Compounds > aspartic acid
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aspartic acid and heme

aspartic acid has been researched along with heme in 74 studies

Research

Studies (74)

TimeframeStudies, this research(%)All Research%
pre-19908 (10.81)18.7374
1990's16 (21.62)18.2507
2000's38 (51.35)29.6817
2010's11 (14.86)24.3611
2020's1 (1.35)2.80

Authors

AuthorsStudies
Erman, JE; Kraut, J; Mauro, JM; Miller, MA; Vitello, LB1
Erman, JE; Kraut, J; Mauro, JM; Satterlee, JD1
Boxer, SG; Gray, HB; Varadarajan, R; Zewert, TE1
Dreybrodt, W; el Naggar, S; Schweitzer-Stenner, R1
Baldassare, JJ; Bunn, HF; Ho, C; Lindstrom, TR1
Joubert, SM; Shanley, BC1
Jardetzky, O; Roberts, GC1
Barlow, GH; Campbell, LL; Drucker, H; Margoliash, E; Trousil, EB1
Dus, K; Erbes, DL; Gunsalus, IC; Katagiri, M; Yu, CA1
Imai, K1
Floris, R; Glumoff, T; Lundell, TK; Piontek, K; Schoemaker, HE; Winterhalter, KH1
Banci, L; Bertini, I; Ferrer, JC; Mauk, AG; Morris, IK; Smith, KM; Smith, M; Turano, P1
Goodin, DB; McRee, DE1
Marzocchi, MP; Neri, F; Smulevich, G; Welinder, KG1
Yamamoto, Y1
Bijloo, GJ; de Groot, MJ; Martens, BJ; van Acker, FA; Vermeulen, NP1
Fei, MJ; Inoue, N; Libeu, CP; Mizushima, T; Nakashima, R; Shinzawa-Itoh, K; Tomizaki, T; Tsukihara, T; Yamaguchi, H; Yamashita, E; Yao, M; Yaono, R; Yoshikawa, S1
Berka, V; Chen, PF; Tsai, AL; Wu, KK1
Behr, J; Grzybek, S; Hellwig, P; Ludwig, B; Mäntele, W; Michel, H1
Bjerrum, MJ; Gleich, GJ; Højrup, P; Overgaard, MT; Oxvig, C; Sorensen, ES; Sottrup-Jensen, L; Thomsen, AR1
Lu, Y; Wang, X1
Buse, G; Hellwig, P; Mäntele, W; Soulimane, T1
Bollen, A; Dekker, HL; Kooter, IM; Moguilevsky, N; Otto, C; Sijtsema, NM; Wever, R1
Dawson, JH; Lu, Y; Pond, AE; Sigman, JA1
Adachi, S; Arakawa, H; Gomi, Y; Nakamura, H; Obayashi, E; Park, SY; Shimizu, H; Shiro, Y; Shoun, H1
Ferguson-Miller, S; Florens, L; Hiser, C; Mills, DA; Qian, J1
Adak, S; Johnson, JD; Santolini, J; Stuehr, DJ; Tikunova, S; Wang, Q1
Green, BA; Reilly, TJ; Smith, AL; Zlotnick, GW1
Fujii, H; Ikeda-Saito, M; Tomita, T; Yoshida, T; Zhang, X1
Bollen, A; Ferrari, RP; Ghibaudi, EM; Moguilevsky, N; Suriano, G; Watanabe, S1
Colas, C; Kuo, JM; Ortiz de Montellano, PR1
Davydov, R; Fujii, H; Hoffman, BM; Ikeda-Saito, M; Kofman, V; Yoshida, T1
Jones, DK; Patel, N; Raven, EL1
Banerjee, R; Blom, H; Boers, GH; Evande, R1
Ciaccio, C; Coletta, M; De Sanctis, G; Feis, A; Neri, F; Santoni, E; Smulevich, G; Welinder, KG1
Brzezinski, P; Ferguson-Miller, S; Gennis, RB; Mills, D; Morgan, J; Namslauer, A; Pawate, AS1
