : (64)

References (51)
  • 2
    • 0025307009 scopus 로고
    • Mechanisms of cytochrome P450 catalysis
    • Guengerich FP, Macdonald TL: Mechanisms of cytochrome P450 catalysis. FASEB J 1990, 4:2453-2459.
    • (1990) FASEB J , vol.4 , pp. 2453-2459
    • Guengerich, F.P.1    Macdonald, T.L.2
  • 3
    • 0029163161 scopus 로고
    • Cytochrome P450 proteins and potential utilization in biodegradation
    • Guengerich FP: Cytochrome P450 proteins and potential utilization in biodegradation. Environ Health Perspect 1995, 103:25-28.
    • (1995) Environ Health Perspect , vol.103 , pp. 25-28
    • Guengerich, F.P.1
  • 4
    • 0029077553 scopus 로고
    • A single cytochrome P-450 system is involved in degradation of the herbicides EPTC (S-ethyl dipropylthiocarbamate) and atrazine by Rhodococcus sp. strain NI86/21
    • Nagy I, Compernolle F, Ghys K, Vanderleyden J, De Mot R: A single cytochrome P-450 system is involved in degradation of the herbicides EPTC (S-ethyl dipropylthiocarbamate) and atrazine by Rhodococcus sp. strain NI86/21. Appl Environ Microbiol 1995, 61:2056-2060.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 2056-2060
    • Nagy, I.1    Compernolle, F.2    Ghys, K.3    Vanderleyden, J.4    De Mot, R.5
  • 5
    • 0027487141 scopus 로고
    • Reductive dehalogenation by cytochrome P450cam: Substrate binding and catalysis
    • Li S, Wackelt LP: Reductive dehalogenation by cytochrome P450cam: substrate binding and catalysis. Biochemistry 1993, 32:9355-9361.
    • (1993) Biochemistry , vol.32 , pp. 9355-9361
    • Li, S.1    Wackelt, L.P.2
  • 6
    • 0000350777 scopus 로고
    • Twenty-five years of P450cam research: Mechanistic insights into oxygenase catalysis
    • Edited by Ortiz de Montellano PR. New York and London: Plenum Press
    • Mueller EJ, Loida PJ, Sligar SG: Twenty-five years of P450cam research: mechanistic insights into oxygenase catalysis. In Cytochrome P450 Structure, Mechanism, and Biochemistry, edn 2. Edited by Ortiz de Montellano PR. New York and London: Plenum Press; 1995:83-124.
    • (1995) Cytochrome P450 Structure, Mechanism, and Biochemistry, Edn 2. , pp. 83-124
    • Mueller, E.J.1    Loida, P.J.2    Sligar, S.G.3
  • 7
    • 0028227789 scopus 로고
    • Oxidation of low molecular weight chloroalkanes by P450cam
    • Lefever MR, Wackett LP: Oxidation of low molecular weight chloroalkanes by P450cam. Biochem Biophys Res Commun 1994, 201:373-378.
    • (1994) Biochem Biophys Res Commun , vol.201 , pp. 373-378
    • Lefever, M.R.1    Wackett, L.P.2
  • 8
    • 9044254525 scopus 로고    scopus 로고
    • P450 superfamily: Update on new sequences, gene mapping accession numbers and nomenclature
    • Nelson DR, Koymans L, Kamataki T, Stefeman JJ, Feyereisen R, Waxman DJ, Waterman MR, Gotoh O, Coon MJ, Estabrook RW et al.: P450 superfamily: update on new sequences, gene mapping accession numbers and nomenclature. Pharmacogenetics 1996, 6:1-42. A comprehensive look at known P450 sequences and classifications. The paper includes the locations of web sites with information and excellent sources for recent information about P450 sequence alignments and current crystal structures.
