heme has been researched along with phenylalanine in 91 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 16 (17.58) | 18.7374 |
| 1990's | 24 (26.37) | 18.2507 |
| 2000's | 32 (35.16) | 29.6817 |
| 2010's | 15 (16.48) | 24.3611 |
| 2020's | 4 (4.40) | 2.80 |
| Authors | Studies |
|---|---|
| Andreeva, AP; Belostotskiĭ, VM | 1 |
| Glenn, AR; May, BK | 1 |
| Bray, RR; Burke, JF; Sanders, SA; Smith, AT; Thorneley, RN | 1 |
| Bray, RC; Burke, JF; Sanders, SA; Smith, AT; Thorneley, RN; Veitch, NC; Williams, RJ | 1 |
| La Mar, GN; Mizukami, H; Yu, LP | 1 |
| Bain, MD; Bingham, P; Chalmers, RA; Jones, M; Purkiss, P; Stacey, TE | 1 |
| Garber, EA; Luntz, TL; Margoliash, E; Schejter, A | 1 |
| Brayer, GD; Louie, GV | 1 |
| Brayer, GD; Louie, GV; Pielak, GJ; Smith, M | 1 |
| Billups, C; Horwitz, J; Kay, E; Shannon, LM; Strickland, EH; Wilchek, M | 1 |
| Sano, S | 1 |
| Amit, N; Formanek, H | 1 |
| Carrell, RW; Owen, MC | 1 |
| Efron, ML; Shahidi, NT | 1 |
| Horwitz, J; Kay, E; Shannon, LM; Strickland, EH | 1 |
| Hatch, TP; Lascelles, J | 1 |
| Bosshard, HR | 1 |
| Krogmann, DW; Markley, JL; Ulrich, EL | 1 |
| Ord, JM; Wildenthal, K | 1 |
| Newmyer, SL; Ortiz de Montellano, PR | 1 |
| Doseeva, VV; Galkin, AG; Gazaryan, IG; Tishkov, VI | 1 |
| Coggins, JR; Kelly, SM; Lindsay, JG; Malarkey, K; McKnight, J; Miles, JS; Munro, AW; Price, NC; Thomson, AJ | 1 |
| Dalbøge, H; Tams, JW; Veitch, NC; Vind, J; Welinder, KG | 1 |
| Porter, TD | 1 |
| Hara, T; Horiuchi, T; Okada, O; Sagara, Y; Sekimizu, K; Yasukochi, T | 1 |
| Berghuis, AM; Brayer, GD; Guillemette, JG; Smith, M | 1 |
| Emerson, SD; Krishnamoorthi, R; La Mar, GN; Mizukami, H; Rajarathnam, K; Vyas, K; Yu, LP | 1 |
| Bardakdjian, J; Galacteros, F; Harousseau, JL; Kister, J; M'Rad, A; Milpied, N; Promé, D; Rapp, MJ; Riou, J; Wajcman, H | 1 |
| Doseeva, VV; Galkin, AG; Gazarian, IG; Tishkov, VI | 1 |
| Manchester, JI; Ornstein, RL | 1 |
| Gettemy, J; Gold, MH; Hildebrand, DP; Kishi, K; Kusters-van Someren, M; Mauk, AG | 1 |
| Mortuza, GB; Whitford, D | 1 |
| Gao, Y; Smith, AT; Veitch, NC; White, CG | 1 |
| Elber, R; Meller, J | 1 |
| Brucker, EA; La Mar, GN; Lile, RA; Nguyen, BD; Olson, JS; Phillips, GN; Vyas, K; Wittenberg, JB; Zhao, X | 1 |
| Chien, EY; Friedman, JM; Peterson, ES; Sligar, SG | 1 |
| Das, TK; Gennis, RB; Pecoraro, C; Rousseau, DL; Tomson, FL | 1 |
| Dou, Y; Gooding, EA; Hochstrasser, RM; Ikeda-Saito, M; Kholodenko, Y | 1 |
| Hendrich, MP; Ho, C; Ho, NT; Jeong, ST | 1 |
| Boffi, A; Chiancone, E; Giangiacomo, L; Guarrera, L; Spagnuolo, C | 1 |
| Hillar, A; Loboda, A; Loewen, PC; Mauk, AG; Pauls, R; Peters, B; Zhang, H | 1 |
| Bendall, DS; Carrell, CJ; Cramer, WA; Howe, CJ; Ponamarev, MV; Schlarb, BG; Smith, JL | 1 |
| Daff, S; Sagami, I; Sato, Y; Shimizu, T | 1 |
| Döpner, S; Harris, TR; Hildebrand, DP; Hildebrandt, P; Mauk, AG; Rosell, FI | 1 |
| Howes, BD; Smith, AT; Smulevich, G; Veitch, NC; White, CG | 1 |
| Ishikawa, H; Ishimori, K; Morishima, I; Takahashi, S; Uchida, T | 1 |
| Arciero, DM; Hooper, AB; Iverson, TM; Rees, DC | 1 |
| Rafferty, SP; Wilson, DJ | 1 |
| Correia, MA; Maltby, D; Medzihradszky, KF; Wang, X | 1 |
| Chapman, SK; Miles, CS; Munro, AW; Murdoch, J; Ost, TW; Reid, GA | 1 |
| Ciaccio, C; Coletta, M; De Sanctis, G; Feis, A; Neri, F; Santoni, E; Smulevich, G; Welinder, KG | 1 |
| Adak, S; Dawson, JH; Goodin, DB; Ikeda-Saito, M; Perera, R; Pond, AE; Sono, M; Stuehr, DJ; Tomita, T; Voegtle, HL | 1 |
| Conover, RC; Daldal, F; Johnson, MK; Knaff, DB; Li, J; Osyczka, A; Qin, H | 1 |
| FUNAHASHI, S; SHICHI, H; SUGIMURA, Y | 1 |
| Chen, Z; Ost, TW; Schelvis, JP | 1 |
| Colas, C; De Montellano, PR | 1 |
| Angove, HC; Cosme, J; Day, PJ; Jhoti, H; Tickle, IJ; Vinkovic, DM; Vonrhein, C; Ward, A; Williams, PA | 1 |
| Erickson, J; Londer, YY; Long, WC; Pessanha, M; Pokkuluri, PR; Salgueiro, CA; Schiffer, M | 1 |
| Akutsu, H; Harada, E; Kobayashi, R; Ozawa, K; Takayama, Y | 1 |
| Lecomte, JT; Mukhopadhyay, K | 1 |
| Anderson, VE; Nukuna, BN; Sun, G | 1 |
| Ishikawa, H; Ishimori, K; Morishima, I; Takahashi, S | 1 |
| Guo, Z; Lu, Y; Wang, Z; Yeung, N; Zhao, X | 1 |
| Lu, Y; Nilges, MJ; Zhao, X | 1 |
| Giovannelli, JL; Ho, C; Ho, NT; Lukin, JA; Simplaceanu, V; Wiltrout, ME | 1 |