Chu, GC; Ikeda-Saito, M; Li, Y; Mar, GN; Syvitski, RT1
Auer, M; Furtmüller, PG; Jakopitsch, C; Jantschko, W; Obinger, C; Regelsberger, G; Rüker, F1
Littlejohn, TK; Takikawa, O; Truscott, RJ; Walker, MJ1
Chen, JJ; Han, AP; Rafie-Kolpin, M1
Carpena, X; Chelikani, P; Fita, I; Loewen, PC1
Aoyama, H; Ishimura, Y; Katayama, Y; Mochizuki, M; Muramoto, K; Shimada, H; Shimokata, K; Shinzawa-Itoh, K; Tsukihara, T; Yamashita, E; Yao, M; Yoshikawa, S1
Adak, S; Konas, D; Panda, K; Sharma, M; Stuehr, DJ1
Brunori, M; D'Itri, E; Forte, E; Giuffrè, A; Ludwig, B; Richter, OM; Sarti, P; Scandurra, FM1
Fushinobu, S; Shoun, H; Su, F; Takaya, N1
Bidwai, A; Clarke, TA; Im, SC; Waskell, L1
Kurokawa, H; Sagami, I; Shimizu, T; Watanabe, M; Yoshimura-Suzuki, T1
Lecomte, JT; Mukhopadhyay, K1
Furukawa, M; Ikeda-Saito, M; Matsui, T; Tomita, T; Unno, M1
Furtmüller, PG; Jakopitsch, C; Jantschko, W; Moguilevsky, N; Neugschwandtner, K; Obinger, C; Zederbauer, M1
Blaney, FE; Bridges, AM; Chenery, RJ; Eggleston, DS; Jones, JJ; Lewis, CJ; Leydon, VR; Modi, S; Oxbrow, AK; Rowland, P; Smyth, MG; Tennant, MG1
Chait, BT; Fushitani, K; Gorr, TA; Kao, WY; Knapp, JE; Qin, J; Riggs, AF; Riggs, CK; Smith, SS1
Carpena, X; Deemagarn, T; Fita, I; Ivancich, A; Loewen, PC; Wiseman, B1
Christensen, O; Ferguson, SJ; Harvat, EM; Stevens, JM; Thöny-Meyer, L1
Battistuzzi, G; Bellei, M; Furtmüller, PG; Jakopitsch, C; Moguilevsky, N; Obinger, C; Stampler, J; Zederbauer, M1
Altun, A; Shaik, S; Thiel, W1
Baer, BR; Kunze, KL; Rettie, AE1
Böhm, A; Hellwig, P; Ludwig, B; Mäntele, W; Pfitzner, U1
Heimdal, J; Rydberg, P; Ryde, U1
de Visser, SP; Straganz, GD1
Bloch, DA; Rauhamäki, V; Verkhovsky, MI; Wikström, M1
Gorres, KL; Pua, KH; Raines, RT1
Baskaran, P; Beuve, A; Heckler, EJ; van den Akker, F1
Hisabori, T; Konno, H; Sugano, Y; Tsuge, H; Yoshida, T1
Gilles-Gonzalez, MA; Gondim, AC; Gonzalez, G; Sousa, EH; Tuckerman, JR1
Alayash, AI; Hicks, WA; Kassa, T; Mollan, TL; Olson, JS; Singleton, E; Soman, J; Strader, MB; Weiss, MJ; Wilson, MT1
Chauhan, VS; Kumari, P; Sahal, D1
Fojtikova, V; Kavan, D; Man, P; Martínek, V; Martinkova, M; Shimizu, T; Stranava, M; Vaněk, O1
Amartely, H; Dvir, H; Kornitzer, D; Nasser, L; Pinsky, M; Weissman, Z1
Iqbal, N; Kaur, P; Sharma, S; Singh, PK; Singh, TP; Sirohi, HV; Tiwari, P1
Cui, Y; Gu, L; Liu, S; Liu, X; Ma, Y; Wang, J; Xu, S; Yuan, Z1
Dojun, N; Ishimori, K; Sekine, Y; Uchida, T1
Baymeeva, NV; Miroshnichenko, II; Safarova, TP; Shipilova, ES; Yakovleva, OB1
Feng, C; Li, J; Zheng, H1