    • (1996) Pharmacogenetics , vol.6 , pp. 1-42
    • Nelson, D.R.1    Koymans, L.2    Kamataki, T.3    Stefeman, J.J.4    Feyereisen, R.5    Waxman, D.J.6    Waterman, M.R.7    Gotoh, O.8    Coon, M.J.9    Estabrook, R.W.10
  • 9
    • 0023645035 scopus 로고
    • High-resolution crystal structure of cytochrome P-450cam
    • Poulos TL, Finzel BC, Howard AJ: High-resolution crystal structure of cytochrome P-450cam. 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
  • 11
    • 0028267490 scopus 로고
    • Crystal structure and refinement of cytochrome P450terp at 2.3 a resolution
    • Haseman CA, Ravichandran KG, Peterson JA, Deisenhofer J: Crystal structure and refinement of cytochrome P450terp at 2.3 A resolution. J Mol Biol 1994, 236:1169-1185.
    • (1994) J Mol Biol , vol.236 , pp. 1169-1185
    • Haseman, C.A.1    Ravichandran, K.G.2    Peterson, J.A.3    Deisenhofer, J.4
  • 12
    • 0029586252 scopus 로고
    • Structure of cytochrome P450eryF involved in erythromysin biosynthesis
    • Cupp-Vickery JR, Poulos TL: Structure of cytochrome P450eryF involved in erythromysin biosynthesis. Nat Struct Biol 1995, 2:144-153.
    • (1995) Nat Struct Biol , vol.2 , pp. 144-153
    • Cupp-Vickery, J.R.1    Poulos, T.L.2
  • 13
    • 0029643786 scopus 로고
    • Structure and function of cytochromes P450: A comparative analysis of three crystal structures
    • Hasemann CA, Kurumbail RG, Boddupalli SS, Peterson JA, Deisenhofer J: Structure and function of cytochromes P450: a comparative analysis of three crystal structures. Structure 1995, 2:41-62. An insightful comparison of three P450 crystal structures providing information about conserved structure as well as highly varying regions.
    • (1995) Structure , vol.2 , pp. 41-62
    • Hasemann, C.A.1    Kurumbail, R.G.2    Boddupalli, S.S.3    Peterson, J.A.4    Deisenhofer, J.5
  • 14
    • 0343090202 scopus 로고    scopus 로고
    • Role of residue 480 in substrate specificity of cytochrome P450 2B5 and 2B11
    • Liu J, He YA, Halpert JR: Role of residue 480 in substrate specificity of cytochrome P450 2B5 and 2B11. Arch Biochem Biophys 1996, 327:167-173.
    • (1996) Arch Biochem Biophys , vol.327 , pp. 167-173
    • Liu, J.1    He, Y.A.2    Halpert, J.R.3
  • 15
    • 0028861062 scopus 로고
    • The role of Thr268 in oxygen activation of cytochrome P450BM-3
    • Yeom H, Sligar SG, Li H, Poulos TL, Fulco AJ: 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
  • 16
    • 0030004087 scopus 로고    scopus 로고
    • Peroxo-iron and oxenoid-iron species as alternative oxygenating agents in cytochrome P450-catalyzed reaction: Switching by threonine-302 to alanine mutagenesis of cytochrome P450 2B4
    • Vaz ADN, Pernecky SJ, Raner GM, Coon MJ: Peroxo-iron and oxenoid-iron species as alternative oxygenating agents in cytochrome P450-catalyzed reaction: switching by threonine-302 to alanine mutagenesis of cytochrome P450 2B4. Proc Natl Acad Sci USA 1996, 93:4644-4648.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4644-4648
    • Vaz, A.D.N.1    Pernecky, S.J.2    Raner, G.M.3    Coon, M.J.4
  • 17
    • 0028823597 scopus 로고
    • Site-directed mutagenesis as a tool for molecular modeling of cytochrome P450 2B1
    • Szklarz GD, He YA, Halpert JR: Site-directed mutagenesis as a tool for molecular modeling of cytochrome P450 2B1. Biochemistry 1995, 34:14312-14322.
    • (1995) Biochemistry , vol.34 , pp. 14312-14322
    • Szklarz, G.D.1    He, Y.A.2    Halpert, J.R.3
  • 18
    • 0028968913 scopus 로고
    • Altering the regiospecificity of androstenedione hydroxylase activity in P450s 2a-4/5 by a mutation of the residue at position 481
    • Iwasaki M, Darden TA, Pedersen LG, Negishi M: Altering the regiospecificity of androstenedione hydroxylase activity in P450s 2a-4/5 by a mutation of the residue at position 481. Biochemistry 1995, 34:5054-5059.