| Choi, PS; Scholes, CP; Shapleigh, JP; Usov, OM | 1 |
| Goodman, M; Halder, P; Hargrove, MS; Hoy, JA; Kundu, S; Premer, S; Savage, A; Smagghe, BJ; Venugopal, A; Weiland, TR | 1 |
| Brenner, S; Girvan, HM; Hay, S; Munro, AW; Scrutton, NS | 1 |
| El-Mashtoly, SF; Kitagawa, T; Nakashima, S; Shimizu, T; Tanaka, A | 1 |
| Shimizu, T; Tanaka, A | 1 |
| Guo, L; Link, JJ; Stevens, JA; Wang, L; Zang, C; Zhong, D | 1 |
| Araki, Y; Igarashi, J; Ito, S; Shimizu, T; Tanaka, A; Wada, T | 1 |
| Cheatham, TE; Moore, CD; Shahrokh, K; Sontum, SF; Yost, GS | 1 |
| Banu, H; Renuka, N; Vasanthakumar, G | 1 |
| Castro, L; Demicheli, V; Kagan, VE; Kapralov, AA; Klein-Seetharaman, J; Maeda, A; Mylnikov, D; Peterson, J; Radi, R; Samhan-Arias, A; Tortora, V; Tyurina, YY; Vladimirov, YA; Weitz, AA; Yanamala, N | 1 |
| Dewilde, S; Ezhevskaya, M; Moens, L; Trandafir, F; Van Doorslaer, S | 1 |
| Donald, LJ; Jha, V; Loewen, PC | 1 |
| De La Rosa, MÁ; Díaz-Moreno, I; García-Heredia, JM; Hildebrandt, P; Ly, HK; Utesch, T | 1 |
| Desmet, F; Dewilde, S; Maurelli, S; Moens, L; Tilleman, L; Trandafir, F; Van Doorslaer, S; Verrept, B | 1 |
| Altenbuchner, J; Birke, J; Hambsch, N; Jendrossek, D; Schmitt, G | 1 |
| Correa-Basurto, J; Hernández-Rodríguez, M; Mendieta-Wejebe, JE; Ramírez-Durán, LA; Rosales-Hernández, MC; Trujillo-Ferrara, J | 1 |
| Dantas, JM; Morgado, L; Pokkuluri, PR; Salgueiro, CA; Turner, DL | 1 |
| Copié, V; Eilers, BJ; Fonner, BA; Lei, B; Liu, M; Moore, R; Stanisich, J; Sullivan-Springhetti, RK; Tripet, BP | 1 |
| Bu, W; Im, S; Meagher, J; Pearl, NM; Rwere, F; Shaik, S; Stuckey, J; Sun, C; Tarasev, M; Usharani, D; Waskell, L; Yang, Y; Zhang, H | 1 |
| Li, W; Lin, YW; Tan, X; Wen, GB; Xiang, Y; Yan, DJ | 1 |
| Hagras, MA; Stuchebrukhov, AA | 1 |
| Fan, CZ; Li, YT; Pan, ZF; Tang, WY; Wang, W | 1 |
| Alcalde, M; Ayala, M; Martin-Diaz, J; Pastor, N; Ramirez-Ramirez, J | 1 |
| Estrin, DA; Issoglio, F; Pedron, FN; Scherlis, DA | 1 |
| Honda, K; Imai, T; Kawamoto, J; Mihara, H; Tanaka, M; Tobe, R | 1 |
| Hsu, MH; Johnson, EF | 1 |
91 other study(ies) available for heme and phenylalanine
| Article | Year |
|---|---|
[Peroxidase activity of hemoglobin, modified at the carboxylic groups of heme and amino acids].
Topics: Amino Acids; Heme; Hemoglobins; Hydrogen-Ion Concentration; Kinetics; Peroxidases; Phenylalanine | 1979 |
Effect of haemin on endogenous protein synthesis in oocytes of the Queensland cane toad Bufo marinus.
Topics: Animals; Bufo marinus; Depression, Chemical; Female; Heme; Hemin; Leucine; Oocytes; Ovum; Phenylalanine; Protein Biosynthesis; Valine | 1975 |
Characterisation of a haem active-site mutant of horseradish peroxidase, Phe41----Val, with altered reactivity towards hydrogen peroxide and reducing substrates.
Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Heme; Horseradish Peroxidase; Hydrogen Peroxide; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oligodeoxyribonucleotides; Oxidation-Reduction; Phenylalanine; Recombinant Proteins; Spectrum Analysis; Structure-Activity Relationship; Valine | 1992 |
Structural studies by proton-NMR spectroscopy of plant horseradish peroxidase C, the wild-type recombinant protein from Escherichia coli and two protein variants, Phe41----Val and Arg38----Lys.
Topics: Arginine; Cyanides; Heme; Horseradish Peroxidase; Hydroxamic Acids; Isoenzymes; Lysine; Magnetic Resonance Spectroscopy; Phenylalanine; Protein Conformation; Recombinant Proteins; Structure-Activity Relationship; Valine | 1992 |
Rearrangement of the distal pocket accompanying E7 His----Gln substitution in elephant carbonmonoxy- and oxymyoglobin: 1H NMR identification of a new aromatic residue in the heme pocket.
Topics: Animals; Binding Sites; Elephants; Glutamine; Heme; Histidine; Kinetics; Magnetic Resonance Spectroscopy; Myoglobin; Phenylalanine; Protein Conformation; Structure-Activity Relationship | 1990 |
Dietary treatment eliminates succinylacetone from the urine of a patient with tyrosinaemia type 1.
Topics: Amino Acid Metabolism, Inborn Errors; Female; Heme; Heptanoates; Heptanoic Acids; Humans; Infant; Methionine; Phenylalanine; Tyrosine | 1990 |
Structural significance of an internal water molecule studied by site-directed mutagenesis of tyrosine-67 in rat cytochrome c.