Reviews

2 review(s) available for aspartic acid and heme

ArticleYear
Nuclear magnetic resonance spectroscopy of amino acids, peptides, and proteins.
    Advances in protein chemistry, 1970, Volume: 24

    Topics: Amides; Amino Acids; Antibodies; Aspartic Acid; Chemical Phenomena; Chemistry; Choline; Chymotrypsin; Copper; Heme; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Metals; Muramidase; Peptides; Protein Binding; Protein Denaturation; Proteins; Ribonucleases; Serum Albumin; Staphylococcus; Transferases

1970
Where is 'outside' in cytochrome c oxidase and how and when do protons get there?
    Biochimica et biophysica acta, 2000, May-12, Volume: 1458, Issue:1

    Topics: Aspartic Acid; Binding Sites; Electron Transport Complex IV; Heme; Lysine; Models, Molecular; Mutation; Oxidation-Reduction; Propionates; Proton Pumps; Proton-Motive Force; Protons; Rhodobacter sphaeroides

2000

Other Studies

72 other study(ies) available for aspartic acid and heme

ArticleYear
Effect of Asp-235-->Asn substitution on the absorption spectrum and hydrogen peroxide reactivity of cytochrome c peroxidase.
    Biochemistry, 1992, Nov-24, Volume: 31, Issue:46

    Topics: Asparagine; Aspartic Acid; Buffers; Cytochrome-c Peroxidase; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; Nitrates; Phosphates; Spectrum Analysis

1992
Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235----Asn-235 mutant.
    Biochemistry, 1990, Sep-18, Volume: 29, Issue:37

    Topics: Asparagine; Aspartic Acid; Cytochrome-c Peroxidase; Escherichia coli; Fungal Proteins; Heme; Magnetic Resonance Spectroscopy; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Fusion Proteins; Saccharomyces cerevisiae

1990
Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobin.
    Science (New York, N.Y.), 1989, Jan-06, Volume: 243, Issue:4887

    Topics: Asparagine; Aspartic Acid; Glutamates; Glutamic Acid; Heme; Humans; Mutation; Myoglobin; Oxidation-Reduction; Protein Conformation; Recombinant Proteins; Thermodynamics; Valine

1989
Haem-apoprotein interactions detected by resonance Raman scattering in Mb- and Hb-derivates lacking the saltbridge His146 beta-Asp94 beta.
    European biophysics journal : EBJ, 1985, Volume: 12, Issue:1

    Topics: Animals; Apoproteins; Aspartic Acid; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Myoglobin; Spectrum Analysis, Raman; Structure-Activity Relationship; Whales

1985
Nuclear magnetic resonance and spin-label studies of hemoglobin Kempsey.
    Biochemistry, 1973, Oct-09, Volume: 12, Issue:21

    Topics: Asparagine; Aspartic Acid; Australia; Carboxyhemoglobin; Cyclic N-Oxides; Electron Spin Resonance Spectroscopy; Heme; Hemoglobins; Hemoglobins, Abnormal; Humans; Inositol; Iodoacetates; Ligands; Magnetic Resonance Spectroscopy; Mutation; Organophosphorus Compounds; Piperidines; Protein Conformation; Spin Labels

1973
Transfer of hydrogen via tricarboxylic acid cycle activity to liver aspartate and glutamate in normal rats and to liver haem in normal and in allylisopropylacetamide-treated rats.
    Enzyme, 1973, Volume: 16, Issue:1

    Topics: Acetamides; Allylisopropylacetamide; Animals; Aspartic Acid; Citric Acid Cycle; Ethanol; Female; Glutamates; Glycine; Heme; Hydrogen; Liver; Malates; Propionates; Rats; Succinates; Tritium

1973
Amino acid composition, heme content, and molecular weight of cytochrome c3 of Desulfovibrio desulfuricans and Desulfovibrio vulgaris.
    Biochemistry, 1970, Mar-31, Volume: 9, Issue:7

    Topics: Amino Acids; Arginine; Aspartic Acid; Cytochromes; Desulfovibrio; Glutamates; Heme; Hydrogen-Ion Concentration; Isoleucine; Molecular Weight

1970
Chemical characterization of cytochrome P-450cam.
    Biochemical and biophysical research communications, 1970, Sep-30, Volume: 40, Issue:6

    Topics: Amino Acid Sequence; Amino Acids; Asparagine; Aspartic Acid; Autoanalysis; Camphor; Carbohydrates; Carboxypeptidases; Chemical Phenomena; Chemistry; Cytochromes; Formates; Heme; Hydrazines; Hydrogen-Ion Concentration; Isoelectric Focusing; Isoflurophate; Molecular Weight; Nitrobenzenes; Peptides; Porphyrins; Pseudomonas; Valine