    • (1995) Biochemistry , vol.34 , pp. 5054-5059
    • Iwasaki, M.1    Darden, T.A.2    Pedersen, L.G.3    Negishi, M.4
  • 19
  • 20
    • 0029876059 scopus 로고    scopus 로고
    • The catalytic mechanism of P450 BM3 involves a 6 Å movement of the bound substrate on reduction
    • Modi S, Sutcliffe MJ, Primrose WU, Lian L-Y, Roberts GCK: The catalytic mechanism of P450 BM3 involves a 6 Å movement of the bound substrate on reduction. Nat Struct Biol 1996, 3:414-417.
    • (1996) Nat Struct Biol , vol.3 , pp. 414-417
    • Modi, S.1    Sutcliffe, M.J.2    Primrose, W.U.3    Lian, L.-Y.4    Roberts, G.C.K.5
  • 21
    • 0029074117 scopus 로고
    • Active-site analysis of ferric P450 enzymes: Hydrogen-bonding effects on the circular dichroism spectra
    • Anderson LA, Peterson JA: Active-site analysis of ferric P450 enzymes: hydrogen-bonding effects on the circular dichroism spectra. Biochem Biophys Res Commun 1995, 211:389-395.
    • (1995) Biochem Biophys Res Commun , vol.211 , pp. 389-395
    • Anderson, L.A.1    Peterson, J.A.2
  • 22
    • 0030458846 scopus 로고    scopus 로고
    • Carbon monoxide binding to cytochrome P450BM-3: Evidence for a substrate dependent conformational change
    • Mclean MA, Yeom H, Sligar SG: Carbon monoxide binding to cytochrome P450BM-3: evidence for a substrate dependent conformational change. Biochimie 1996, 78:700-705.
    • (1996) Biochimie , vol.78 , pp. 700-705
    • Mclean, M.A.1    Yeom, H.2    Sligar, S.G.3
  • 23
    • 0030040103 scopus 로고    scopus 로고
    • Improved binding of cytochrome P450cam substrate analogues designed to fill extra space in the substrate binding pocket
    • Helms V, Deprez E, Gill E, Barret C, Hui Bon Hoa G, Wade RC: Improved binding of cytochrome P450cam substrate analogues designed to fill extra space in the substrate binding pocket Biochemistry 1996, 35:1485-1499.
    • (1996) Biochemistry , vol.35 , pp. 1485-1499
    • Helms, V.1    Deprez, E.2    Gill, E.3    Barret, C.4    Hui Bon Hoa, G.5    Wade, R.C.6
  • 24
    • 0024208742 scopus 로고
    • The role of active site hydrogen bonding in cytochrome P-450cam as revealed by site-directed mutagenesis
    • Atkins WM, Sligar SG: The role of active site hydrogen bonding in cytochrome P-450cam as revealed by site-directed mutagenesis. J Biol Chem 1988, 263:18842-18849.
    • (1988) J Biol Chem , vol.263 , pp. 18842-18849
    • Atkins, W.M.1    Sligar, S.G.2
  • 25
    • 1542503695 scopus 로고    scopus 로고
    • Engineering the selectivity of aliphatic C-H bond oxidation catalyzed by cytochrome P450cam
    • Jones NE, England PA, Rouch DA, Wong L-L: Engineering the selectivity of aliphatic C-H bond oxidation catalyzed by cytochrome P450cam. J Chem Soc Chem Commun 1996:2413-2414. An example of how the regioselectivity of a cytochrome P450 can be dramatically altered by site-directed mutagenesis.
    • J Chem Soc Chem Commun , vol.1996 , pp. 2413-2414
    • Jones, N.E.1    England, P.A.2    Rouch, D.A.3    Wong, L.-L.4
  • 29
    • 0027503325 scopus 로고
    • Engineering cytochrome P450cam to increase the stereospecificity and coupling of aliphatic hydroxylation
    • Loida PJ, Sligar SG: Engineering cytochrome P450cam to increase the stereospecificity and coupling of aliphatic hydroxylation. Protein Eng 1993, 6:207-212.