Topics: Animals; Cytochrome c Group; DNA Mutational Analysis; Heme; Hydrogen Bonding; Magnetic Resonance Spectroscopy; Models, Molecular; Phenylalanine; Protein Conformation; Rats; Recombinant Proteins; Structure-Activity Relationship; Thermodynamics; Tyrosine; Urea; Water | 1989 |
A polypeptide chain-refolding event occurs in the Gly82 variant of yeast iso-1-cytochrome c.
Topics: Amino Acid Sequence; Computer Simulation; Cytochrome c Group; Cytochromes c; Electron Transport; Fungal Proteins; Glycine; Heme; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Phenylalanine; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Structure-Activity Relationship; Water | 1989 |
Role of phenylalanine-82 in yeast iso-1-cytochrome c and remote conformational changes induced by a serine residue at this position.
Topics: Cytochrome c Group; Cytochromes c; Electron Transport; Heme; Mutation; Oxidation-Reduction; Phenylalanine; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Serine | 1988 |
Near-ultraviolet absorption bands of tryptophan. Studies using horseradish peroxidase isoenzymes, bovine and horse heart cytochrome c, and N-stearyl-L-tryptophan n-hexyl ester.
Topics: Animals; Cattle; Chemical Phenomena; Chemistry; Cold Temperature; Cyclohexanes; Cytochromes; Energy Transfer; Esters; Glycerol; Heme; Horses; Hydrogen-Ion Concentration; Indoles; Isoenzymes; Myocardium; Peroxidases; Phenylalanine; Plants; Spectrophotometry; Stearic Acids; Tryptophan; Tyrosine; Ultraviolet Rays | 1971 |
Cytochrome C and porphyrin--peptides. I. Characterization of cytochrome C and status of studies on its chemical synthesis.
Topics: Amino Acids; Animals; Apoproteins; Cattle; Chemical Phenomena; Chemistry; Cysteine; Cytochromes; Heart; Heme; Horses; Hydrolysis; Iron; Peptides; Phenylalanine; Porphyrins | 1971 |
[The oxygen affinity of Chironomus thummi erythrocruorins].
Topics: Animals; Blood Proteins; Cetacea; Chemical Phenomena; Chemistry; Chromatography, DEAE-Cellulose; Diptera; Heme; Histidine; Isoleucine; Myoglobin; Oxygen; Phenylalanine; X-Ray Diffraction | 1970 |
A new approach to haemoglobin variant identification. Haemoglobin Christchurch beta-71 (E15) phenylalanine leads to serine.
Topics: Adolescent; Amino Acid Sequence; Amino Acids; Anemia, Hemolytic; Anemia, Pernicious; Autoradiography; Carbon Isotopes; Chromatography, Thin Layer; Drug Stability; Electrophoresis; Erythrocytes; Female; Heme; Hemoglobinopathies; Hemoglobins; Hemoglobins, Abnormal; Hemolysis; Humans; Methods; New Zealand; Peptides; Phenylalanine; Serine | 1971 |
Excretion of delta-aminolevulinic acid in the absence of demonstrable erythropoiesis.
Topics: Adolescent; Amino Acids; Aminobutyrates; Ammonia; Anemia, Aplastic; Autoanalysis; Chemistry, Clinical; Child; Child, Preschool; Chromatography, Ion Exchange; Erythropoiesis; Heme; Histidine; Humans; Lead Poisoning; Levulinic Acids; Lysine; Middle Aged; Ornithine; Phenylalanine; Tyrosine | 1968 |
Peroxidase isoenzymes from horseradish roots. 3. Circular dichroism of isoenzymes and apoisoenzymes.
Topics: Binding Sites; Heme; Isoenzymes; Peroxidases; Phenylalanine; Plants; Spectrophotometry; Spectrum Analysis; Tryptophan; Tyrosine; Ultraviolet Rays | 1968 |
Bacteriochlorophyll and heme synthesis in Rhodopseudomonas spheroides: possible role of heme in regulation of the branched biosynthetic pathway.
Topics: Amino Acids; Azaguanine; Chlorophyll; Feedback; Heme; Iron Isotopes; Levulinic Acids; Molecular Biology; Mutation; Phenylalanine; Porphyrins; Puromycin; Rhodopseudomonas | 1969 |
Alkaline isomerization of ferricytochrome c: lysine is not replacing methionine at the sixth co-ordination site of the haem iron.
Topics: Acetylation; Amino Acids; Animals; Binding, Competitive; Cytochrome c Group; Heme; Hydrogen-Ion Concentration; Isomerism; Kinetics; Lysine; Methionine; Phenylalanine; Protein Conformation | 1981 |
Structure and heme environment of ferrocytochrome c553 from 1H NMR studies.
Topics: Cyanobacteria; Cytochrome c Group; Heme; Histidine; Magnetic Resonance Spectroscopy; Methionine; Phenylalanine; Protein Conformation; Tryptophan; Tyrosine | 1982 |
Increased release of delta-aminolevulinic acid from protein during inhibition of protein synthesis in heart: evidence for the extensive reutilization of heme in cardiac protein metabolism.
Topics: Aminolevulinic Acid; Animals; Cycloheximide; Heart; Heme; Levulinic Acids; Mice; Myocardium; Organ Culture Techniques; Phenylalanine; Proteins; Puromycin | 1980 |
Horseradish peroxidase His-42 --> Ala, His-42 --> Val, and Phe-41 --> Ala mutants. Histidine catalysis and control of substrate access to the heme iron.
Topics: Alanine; Animals; Catalysis; Cell Line; Heme; Histidine; Horseradish Peroxidase; Imines; Iron; Kinetics; Mutagenesis, Site-Directed; Phenylalanine; Recombinant Proteins; Spectrum Analysis; Spodoptera; Substrate Specificity; Sulfides; Sulfoxides; Valine | 1995 |
Effect of single-point mutations Phe41-->His and Phe143-->Glu on folding and catalytic properties of recombinant horseradish peroxidase expressed in E. coli.
Topics: Base Sequence; Binding Sites; Catalysis; Escherichia coli; Glutamic Acid; Heme; Histidine; Horseradish Peroxidase; Hydrogen Peroxide; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenylalanine; Point Mutation; Protein Folding; Recombinant Proteins; Structure-Activity Relationship | 1994 |
The role of tryptophan 97 of cytochrome P450 BM3 from Bacillus megaterium in catalytic function. Evidence against the 'covalent switching' hypothesis of P-450 electron transfer.
