Structure and function of cytochromes P450: a comparative analysis of three crystal structures.

[1]  M. Waterman,et al.  Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding. , 1992, The Journal of biological chemistry.

[2]  D. G. Davis,et al.  Engineering mouse P450coh to a novel corticosterone 15 alpha-hydroxylase and modeling steroid-binding orientation in the substrate pocket. , 1993, The Journal of biological chemistry.

[3]  R. Lindberg,et al.  Alteration of mouse cytochrome P450coh substrate specificity by mutation of a single amino-acid residue , 1989, Nature.

[4]  J. Lambeth,et al.  Ionic effects on adrenal steroidogenic electron transport. The role of adrenodoxin as an electron shuttle. , 1979, The Journal of biological chemistry.

[5]  R. Estabrook,et al.  Cytochrome P450 and the arachidonate cascade 1 , 1992, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[6]  M. Dufau,et al.  Dissociation of hydroxylase and lyase activities by site-directed mutagenesis of the rat P45017 alpha. , 1991, Molecular endocrinology.

[7]  Charles E. Bugg,et al.  Crystallographic and Modeling Methods in Molecular Design , 1990, Springer New York.

[8]  V. Coghlan,et al.  Site-specific mutations in human ferredoxin that affect binding to ferredoxin reductase and cytochrome P450scc. , 1991, The Journal of biological chemistry.

[9]  M. Komori,et al.  Replacement of Thr-303 of P450 2E1 with serine modifies the regioselectivity of its fatty acid hydroxylase activity. , 1993, Journal of biochemistry.

[10]  Y Fujii-Kuriyama,et al.  Site-directed mutageneses of rat liver cytochrome P-450d: catalytic activities toward benzphetamine and 7-ethoxycoumarin. , 1989, Biochemistry.

[11]  U. Meyer,et al.  Sequence requirements for cytochrome P-450IID1 catalytic activity. A single amino acid change (Ile380 Phe) specifically decreases Vmax of the enzyme for bufuralol but not debrisoquine hydroxylation. , 1990, The Journal of biological chemistry.

[12]  M. Negishi,et al.  Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and site-directed mutagenesis. , 1991, The Journal of biological chemistry.

[13]  R. Raag,et al.  Cytochrome P450cam: crystallography, oxygen activation, and electron transfer1 , 1992, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[14]  R. Raag,et al.  Inhibitor-induced conformational change in cytochrome P-450CAM. , 1993, Biochemistry.

[15]  O. Gotoh,et al.  Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences. , 1992, The Journal of biological chemistry.

[16]  T. Noguti,et al.  Hydrogen bond network of cytochrome P-450cam: a network connecting the heme group with helix K. , 1992, Biochimica et biophysica acta.

[17]  S. Black,et al.  Steroid 17 alpha-hydroxylase and 17,20-lyase activities of P450c17: contributions of serine106 and P450 reductase. , 1993, Endocrinology.

[18]  T. Poulos,et al.  High-resolution crystal structure of cytochrome P450cam. , 1987, Journal of molecular biology.

[19]  J. Trudell,et al.  Association of cytochrome b5 and cytochrome P-450 reductase with cytochrome P-450 in the membrane of reconstituted vesicles. , 1982, The Journal of biological chemistry.

[20]  D. Eisenberg,et al.  Three-dimensional profiles from residue-pair preferences: identification of sequences with beta/alpha-barrel fold. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[21]  T. Poulos,et al.  Putidaredoxin competitively inhibits cytochrome b5-cytochrome P-450cam association: a proposed molecular model for a cytochrome P-450cam electron-transfer complex. , 1989, Biochemistry.

[22]  Barry Honig,et al.  Focusing of electric fields in the active site of Cu‐Zn superoxide dismutase: Effects of ionic strength and amino‐acid modification , 1986, Proteins.

[23]  K. Degtyarenko,et al.  Secondary structure and membrane topology of cytochrome P450s. , 1989, Archives of biochemistry and biophysics.

[24]  J. Sussman,et al.  An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[25]  Andrew Howard,et al.  Crystal structures of metyrapone- and phenylimidazole-inhibited complexes of cytochrome P-450cam , 1993 .

[26]  J. Devereux,et al.  A comprehensive set of sequence analysis programs for the VAX , 1984, Nucleic Acids Res..

[27]  J Deisenhofer,et al.  Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's. , 1993, Science.

[28]  H Koga,et al.  Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: possible role of the hydroxy amino acid in oxygen activation. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[29]  M. Kjeldgaard,et al.  O: A Macromolecule Modeling Environment , 1990 .

[30]  F. Guengerich.  Reactions and significance of cytochrome P-450 enzymes. , 1991, The Journal of biological chemistry.

[31]  S. Wrighton,et al.  The human hepatic cytochromes P450 involved in drug metabolism. , 1992, Critical reviews in toxicology.