    • (1993) Protein Eng , vol.6 , pp. 207-212
    • Loida, P.J.1    Sligar, S.G.2
  • 30
    • 0000253264 scopus 로고
    • Theoretical investigation of the anaerobic reduction of halogenated alkanes by cytochrome P-450. 2. Vertical electron affinities of chlorofluoromethanes as a measure of their activity
    • Luke BT, Loew GH, McLean AD: Theoretical investigation of the anaerobic reduction of halogenated alkanes by cytochrome P-450. 2. Vertical electron affinities of chlorofluoromethanes as a measure of their activity. J Am Chem Soc 1988, 110:3396-3400.
    • (1988) J am Chem Soc , vol.110 , pp. 3396-3400
    • Luke, B.T.1    Loew, G.H.2    McLean, A.D.3
  • 31
    • 0028845403 scopus 로고
    • Enzyme-catalyzed dehalogenation of pentachloroethane: Why F87W-cytochrome P450cam is faster than wild type
    • cam are used to explain why this mutant dehalogenates faster than wild-type enzyme.
    • (1995) Protein Eng , vol.8 , pp. 801-807
    • Manchester, J.I.1    Ornstein, R.L.2
  • 34
    • 0343161831 scopus 로고    scopus 로고
    • Pseudomonas cytochrome P-450 oxygenases: Pogress toward de novo design for bioremediation
    • Edited by Nakazawa T. Washington, DC: ASM Press
    • cam to carry out dehalogenation reactions. Increases in dehalogenation rates of up to 150% over wild type were demonstrated.
    • (1996) Molecular Biology of Pseudomonads , pp. 342-350
    • Sligar, S.G.1    Mueller, E.J.2    Loida, P.J.3
  • 35
    • 0029559738 scopus 로고
    • Molecular dynamics simulations indicate that F87W, T185F-cytochrome P450cam may reductively dehalogenate 1,1,1-trichloroethane
    • cam. This is a good example of how molecular dynamics simulations may be important for designing P450s to carry out novel reactions.
    • (1995) J Biomol Struct Dyn , vol.13 , pp. 413-422
    • Manchester, J.I.1    Ornstein, R.L.2
  • 36
    • 0030457185 scopus 로고    scopus 로고
    • Rational approach to improving reductive catalysis by cytochrome P450cam
    • Manchester JI, Ornstein RL: Rational approach to improving reductive catalysis by cytochrome P450cam. Biochimie 1996, 78:714-722.
    • (1996) Biochimie , vol.78 , pp. 714-722
    • Manchester, J.I.1    Ornstein, R.L.2
  • 38
    • 0342292194 scopus 로고
    • Biomacromolecules: From 3-D structure to applications
    • Edited by Ornstein RL. Pasco, WA: Battelle Press
    • Ornstein RL: Biomacromolecules: from 3-D structure to applications. In Proceedings of the Thirty-Fourth Hanford Symposium on Health and the Environment. Edited by Ornstein RL. Pasco, WA: Battelle Press; 1995. This report includes a wide variety of approaches to the problem of biore-mediation and some possible solutions. It is an impressive overview of the state of the art in bioremediation science.
    • (1995) Proceedings of the Thirty-Fourth Hanford Symposium on Health and the Environment
    • Ornstein, R.L.1
  • 39
    • 0029880618 scopus 로고    scopus 로고
    • Conversion from farnesyl diphosphate synthase to geranylgeranyl diphosphate synthase by random chemical mutagenesis
    • Ohnuma S-I, Nakasawa T, Hisashi H: Conversion from farnesyl diphosphate synthase to geranylgeranyl diphosphate synthase by random chemical mutagenesis. J Biol Chem 1996, 271:10087-10095.