Topics: Alanine; Bacillus megaterium; Bacterial Proteins; Base Sequence; Catalysis; Circular Dichroism; Cytochrome P-450 Enzyme System; DNA Primers; Electron Spin Resonance Spectroscopy; Electron Transport; Escherichia coli; Heme; Mixed Function Oxygenases; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; NADPH-Ferrihemoprotein Reductase; Phenylalanine; Protein Structure, Secondary; Spectrophotometry, Ultraviolet; Tryptophan; Tyrosine | 1994 |
NMR studies of recombinant Coprinus peroxidase and three site-directed mutants. Implications for peroxidase substrate binding.
Topics: Amino Acid Sequence; Asparagine; Binding Sites; Coprinus; Glutamine; Heme; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Peroxidase; Phenylalanine; Recombinant Proteins; Substrate Specificity | 1994 |
Mutagenesis at a highly conserved phenylalanine in cytochrome P450 2E1 affects heme incorporation and catalytic activity.
Topics: Amino Acid Sequence; Animals; Catalysis; Conserved Sequence; Cytochrome P-450 CYP2E1; Cytochrome P-450 Enzyme System; Escherichia coli; Heme; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; NADP; Oxidoreductases, N-Demethylating; Phenylalanine; Rabbits; Structure-Activity Relationship | 1994 |
Putative functions of phenylalanine-350 of Pseudomonas putida cytochrome P-450cam.
Topics: Base Sequence; Cytochrome P-450 Enzyme System; Electron Transport; Escherichia coli; Ferredoxins; Heme; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Phenylalanine; Pseudomonas putida | 1994 |
Mutation of tyrosine-67 to phenylalanine in cytochrome c significantly alters the local heme environment.
Topics: Cytochrome c Group; Electron Transport; Escherichia coli; Heme; Hydrogen Bonding; Mutagenesis, Site-Directed; Oxidation-Reduction; Peptides; Phenylalanine; Protein Conformation; Saccharomyces cerevisiae; Tyrosine | 1994 |
1H NMR investigation of the heme cavity of elephant (E7 Gln) met-cyano-myoglobin. Evidence for a B-helix phenylalanine interaction with bound ligand.
Topics: Animals; Elephants; Glutamine; Heme; Ligands; Magnetic Resonance Spectroscopy; Metmyoglobin; Phenylalanine; Protein Conformation | 1993 |
Hb Saint Nazaire (beta 103[G5]Phe-->Ile): a new example of polycythemia due to a hemoglobin variant with increased oxygen affinity.
Topics: Adolescent; Adult; Aged; Amino Acids; Chromatography, High Pressure Liquid; Genetic Variation; Heme; Hemoglobins, Abnormal; Humans; Isoleucine; Leucine; Male; Mass Spectrometry; Middle Aged; Oxygen; Phenylalanine; Polycythemia | 1993 |
[Production and catalytic properties of point mutants Phe41--->His and Phe143--->Glu of horseradish peroxidase, expressed in Escherichia coli].
Topics: Amino Acid Sequence; Base Sequence; Catalysis; Cloning, Molecular; DNA, Recombinant; Enzyme Stability; Escherichia coli; Glutamic Acid; Heme; Histidine; Horseradish Peroxidase; Molecular Sequence Data; Oxidation-Reduction; Phenylalanine; Point Mutation | 1995 |
Enzyme-catalyzed dehalogenation of pentachloroethane: why F87W-cytochrome P450cam is faster than wild type.
Topics: Binding Sites; Camphor 5-Monooxygenase; Computer Simulation; Crystallography, X-Ray; Cytochrome P-450 Enzyme System; Ethane; Heme; Hydrocarbons, Chlorinated; Kinetics; Mixed Function Oxygenases; Models, Molecular; Phenylalanine; Point Mutation; Protein Conformation; Recombinant Proteins | 1995 |
Site-directed mutations at phenylalanine-190 of manganese peroxidase: effects on stability, function, and coordination.
Topics: Basidiomycota; Circular Dichroism; Electron Spin Resonance Spectroscopy; Enzyme Stability; Ferrocyanides; Heme; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Peroxidases; Phenylalanine; Polymerase Chain Reaction; Protein Denaturation; Spectrophotometry; Temperature | 1997 |
Mutagenesis of residues 27 and 78 modulates heme orientation in cytochrome b5.
Topics: Amino Acid Sequence; Animals; Cattle; Crystallography, X-Ray; Cytochromes b5; Heme; Magnetic Resonance Spectroscopy; Microsomes; Molecular Sequence Data; Mutagenesis, Site-Directed; Nicotiana; Phenylalanine; Plants, Toxic; Rats; Tyrosine | 1997 |
Identification of a critical phenylalanine residue in horseradish peroxidase, Phe179, by site-directed mutagenesis and 1H-NMR: implications for complex formation with aromatic donor molecules.
Topics: Benzoates; Benzoic Acid; Cyanides; Heme; Horseradish Peroxidase; Hydrogen-Ion Concentration; Hydroxamic Acids; Isoenzymes; Mutagenesis, Site-Directed; Mutation; Nuclear Magnetic Resonance, Biomolecular; Phenylalanine; Protons; Recombinant Proteins; Terminology as Topic | 1997 |
Computer simulations of carbon monoxide photodissociation in myoglobin: structural interpretation of the B states.
Topics: Animals; Biophysical Phenomena; Biophysics; Carbon Monoxide; Computer Simulation; Crystallography, X-Ray; Heme; Myoglobin; Phenylalanine; Photolysis; Point Mutation; Probability; Protein Conformation; Software; Spectrophotometry, Infrared; Static Electricity; Vibration; Whales | 1998 |
Solution and crystal structures of a sperm whale myoglobin triple mutant that mimics the sulfide-binding hemoglobin from Lucina pectinata.
Topics: Amino Acid Sequence; Animals; Binding Sites; Bivalvia; Crystallography, X-Ray; Glutamine; Heme; Hemoglobins; Hemoglobins, Abnormal; Models, Molecular; Mutagenesis, Site-Directed; Myoglobin; Nuclear Magnetic Resonance, Biomolecular; Phenylalanine; Point Mutation; Protein Conformation; Recombinant Proteins; Whales; X-Ray Diffraction | 1998 |
Functional implications of the proximal hydrogen-bonding network in myoglobin: a resonance Raman and kinetic study of Leu89, Ser92, His97, and F-helix swap mutants.