1970
Oxygen-equilibrium characteristics of abnormal hemoglobin Hiroshima (alpha-2 beta-2 143 Asp).
    Archives of biochemistry and biophysics, 1968, Sep-20, Volume: 127, Issue:1

    Topics: Aspartic Acid; Chemical Phenomena; Chemistry; Electrophoresis; Genetic Variation; Heme; Hemoglobins; Hemoglobins, Abnormal; Hemolysis; Histidine; Humans; Hydrogen-Ion Concentration; Japan; Molecular Biology; Oxygen; Peptides; Spectrophotometry

1968
Do carbohydrates play a role in the lignin peroxidase cycle? Redox catalysis in the endergonic region of the driving force.
    Bioorganic & medicinal chemistry, 1994, Volume: 2, Issue:6

    Topics: Aspartic Acid; Benzyl Alcohols; Binding Sites; Carbohydrates; Electron Transport; Glycoproteins; Heme; Hydrogen Bonding; Kinetics; Models, Theoretical; Oxidation-Reduction; Peroxidases; Protein Conformation; Thermodynamics

1994
Active site coordination chemistry of the cytochrome c peroxidase Asp235Ala variant: spectroscopic and functional characterization.
    Biochemistry, 1994, Jun-28, Volume: 33, Issue:25

    Topics: Alanine; Aspartic Acid; Base Sequence; Binding Sites; Cytochrome-c Peroxidase; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Iron; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Recombinant Proteins; Spectrum Analysis; Structure-Activity Relationship; Temperature; Tryptophan

1994
The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme.
    Biochemistry, 1993, Apr-06, Volume: 32, Issue:13

    Topics: Aspartic Acid; Binding Sites; Crystallography; Cytochrome-c Peroxidase; DNA Mutational Analysis; Electron Spin Resonance Spectroscopy; Ferric Compounds; Free Radicals; Heme; Histidine; Hydrogen Bonding; In Vitro Techniques; Kinetics; Models, Molecular; Oxidation-Reduction; Recombinant Proteins; Structure-Activity Relationship; Tryptophan; X-Ray Diffraction

1993
Versatility of heme coordination demonstrated in a fungal peroxidase. Absorption and resonance Raman studies of Coprinus cinereus peroxidase and the Asp245-->Asn mutant at various pH values.
    Biochemistry, 1996, Aug-13, Volume: 35, Issue:32

    Topics: Asparagine; Aspartic Acid; Catalysis; Coprinus; Ferrous Compounds; Heme; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; Peroxidases; Spectrum Analysis, Raman

1996
1H-NMR study of inter-segmental hydrogen bonds in sperm whale and horse apomyoglobins.
    European journal of biochemistry, 1997, Jan-15, Volume: 243, Issue:1-2

    Topics: Animals; Apoproteins; Aspartic Acid; Guanidine; Guanidines; Heme; Histidine; Horses; Hydrogen Bonding; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Myoglobin; Protein Conformation; Protein Denaturation; Temperature; Whales

1997
A refined substrate model for human cytochrome P450 2D6.
    Chemical research in toxicology, 1997, Volume: 10, Issue:1

    Topics: Aspartic Acid; Binding Sites; Cytochrome P-450 CYP2D6; Heme; Humans; Models, Molecular; Oxidation-Reduction; Protein Conformation; Substrate Specificity

1997
Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase.
    Science (New York, N.Y.), 1998, Jun-12, Volume: 280, Issue:5370

    Topics: Animals; Aspartic Acid; Azides; Binding Sites; Carbon Monoxide; Cattle; Copper; Crystallography, X-Ray; Electron Transport Complex IV; Heme; Hydrogen Bonding; Hydrogen Peroxide; Hydrogen-Ion Concentration; Ligands; Metals; Models, Chemical; Models, Molecular; Myocardium; Oxidation-Reduction; Oxygen; Protein Conformation; Proton Pumps; Tyrosine

1998
Effects of Asp-369 and Arg-372 mutations on heme environment and function in human endothelial nitric-oxide synthase.
    The Journal of biological chemistry, 1998, Dec-18, Volume: 273, Issue:51

    Topics: Amino Acid Sequence; Amino Acid Substitution; Arginine; Aspartic Acid; Carbon Monoxide; Catalytic Domain; DNA Primers; Heme; Humans; Imidazoles; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Nitric Oxide Synthase Type II; Nitric Oxide Synthase Type III; Recombinant Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Spectrophotometry