    • (1996) J Biol Chem , vol.271 , pp. 10087-10095
    • Ohnuma, S.-I.1    Nakasawa, T.2    Hisashi, H.3
  • 40
    • 0028149977 scopus 로고
    • Alteration of substrate specificity and optimum pH of sarcosine oxidase by random and site-directed mutagenesis
    • Nishiya Y, Imanaka T: Alteration of substrate specificity and optimum pH of sarcosine oxidase by random and site-directed mutagenesis. Appl Environ Microbiol 1994, 60:4213-4215.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 4213-4215
    • Nishiya, Y.1    Imanaka, T.2
  • 41
    • 0027245444 scopus 로고
    • Random mutagenesis of the substrate-binding site of a serine protease can generate enzymes with increased activities and altered primary specificities
    • Graham LD, Haggett KD, Jennings PA: Random mutagenesis of the substrate-binding site of a serine protease can generate enzymes with increased activities and altered primary specificities. Biochemistry 1993, 32:6250-6258.
    • (1993) Biochemistry , vol.32 , pp. 6250-6258
    • Graham, L.D.1    Haggett, K.D.2    Jennings, P.A.3
  • 42
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer WPC: Rapid evolution of a protein in vitro by DNA shuffling. Nature 1994, 370:389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 43
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer WPC: DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution. Proc Natl Acad Sci USA 1994, 91:10747-10751.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10747-10751
    • Stemmer, W.P.C.1
  • 44
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri A, Whitehorn EA, Tate E, Stemmer WPC: Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat Biotechnol 1996, 14:315-319. An excellent demonstration of how DNA shuffling can be utilized to synthetically evolve enzymes to carry out desired functions.
    • (1996) Nat Biotechnol , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.A.2    Tate, E.3    Stemmer, W.P.C.4
  • 46
    • 0028258507 scopus 로고
    • Semi-artificial hydroxylating enzymes created by flavins binding to cytochrome P450 2B4 and by bleomycin binding to NADPH-cytochrome P450 reductase
    • Uvarov VY, Shumyantseva VV, Bykhovskaya EA, Kolyada LN, Archakov Al: Semi-artificial hydroxylating enzymes created by flavins binding to cytochrome P450 2B4 and by bleomycin binding to NADPH-cytochrome P450 reductase. Biochem Biophys Res Commun 1994, 200:722-725.
    • (1994) Biochem Biophys Res Commun , vol.200 , pp. 722-725
    • Uvarov, V.Y.1    Shumyantseva, V.V.2    Bykhovskaya, E.A.3    Kolyada, L.N.4    Archakov, A.L.5
  • 47
    • 0029809775 scopus 로고    scopus 로고
    • Putidaredoxin reductase-putidaredoxin-cytochrome P450cam triple fusion protein
    • Sibbesen O, DeVoss JJ, Ortiz de Montellano PR: 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    DeVoss, J.J.2    De Ortiz Montellano, P.R.3
  • 48
    • 0030199369 scopus 로고    scopus 로고
    • Luciferase-dependent cytochrome P-450-catalyzed dehalogenation in genetically engineered Pseudomonas
    • cam dehalogenation reactions.
    • (1996) Biotechnol Prog , vol.12 , pp. 474-479
    • Shanker, R.1    Atkins, W.M.2
  • 49
    • 0024468304 scopus 로고
    • 5-cytochrome P-450cam association: A proposed molecular model for a cytochrome P-450cam electron-transfer complex
    • 5-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
  • 50
    • 0029666288 scopus 로고    scopus 로고
    • Role of Arg112 of cytochrome P450cam in the electron transfer from reduced putidaredoxin
    • Unno M, Shimada H, Toba Y, Makino R, Ishimura Y: Role of Arg112 of cytochrome P450cam in the electron transfer from reduced putidaredoxin. J Biol Chem 1996, 271:17869-17874.
    • (1996) J Biol Chem , vol.271 , pp. 17869-17874
    • Unno, M.1    Shimada, H.2    Toba, Y.3    Makino, R.4    Ishimura, Y.5
  • 51
    • 0029144146 scopus 로고
    • Recruitment of co-metabolic enzymes for environmental detoxification of organohalides
    • cam and oxidative dechlorogenation by toluene dioxygenase.
    • (1995) Environ Health Perspect , vol.103 , pp. 45-48
    • Wackett, L.P.1


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