Topics: Animals; Heme; Histidine; Humans; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Leucine; Models, Molecular; Mutagenesis, Site-Directed; Myoglobin; Phenylalanine; Photolysis; Propionates; Protein Structure, Secondary; Spectrum Analysis, Raman; Whales | 1998 |
The post-translational modification in cytochrome c oxidase is required to establish a functional environment of the catalytic site.
Topics: Binding Sites; Catalysis; Electron Transport Complex IV; Heme; Ligands; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Protein Processing, Post-Translational; Rhodobacter sphaeroides; Spectrum Analysis, Raman; Tyrosine | 1998 |
Heme protein dynamics revealed by geminate nitric oxide recombination in mutants of iron and cobalt myoglobin.
Topics: Amino Acid Substitution; Animals; Cobalt; Heme; Iron; Isoleucine; Mutagenesis, Site-Directed; Myoglobin; Nitric Oxide; Phenylalanine; Thermodynamics; Whales | 1999 |
Recombinant hemoglobin(alpha 29leucine --> phenylalanine, alpha 96valine --> tryptophan, beta 108asparagine --> lysine) exhibits low oxygen affinity and high cooperativity combined with resistance to autoxidation.
Topics: Amino Acid Substitution; Asparagine; Carbon Monoxide; Electron Spin Resonance Spectroscopy; Heme; Hemoglobins; Humans; Kinetics; Leucine; Lysine; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Oxygen; Oxyhemoglobins; Phenylalanine; Protein Binding; Recombinant Proteins; Tryptophan; Valine | 1999 |
Proximal and distal effects on the coordination chemistry of ferric Scapharca homodimeric hemoglobin as revealed by heme pocket mutants.
Topics: Amino Acid Substitution; Animals; Bivalvia; Dimerization; Ferric Compounds; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Leucine; Phenylalanine; Point Mutation; Spectrophotometry; Spectrum Analysis, Raman; Ultracentrifugation; Valine | 2000 |
Modulation of the activities of catalase-peroxidase HPI of Escherichia coli by site-directed mutagenesis.
Topics: Amino Acid Substitution; Bacterial Proteins; Binding Sites; Catalase; Catalysis; Electron Spin Resonance Spectroscopy; Enzyme Activation; Enzyme Inhibitors; Escherichia coli; Escherichia coli Proteins; Heme; Leucine; Mass Spectrometry; Mutagenesis, Site-Directed; Peroxidases; Phenylalanine; Recombinant Proteins; Substrate Specificity; Tryptophan | 2000 |
Tryptophan-heme pi-electrostatic interactions in cytochrome f of oxygenic photosynthesis.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Chlamydomonas reinhardtii; Chloroplasts; Cyanobacteria; Cytochromes; Cytochromes f; Heme; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Photosynthesis; Static Electricity; Tryptophan; Tyrosine | 2000 |
Aromatic residues and neighboring Arg414 in the (6R)-5,6,7, 8-tetrahydro-L-biopterin binding site of full-length neuronal nitric-oxide synthase are crucial in catalysis and heme reduction with NADPH.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Arginine; Binding Sites; Biopterins; Catalysis; Dimerization; Drosophila; Glutamine; Heme; Humans; Hydrogen Bonding; Leucine; Mice; Models, Molecular; Molecular Sequence Data; NADP; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction; Phenylalanine; Rats; Spectrophotometry, Atomic; Structure-Activity Relationship; Tryptophan | 2000 |
Characterization of an alkaline transition intermediate stabilized in the Phe82Trp variant of yeast iso-1-cytochrome c.
Topics: Amino Acid Substitution; Cytochrome c Group; Cytochromes c; Electrochemistry; Electron Spin Resonance Spectroscopy; Enzyme Stability; Fungal Proteins; Heme; Hydrogen-Ion Concentration; Iron; Kinetics; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Phenylalanine; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrum Analysis, Raman; Structure-Activity Relationship; Tryptophan | 2000 |
Haem-linked interactions in horseradish peroxidase revealed by spectroscopic analysis of the Phe-221-->Met mutant.
Topics: Arabidopsis; Catalysis; Heme; Horseradish Peroxidase; Hydrogen-Ion Concentration; Hydroxamic Acids; Kinetics; Ligands; Magnetic Resonance Spectroscopy; Methionine; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Phenylalanine; Plasmids; Spectrum Analysis, Raman | 2001 |
Ligand migration in human myoglobin: steric effects of isoleucine 107(G8) on O(2) and CO binding.
Topics: Alanine; Amino Acid Substitution; Binding Sites; Heme; Humans; Isoleucine; Kinetics; Leucine; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Myoglobin; Phenylalanine; Protein Conformation; Recombinant Proteins; Thermodynamics; Valine | 2001 |
High-resolution structures of the oxidized and reduced states of cytochrome c554 from Nitrosomonas europaea.
Topics: Amino Acid Motifs; Amino Acid Sequence; Crystallography, X-Ray; Cytochrome c Group; Heme; Histidine; Models, Molecular; Molecular Sequence Data; Nitrosomonas; Oxidation-Reduction; Phenylalanine; Protein Conformation; Protein Folding | 2001 |
A structural role for tryptophan 188 of inducible nitric oxide synthase.
Topics: Amino Acid Substitution; Animals; Circular Dichroism; Heme; Mice; Mutagenesis, Site-Directed; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Nitric Oxide Synthase Type II; Phenylalanine; Protein Conformation; Spectrophotometry, Ultraviolet; Tryptophan | 2001 |
Phosphorylation of native and heme-modified CYP3A4 by protein kinase C: a mass spectrometric characterization of the phosphorylated peptides.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Chromatography, Liquid; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme System; Cytosol; Enzyme Inhibitors; Heme; Humans; Kinetics; Liver; Mass Spectrometry; Mixed Function Oxygenases; Models, Molecular; Mutagenesis; Okadaic Acid; Peptide Fragments; Phenylalanine; Phosphopeptides; Phosphorylation; Protein Conformation; Protein Kinase C; Protein Structure, Secondary; Rats; Recombinant Proteins; Sequence Deletion; Serine; Staurosporine | 2001 |
Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3.