[32]  B Honig,et al.  Electrostatic control of midpoint potentials in the cytochrome subunit of the Rhodopseudomonas viridis reaction center. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[33]  M. J. Coon,et al.  Cytochrome P-450 : multiplicity of isoforms, substrates, and catalytic and regulatory mechanisms , 1991 .

[34]  B C Finzel,et al.  Crystal structure of substrate-free Pseudomonas putida cytochrome P-450. , 1986, Biochemistry.

[35]  G J Williams,et al.  The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.

[36]  M. J. Coon,et al.  Oxygen activation by cytochrome P-450. , 1980, Annual review of biochemistry.

[37]  M. J. Coon,et al.  The P450 superfamily: update on new sequences, gene mapping, accession numbers, early trivial names of enzymes, and nomenclature. , 1993, DNA and cell biology.

[38]  A. Fulco.  P450BM-3 and other inducible bacterial P450 cytochromes: biochemistry and regulation. , 1991, Annual review of pharmacology and toxicology.

[39]  S. Sligar,et al.  The roles of active site hydrogen bonding in cytochrome P-450cam as revealed by site-directed mutagenesis. , 1988, The Journal of biological chemistry.

[40]  S. Sligar,et al.  The cytochrome P-450cam binding surface as defined by site-directed mutagenesis and electrostatic modeling. , 1990, Biochemistry.

[41]  T. Aoyama,et al.  Sequence requirements for cytochrome P-450IIB1 catalytic activity. Alteration of the stereospecificity and regioselectivity of steroid hydroxylation by a simultaneous change of two hydrophobic amino acid residues to phenylalanine. , 1989, The Journal of biological chemistry.

[42]  J. Peterson,et al.  The involvement of carboxylate groups of putidaredoxin in the reaction with putidaredoxin reductase. , 1986, The Journal of biological chemistry.

[43]  David F. V. Lewis,et al.  The sequence homologies of cytochromes P-450 and active-site geometries , 1992, J. Comput. Aided Mol. Des..

[44]  C. Mendelson,et al.  Structure-function relationships of human aromatase cytochrome P-450 using molecular modeling and site-directed mutagenesis. , 1991, The Journal of biological chemistry.

[45]  D. Mock,et al.  Equilibrium and kinetic studies of the interaction of cytochrome P-450cam and putidaredoxin. , 1982, The Journal of biological chemistry.

[46]  D. Nelson,et al.  Secondary structure prediction of 52 membrane-bound cytochromes P450 shows a strong structural similarity to P450cam. , 1989, Biochemistry.

[47]  D. Zhou,et al.  Functional domains of aromatase cytochrome P450 inferred from comparative analyses of amino acid sequences and substantiated by site-directed mutagenesis experiments. , 1992, The Journal of biological chemistry.

[48]  M. Sternberg,et al.  A predicted three-dimensional structure of human cytochrome P450: implications for substrate specificity. , 1991, Protein engineering.

[49]  T. Poulos,et al.  A site-directed mutagenesis study of human placental aromatase. , 1992, The Journal of biological chemistry.

[50]  K. Sekimizu,et al.  Putative functions of phenylalanine-350 of Pseudomonas putida cytochrome P-450cam. , 1994, Biochimica et biophysica acta.

[51]  R. Raag,et al.  The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450CAM. , 1991, Biochemistry.

[52]  P. Hollenberg.  Mechanisms of cytochrome P450 and peroxidase‐catalyzed xenobiotic metabolism , 1992, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[53]  J Deisenhofer,et al.  Crystal structure and refinement of cytochrome P450terp at 2.3 A resolution. , 1994, Journal of molecular biology.

[54]  A. Lesk,et al.  The relation between the divergence of sequence and structure in proteins. , 1986, The EMBO journal.

[55]  C. Ouzounis,et al.  Primary and secondary structural patterns in eukaryotic cytochrome P-450 families correspond to structures of the helix-rich domain of Pseudomonas putida cytochrome P-450cam. Indications for a similar overall topology. , 1991, European journal of biochemistry.

[56]  S. Martinis,et al.  Crystal structure of the cytochrome P-450CAM active site mutant Thr252Ala. , 1991, Biochemistry.

[57]  T. Kronbach,et al.  Hybrid cytochromes P-450 identify a substrate binding domain in P-450IIC5 and P-450IIC4. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[58]  Y. Fujii‐Kuriyama,et al.  P450 and Human Cancer , 1991, Japanese journal of cancer research : Gann.

[59]  S. Sligar,et al.  Engineering cytochrome P-450cam to increase the stereospecificity and coupling of aliphatic hydroxylation. , 1993, Protein engineering.

[60]  S. Sligar,et al.  Catalytic mechanism of cytochrome P-450: evidence for a distal charge relay , 1992 .