1998
Electrochemical and ultraviolet/visible/infrared spectroscopic analysis of heme a and a3 redox reactions in the cytochrome c oxidase from Paracoccus denitrificans: separation of heme a and a3 contributions and assignment of vibrational modes.
    Biochemistry, 1999, Feb-09, Volume: 38, Issue:6

    Topics: Arginine; Aspartic Acid; Electrochemistry; Electron Transport Complex IV; Glutamic Acid; Heme; Molecular Conformation; Oxidation-Reduction; Paracoccus denitrificans; Porphyrins; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Tyrosine

1999
Biochemical evidence for heme linkage through esters with Asp-93 and Glu-241 in human eosinophil peroxidase. The ester with Asp-93 is only partially formed in vivo.
    The Journal of biological chemistry, 1999, Jun-11, Volume: 274, Issue:24

    Topics: Amino Acid Sequence; Aspartic Acid; Chromatography, High Pressure Liquid; Eosinophil Peroxidase; Eosinophils; Esters; Glutamic Acid; Heme; Humans; Lactoperoxidase; Molecular Sequence Data; Oligopeptides; Peroxidases; Sequence Analysis

1999
Proton NMR investigation of the heme active site structure of an engineered cytochrome c peroxidase that mimics manganese peroxidase.
    Biochemistry, 1999, Jul-13, Volume: 38, Issue:28

    Topics: Arginine; Aspartic Acid; Binding Sites; Cyanides; Cytochrome-c Peroxidase; Glutamic Acid; Glycine; Heme; Histidine; Leucine; Molecular Mimicry; Nuclear Magnetic Resonance, Biomolecular; Peroxidases; Protein Engineering; Protons; Spectrophotometry; Valine

1999
Electrochemical, FTIR, and UV/VIS spectroscopic properties of the ba(3) oxidase from Thermus thermophilus.
    Biochemistry, 1999, Jul-27, Volume: 38, Issue:30

    Topics: Arginine; Aspartic Acid; Buffers; Cytochrome b Group; Deuterium Oxide; Electrochemistry; Electron Transport Complex IV; Glutamic Acid; Heme; Lysine; Oxidation-Reduction; Peptides; Phosphates; Porphyrins; Potentiometry; Propionates; Protein Conformation; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Thermus thermophilus; Tyrosine; Water

1999
Characterization of the Asp94 and Glu242 mutants in myeloperoxidase, the residues linking the heme group via ester bonds.
    European journal of biochemistry, 1999, Volume: 264, Issue:1

    Topics: Aspartic Acid; Esters; Glutamic Acid; Heme; Kinetics; Mutagenesis, Site-Directed; Peroxidase; Spectrum Analysis, Raman

1999
Engineering cytochrome c peroxidase into cytochrome P450: a proximal effect on heme-thiolate ligation.
    Biochemistry, 1999, Aug-24, Volume: 38, Issue:34

    Topics: Aspartic Acid; Circular Dichroism; Cysteine; Cytochrome c Group; Cytochrome P-450 Enzyme System; Cytochrome-c Peroxidase; Cytochromes c; Electron Spin Resonance Spectroscopy; Escherichia coli; Ferric Compounds; Heme; Histidine; Imidazoles; Leucine; Ligands; Mutagenesis, Site-Directed; Protein Engineering; Spectrophotometry, Ultraviolet

1999
Proton delivery in NO reduction by fungal nitric-oxide reductase. Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes.
    The Journal of biological chemistry, 2000, Feb-18, Volume: 275, Issue:7

    Topics: Aspartic Acid; Base Sequence; Catalysis; Crystallography, X-Ray; DNA Primers; Ferric Compounds; Fusarium; Heme; Hydrogen Bonding; Kinetics; Models, Molecular; Molecular Structure; Mutagenesis, Site-Directed; Nitric Oxide; Oxidation-Reduction; Oxidoreductases; Protons; Serine

2000
Neuronal nitric-oxide synthase mutant (Ser-1412 --> Asp) demonstrates surprising connections between heme reduction, NO complex formation, and catalysis.
    The Journal of biological chemistry, 2001, Jan-12, Volume: 276, Issue:2