Topics: Amino Acid Sequence; Bacterial Proteins; Carbon Monoxide; Cytochrome P-450 Enzyme System; Escherichia coli; Fatty Acids; Heme; Iron; Kinetics; Mixed Function Oxygenases; Molecular Sequence Data; Mutation; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Oxygen; Phenylalanine; Potentiometry; Sequence Homology, Amino Acid; Sulfur; Thermodynamics; Titrimetry | 2001 |
Fine-tuning of the binding and dissociation of CO by the amino acids of the heme pocket of Coprinus cinereus peroxidase.
Topics: Amino Acid Substitution; Amino Acids; Anions; Arginine; Asparagine; Aspartic Acid; Carbon Monoxide; Coprinus; Cytochrome-c Peroxidase; Ferrous Compounds; Heme; Kinetics; Ligands; Mutation; Peroxidase; Phenylalanine; Protein Binding; Spectrophotometry, Infrared; Spectrum Analysis, Raman | 2002 |
Spectroscopic characterization of five- and six-coordinate ferrous-NO heme complexes. Evidence for heme Fe-proximal cysteinate bond cleavage in the ferrous-NO adducts of the Trp-409Tyr/Phe proximal environment mutants of neuronal nitric oxide synthase.
Topics: Circular Dichroism; Cysteine; Electron Spin Resonance Spectroscopy; Ferric Compounds; Ferrous Compounds; Heme; Humans; Iron-Sulfur Proteins; Ligands; Mutagenesis, Site-Directed; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction; Phenylalanine; Protein Structure, Tertiary; Solvents; Spectrophotometry, Ultraviolet; Tryptophan; Tyrosine | 2003 |
Role of acidic and aromatic amino acids in Rhodobacter capsulatus cytochrome c1. A site-directed mutagenesis study.
Topics: Amino Acids; Animals; Cattle; Chickens; Cytochromes c1; Electron Spin Resonance Spectroscopy; Heme; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Photosynthesis; Protein Binding; Rhodobacter capsulatus; Tyrosine; Yeasts | 2003 |
HAEMPROTEINS IN HEART MICROSOMES. II. A POSSIBLE ROLE FOR HAEMPROTEOLIPID IN HAEMPROTEIN BIOSYNTHESIS.
Topics: Ascorbic Acid; Chloramphenicol; Dactinomycin; Heme; Hemeproteins; Iron; Iron Isotopes; Microsomes; Myocardium; NAD; Pharmacology; Phenylalanine; Porphyrins; Proteins; Research; Surface-Active Agents | 1965 |
Phe393 mutants of cytochrome P450 BM3 with modified heme redox potentials have altered heme vinyl and propionate conformations.
Topics: Amino Acid Substitution; Bacillus megaterium; Bacterial Proteins; Cytochrome P-450 Enzyme System; Ferric Compounds; Ferrous Compounds; Heme; Iron-Sulfur Proteins; Mixed Function Oxygenases; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Phenylalanine; Propionates; Protein Conformation; Protein Structure, Tertiary; Spectrum Analysis, Raman; Substrate Specificity; Tryptophan; Tyrosine; Vinyl Compounds | 2004 |
Horseradish peroxidase mutants that autocatalytically modify their prosthetic heme group: insights into mammalian peroxidase heme-protein covalent bonds.
Topics: Animals; Carboxylic Acids; Catalysis; Cell Line; Chromatography, High Pressure Liquid; Cloning, Molecular; DNA; Electrophoresis, Polyacrylamide Gel; Genetic Variation; Glutamic Acid; Glycine; Heme; Horseradish Peroxidase; Hydrogen Peroxide; Hydrogen-Ion Concentration; Insecta; Kinetics; Leucine; Mass Spectrometry; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Peroxidase; Phenylalanine; Porphyrins; Protein Structure, Secondary; Serine; Spectrophotometry; Time Factors; Ultraviolet Rays | 2004 |
Crystal structures of human cytochrome P450 3A4 bound to metyrapone and progesterone.
Topics: Binding Sites; Crystallization; Crystallography, X-Ray; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme System; Heme; Humans; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Ligands; Metyrapone; Models, Molecular; Phenylalanine; Progesterone; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Water | 2004 |
Redox characterization of Geobacter sulfurreducens cytochrome c7: physiological relevance of the conserved residue F15 probed by site-specific mutagenesis.
Topics: Amino Acid Substitution; Bacterial Proteins; Conserved Sequence; Cytochrome c Group; Desulfuromonas; Geobacter; Heme; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Phenylalanine; Protons; Spectrophotometry, Ultraviolet; Thermodynamics; Tyrosine | 2004 |
Roles of noncoordinated aromatic residues in redox regulation of cytochrome c3 from Desulfovibrio vulgaris Miyazaki F.
Topics: Amino Acid Sequence; Amino Acid Substitution; Amino Acids, Aromatic; Cytochrome c Group; Desulfovibrio vulgaris; Electrochemistry; Heme; Histidine; Leucine; Molecular Sequence Data; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Phenylalanine; Tyrosine | 2004 |
A relationship between heme binding and protein stability in cytochrome b5.
Topics: Animals; Aspartic Acid; Cytochromes b5; Heme; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Phenylalanine; Protein Binding; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Rats; Temperature; Thermodynamics; Urea | 2004 |
Hydroxyl radical oxidation of cytochrome c by aerobic radiolysis.
Topics: Aerobiosis; Amino Acid Sequence; Animals; Cytochromes c; Dose-Response Relationship, Radiation; Electrons; Heme; Horses; Hydroxyl Radical; Hydroxylation; Intracellular Membranes; Methionine; Mitochondria, Heart; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Peptide Fragments; Phenylalanine; Protein Conformation; Pulse Radiolysis; Rats; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrophotometry, Ultraviolet; Tyrosine | 2004 |
Steric effects of isoleucine 107 on heme reorientation reaction in human myoglobin.
Topics: Biochemistry; Heme; Hemin; Histidine; Humans; Isoleucine; Kinetics; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Structure; Myoglobin; Phenylalanine; Proteins; Spectrophotometry; Spectrum Analysis, Raman; Stereoisomerism; X-Rays | 2004 |
Effects of metal ions in the CuB center on the redox properties of heme in heme-copper oxidases: spectroelectrochemical studies of an engineered heme-copper center in myoglobin.