[61]  S. Boddupalli,et al.  Fatty acid monooxygenation by cytochrome P-450BM-3. , 1990, The Journal of biological chemistry.

[62]  D. Beale,et al.  Structure and function of the constant regions of immunoglobulins , 1976, Quarterly Reviews of Biophysics.

[63]  M. J. Coon,et al.  Aliphatic hydroxylation by highly purified liver microsomal cytochrome P-450. Evidence for a carbon radical intermediate. , 1978, Biochemical and biophysical research communications.

[64]  K. Mihara,et al.  The amino‐terminal structures that determine topological orientation of cytochrome P‐450 in microsomal membrane. , 1990, The EMBO journal.

[65]  Ortiz de Montellano,et al.  Cytochrome P-450: Structure, Mechanism, and Biochemistry , 1986 .

[66]  S. D. Black.  Membrane topology of the mammalian P450 cytochromes , 1992, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[67]  S. Boddupalli,et al.  Reconstitution of the fatty acid hydroxylation function of cytochrome P-450BM-3 utilizing its individual recombinant hemo- and flavoprotein domains. , 1992, The Journal of biological chemistry.

[68]  J. Halpert,et al.  Engineering of cytochrome P450 2B1 specificity. Conversion of an androgen 16 beta-hydroxylase to a 15 alpha-hydroxylase. , 1993, The Journal of biological chemistry.

[69]  Y. Fujii‐Kuriyama,et al.  Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagenesis. Interaction with NADPH-cytochrome P450 reductase. , 1991, The Journal of biological chemistry.

[70]  R. Raag,et al.  Crystal structures of cytochrome P-450CAM complexed with camphane, thiocamphor, and adamantane: factors controlling P-450 substrate hydroxylation. , 1991, Biochemistry.

[71]  Julian,et al.  Cytochrome P-450terp. Isolation and purification of the protein and cloning and sequencing of its operon. , 1992, The Journal of biological chemistry.

[72]  K. Korzekwa,et al.  Site-directed mutagenesis of cytochrome P450s CYP2A1 and CYP2A2: influence of the distal helix on the kinetics of testosterone hydroxylation. , 1992, Biochemistry.

[73]  A. D. McLachlan,et al.  Profile analysis: detection of distantly related proteins. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[74]  B C Finzel,et al.  The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450. , 1985, The Journal of biological chemistry.

[75]  K. Yura,et al.  Essential role of the Arg112 residue of cytochrome P450cam for electron transfer from reduced putidaredoxin , 1993, FEBS letters.

[76]  E. Getzoff,et al.  Faster superoxide dismutase mutants designed by enhancing electrostatic guidance , 1992, Nature.

[77]  R. Raag,et al.  Crystal structure of the carbon monoxide-substrate-cytochrome P-450CAM ternary complex. , 1989, Biochemistry.

[78]  R. Kassner,et al.  A theoretical model for the effects of local nonpolar heme environments on the redox potentials in cytochromes. , 1973, Journal of the American Chemical Society.

[79]  D. Nelson,et al.  On the membrane topology of vertebrate cytochrome P-450 proteins. , 1988, The Journal of biological chemistry.

[80]  K. Holm,et al.  Prostaglandin metabolism by hepatic cytochrome P-450. , 1989, Drug metabolism reviews.

[81]  P. Ortiz de Montellano,et al.  Formation, crystal structure, and rearrangement of a cytochrome P-450cam iron-phenyl complex. , 1990, Biochemistry.

[82]  T Shimizu,et al.  Role of Glu318 at the putative distal site in the catalytic function of cytochrome P450d. , 1992, Biochemistry.

[83]  J. Halpert,et al.  Role of residue 478 as a determinant of the substrate specificity of cytochrome P450 2B1. , 1992, Biochemistry.

[84]  Dr. Peter F. Hall,et al.  Cytochromes P-450 and the regulation of steroid synthesis , 1986, Steroids.

[85]  B. Kemper,et al.  A single amino acid substitution confers progesterone 6 beta-hydroxylase activity to rabbit cytochrome P450 2C3. , 1993, The Journal of biological chemistry.

[86]  Y. Imai,et al.  Point mutations at threonine-301 modify substrate specificity of rabbit liver microsomal cytochromes P-450 (laurate (ω-1)-hydroxylase and testosterone 16α-hydroxylase) , 1989 .

[87]  F S Mathews,et al.  The structure, function and evolution of cytochromes. , 1985, Progress in biophysics and molecular biology.

[88]  L. Geren,et al.  Identification of specific carboxylate groups on adrenodoxin that are involved in the interaction with adrenodoxin reductase. , 1984, The Journal of biological chemistry.

[89]  K. Pommerening,et al.  Modification of carboxyl groups on NADPH-cytochrome P-450 reductase involved in binding of cytochromes c and P-450 LM2. , 1987, Biochemistry international.