Topics: Amine Oxidase (Copper-Containing); Animals; Cations, Divalent; Cattle; Copper; Electron Transport; Electron Transport Complex IV; Heme; Histidine; Leucine; Myoglobin; Oxidation-Reduction; Phenylalanine; Potentiometry; Protein Engineering; Spectrophotometry, Ultraviolet; Whales; Zinc | 2005 |
Redox-dependent structural changes in an engineered heme-copper center in myoglobin: insights into chloride binding to CuB in heme copper oxidases.
Topics: Amino Acid Substitution; Animals; Binding Sites; Copper; Electrolysis; Electron Spin Resonance Spectroscopy; Ferric Compounds; Heme; Histidine; Hydroxides; Leucine; Myoglobin; Oxidation-Reduction; Phenylalanine; Potassium Chloride; Potentiometry; Spectrophotometry, Ultraviolet; Whales | 2005 |
A biophysical investigation of recombinant hemoglobins with aromatic B10 mutations in the distal heme pockets.
Topics: Adult; Amino Acid Substitution; Azides; Heme; Hemoglobin A; Hemoglobins; Humans; Leucine; Nitric Oxide; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Oxygen; Phenylalanine; Protein Binding; Protein Structure, Secondary; Recombinant Proteins; Thermodynamics; Tryptophan | 2005 |
ENDOR investigation of the liganding environment of mixed-spin ferric cytochrome c'.
Topics: Binding Sites; Coumarins; Cytochromes c'; Electron Spin Resonance Spectroscopy; Ferric Compounds; Heme; Histidine; Hydrogen; Hydrogen Bonding; Iron; Ligands; Nitrogen; Phenylalanine; Protons; Rhodobacter sphaeroides | 2005 |
Role of phenylalanine B10 in plant nonsymbiotic hemoglobins.
Topics: Animals; Azides; Carbon Monoxide; Crystallography, X-Ray; Heme; Hemoglobins; Iron; Ligands; Models, Molecular; Mutant Proteins; Oryza; Oxidation-Reduction; Oxygen; Phenylalanine; Potentiometry; Protein Binding; Spectroscopy, Fourier Transform Infrared; Symbiosis | 2006 |
Conformational dynamics of the cytochrome P450 BM3/N-palmitoylglycine complex: the proposed "proximal-distal" transition probed by temperature-jump spectroscopy.
Topics: Algorithms; Bacterial Proteins; Binding Sites; Crystallography, X-Ray; Cytochrome P-450 Enzyme System; Glycine; Heme; Iron; Magnetic Resonance Spectroscopy; Mixed Function Oxygenases; NADPH-Ferrihemoprotein Reductase; Palmitic Acids; Phenylalanine; Protein Conformation; Spectrophotometry, Ultraviolet; Spectrum Analysis | 2007 |
Roles of Arg-97 and Phe-113 in regulation of distal ligand binding to heme in the sensor domain of Ec DOS protein. Resonance Raman and mutation study.
Topics: Amino Acid Substitution; Arginine; Carbon Monoxide; Carrier Proteins; Escherichia coli; Escherichia coli Proteins; Heme; Hydrogen Bonding; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Mutation, Missense; Nitric Oxide; Phenylalanine; Phosphoric Diester Hydrolases; Protein Structure, Tertiary; Spectrum Analysis, Raman | 2008 |
Ligand binding to the Fe(III)-protoporphyrin IX complex of phosphodiesterase from Escherichia coli (Ec DOS) markedly enhances catalysis of cyclic di-GMP: roles of Met95, Arg97, and Phe113 of the putative heme distal side in catalytic regulation and ligand
Topics: Animals; Arginine; Catalysis; Cattle; Cyclic GMP; Escherichia coli Proteins; Ferric Compounds; Heme; Ligands; Methionine; Mutagenesis, Site-Directed; Phenylalanine; Phosphoric Diester Hydrolases; Protein Binding; Protein Structure, Tertiary; Protoporphyrins | 2008 |
Ultrafast proteinquake dynamics in cytochrome c.
Topics: Animals; Cytochromes c; Ferric Compounds; Ferrous Compounds; Heme; Horses; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Photolysis; Protein Conformation; Spectrophotometry, Ultraviolet; Thermodynamics; Tryptophan | 2009 |
Role of Phe113 at the distal side of the heme domain of an oxygen-sensor (Ec DOS) in the characterization of the heme environment.
Topics: Amino Acid Sequence; Carbon Monoxide; Crystallography, X-Ray; Cyanides; Escherichia coli; Escherichia coli Proteins; Heme; Molecular Sequence Data; Molecular Structure; Oxygen; Phenylalanine; Phosphoric Diester Hydrolases | 2009 |
Improved cytochrome P450 3A4 molecular models accurately predict the Phe215 requirement for raloxifene dehydrogenation selectivity.
Topics: Amino Acid Substitution; Catalytic Domain; Crystallography, X-Ray; Cytochrome P-450 CYP3A; Enzyme Activation; Heme; Humans; Models, Molecular; Phenylalanine; Protein Binding; Raloxifene Hydrochloride | 2010 |
Reduced catalytic activity of human CYP2C9 natural alleles for gliclazide: molecular dynamics simulation and docking studies.
Topics: Alleles; Aryl Hydrocarbon Hydroxylases; Binding Sites; Biocatalysis; Catalytic Domain; Cytochrome P-450 CYP2C9; Enzyme Stability; Genotype; Gliclazide; Heme; Humans; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Hydroxylation; Hypoglycemic Agents; Molecular Dynamics Simulation; Mutation; Phenylalanine; Protein Binding; Protein Structure, Tertiary | 2011 |
Topography of tyrosine residues and their involvement in peroxidation of polyunsaturated cardiolipin in cytochrome c/cardiolipin peroxidase complexes.
Topics: Animals; Cardiolipins; Computer Simulation; Cytochromes c; Electron Spin Resonance Spectroscopy; Heme; Horses; Hydrogen Peroxide; Iron; Magnetic Resonance Spectroscopy; Mitochondrial Membranes; Mutation; Myocardium; Oxygen; Oxygenases; Peroxidase; Peroxidases; Phenylalanine; Tyrosine | 2011 |
EPR investigation of the role of B10 phenylalanine in neuroglobin - evidence that B10Phe mediates structural changes in the heme region upon disulfide-bridge formation.
Topics: Brain; Cloning, Molecular; Cysteine; Disulfides; Electron Spin Resonance Spectroscopy; Escherichia coli; Globins; Heme; Humans; Hydrogen Peroxide; Kinetics; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Nerve Tissue Proteins; Neuroglobin; Oxidation-Reduction; Phenylalanine; Protein Binding; Protein Conformation; Recombinant Proteins; Spectrometry, Fluorescence; Transformation, Bacterial | 2011 |
Mutation of Phe413 to Tyr in catalase KatE from Escherichia coli leads to side chain damage and main chain cleavage.
Topics: Arginine; Catalase; Crystallography, X-Ray; Escherichia coli; Genetic Variation; Heme; Hydrogen Peroxide; Kinetics; Mass Spectrometry; Models, Molecular; Molecular Conformation; Mutation; Oxygen; Phenylalanine; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Tyrosine | 2012 |
Perturbation of the redox site structure of cytochrome c variants upon tyrosine nitration.
Topics: Cytochromes c; Fatty Acids; Heme; Humans; Iron; Kinetics; Lysine; Methionine; Mutation; Nitro Compounds; Oxidation-Reduction; Phenylalanine; Protein Stability; Protein Structure, Quaternary; Recombinant Proteins; Silver Compounds; Static Electricity; Sulfhydryl Compounds; Tyrosine; Water | 2012 |
Marked difference in the electronic structure of cyanide-ligated ferric protoglobins and myoglobin due to heme ruffling.
Topics: Animals; Electron Spin Resonance Spectroscopy; Electrons; Escherichia coli; Ferricyanides; Globins; Heme; Horses; Ligands; Methanosarcina; Myoglobin; Phenylalanine; Protein Conformation; Recombinant Proteins; Thermodynamics | 2012 |
Phe317 is essential for rubber oxygenase RoxA activity.
Topics: Amino Acid Substitution; Catalytic Domain; Heme; Latex; Mutagenesis, Site-Directed; Mutant Proteins; Oxygenases; Phenylalanine; Spectrophotometry, Ultraviolet; Xanthomonas | 2012 |
Mapping myeloperoxidase to identify its promiscuity properties using docking and molecular dynamics simulations.
Topics: 4-Aminobenzoic Acid; Animals; Anti-Inflammatory Agents, Non-Steroidal; Binding Sites; Catalytic Domain; Chemical Phenomena; Databases, Protein; Drug Design; Enzyme Inhibitors; Heme; Humans; Kinetics; Ligands; Molecular Conformation; Molecular Docking Simulation; Molecular Dynamics Simulation; Peroxidase; Phenylalanine; Structure-Activity Relationship; Substrate Specificity | 2013 |
Solution structure of a mutant of the triheme cytochrome PpcA from Geobacter sulfurreducens sheds light on the role of the conserved aromatic residue F15.
Topics: Cytochrome c Group; Geobacter; Heme; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; Mutant Proteins; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Periplasm; Phenylalanine; Protein Conformation; Thermodynamics | 2013 |
Solution structure and molecular determinants of hemoglobin binding of the first NEAT domain of IsdB in Staphylococcus aureus.
Topics: Amino Acid Sequence; Antigens, Bacterial; Cation Transport Proteins; Heme; Hemoglobins; Methemoglobin; Nuclear Magnetic Resonance, Biomolecular; Phenylalanine; Protein Structure, Tertiary; Receptors, Cell Surface; Staphylococcus aureus | 2014 |
Structural and functional characterization of a cytochrome P450 2B4 F429H mutant with an axial thiolate-histidine hydrogen bond.
Topics: Amino Acid Substitution; Aryl Hydrocarbon Hydroxylases; Binding Sites; Crystallography, X-Ray; Cytochrome P450 Family 2; Cytochromes b5; Electron Transport; Heme; Histidine; Hydrogen Bonding; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Mutant Proteins; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Phenylalanine; Protein Conformation; Recombinant Proteins; Structural Homology, Protein; Substrate Specificity; Thermodynamics | 2014 |
A novel tyrosine-heme C−O covalent linkage in F43Y myoglobin: a new post-translational modification of heme proteins.
Topics: Amino Acid Substitution; Animals; Crystallography, X-Ray; Heme; Hydrogen Peroxide; Models, Molecular; Myoglobin; Oxidation-Reduction; Phenylalanine; Protein Conformation; Protein Processing, Post-Translational; Solutions; Spectrophotometry; Tyrosine; Whales | 2015 |
Internal switches modulating electron tunneling currents in respiratory complex III.
Topics: Crystallography, X-Ray; Cytochromes c; Electron Transport; Electron Transport Complex III; Electrons; Heme; Models, Chemical; Models, Molecular; Molecular Structure; Mutation; Oxidation-Reduction; Phenylalanine; Protein Binding; Protein Conformation | 2016 |
[Research on Early Diagnosis of Gastric Cancer by the Surface Enhanced Raman Spectroscopy of Human Hemoglobin].
Topics: Asparagine; Early Detection of Cancer; Heme; Hemoglobins; Humans; Methemoglobin; Multivariate Analysis; Oxyhemoglobins; Phenylalanine; Principal Component Analysis; Spectrum Analysis, Raman; Stomach Neoplasms; Tyrosine | 2015 |
Exploring the Role of Phenylalanine Residues in Modulating the Flexibility and Topography of the Active Site in the Peroxygenase Variant PaDa-I.
Topics: Agrocybe; Biocatalysis; Catalytic Domain; Heme; Hydrogen Peroxide; Mixed Function Oxygenases; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Mutation; Phenylalanine; Saccharomyces cerevisiae | 2020 |
Electron transfer pathways from quantum dynamics simulations.
Topics: Electron Transport; Heme; Models, Chemical; Molecular Dynamics Simulation; Peroxidases; Phenylalanine; Quantum Theory; Trypanosoma cruzi; Tryptophan | 2020 |
Group II truncated haemoglobin YjbI prevents reactive oxygen species-induced protein aggregation in
Topics: Bacillus subtilis; Bacterial Proteins; Biofilms; Heme; Hydrogen Peroxide; Hypochlorous Acid; Membrane Proteins; Oxidoreductases; Peroxidases; Phenylalanine; Protein Aggregates; Serum Albumin, Bovine; Truncated Hemoglobins; Water | 2022 |
Differential Effects of Clotrimazole on X-Ray Crystal Structures of Human Cytochromes P450 3A5 and 3A4.
Topics: Clotrimazole; Cytochrome P-450 CYP3A; Heme; Humans; Iron; Phenylalanine; X-Rays | 2023 |