    Topics: Amino Acid Substitution; Aspartic Acid; Binding Sites; Calmodulin; Catalysis; Cytochrome c Group; Glycine max; Heme; Kinetics; Mutagenesis, Site-Directed; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction; Polymerase Chain Reaction; Recombinant Proteins; Serine

2001
Contribution of the DDDD motif of H. influenzae e (P4) to phosphomonoesterase activity and heme transport.
    FEBS letters, 2001, Apr-06, Volume: 494, Issue:1-2

    Topics: Aspartic Acid; Bacterial Outer Membrane Proteins; Binding Sites; Biological Transport; Escherichia coli; Esterases; Haemophilus influenzae; Heme; Lipoproteins; Mutagenesis, Site-Directed; Phosphoric Monoester Hydrolases

2001
A role for highly conserved carboxylate, aspartate-140, in oxygen activation and heme degradation by heme oxygenase-1.
    Journal of the American Chemical Society, 2001, Jul-11, Volume: 123, Issue:27

    Topics: Animals; Aspartic Acid; Carboxylic Acids; Catalytic Domain; Conserved Sequence; Heme; Heme Oxygenase (Decyclizing); Heme Oxygenase-1; Hydrogen Peroxide; Hydrolysis; Mutation; NADPH-Ferrihemoprotein Reductase; Oxygen; Rats; Recombinant Proteins

2001
Glu375Gln and Asp225Val mutants: about the nature of the covalent linkages between heme group and apo-Protein in bovine lactoperoxidase.
    Bioorganic & medicinal chemistry letters, 2001, Nov-05, Volume: 11, Issue:21

    Topics: Amino Acid Substitution; Animals; Aspartic Acid; Base Sequence; Blotting, Western; Cattle; CHO Cells; Cricetinae; DNA Primers; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Glutamic Acid; Glycine; Heme; Lactoperoxidase; Mutation; Valine

2001
Asp-225 and glu-375 in autocatalytic attachment of the prosthetic heme group of lactoperoxidase.
    The Journal of biological chemistry, 2002, Mar-01, Volume: 277, Issue:9

    Topics: Animals; Aspartic Acid; Binding Sites; Catalysis; Cattle; Cell Line; Chromatography, High Pressure Liquid; Cloning, Molecular; Cross-Linking Reagents; Electrophoresis, Polyacrylamide Gel; Gas Chromatography-Mass Spectrometry; Glutamic Acid; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Insecta; Iron; Lactoperoxidase; Models, Chemical; Models, Molecular; Mutation; Porphyrins; Protein Conformation; Protoporphyrins; Recombinant Proteins; Spectrophotometry

2002
Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutants.
    Journal of the American Chemical Society, 2002, Feb-27, Volume: 124, Issue:8

    Topics: Aspartic Acid; Catalysis; Electron Spin Resonance Spectroscopy; Heme; Heme Oxygenase (Decyclizing); Models, Molecular; Mutation; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction

2002
Redox control in heme proteins: electrostatic substitution in the active site of leghemoglobin.
    Archives of biochemistry and biophysics, 2002, Apr-01, Volume: 400, Issue:1

    Topics: Aspartic Acid; Binding Sites; Circular Dichroism; Electrochemistry; Glycine max; Heme; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Leghemoglobin; Leucine; Models, Chemical; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Binding; Recombinant Proteins; Spectrophotometry; Spectrum Analysis, Raman; Time Factors

2002
Alleviation of intrasteric inhibition by the pathogenic activation domain mutation, D444N, in human cystathionine beta-synthase.
    Biochemistry, 2002, Oct-01, Volume: 41, Issue:39

    Topics: Allosteric Regulation; Amino Acid Substitution; Asparagine; Aspartic Acid; Carbon Monoxide; Cell Line; Cystathionine beta-Synthase; Enzyme Activation; Ferrous Compounds; Fibroblasts; Heme; Humans; Kinetics; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Recombinant Proteins; RNA, Messenger; S-Adenosylmethionine

2002
Fine-tuning of the binding and dissociation of CO by the amino acids of the heme pocket of Coprinus cinereus peroxidase.
    Biochemistry, 2002, Nov-05, Volume: 41, Issue:44

    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
A mutation in subunit I of cytochrome oxidase from Rhodobacter sphaeroides results in an increase in steady-state activity but completely eliminates proton pumping.
    Biochemistry, 2002, Nov-12, Volume: 41, Issue:45

    Topics: Amino Acid Substitution; Asparagine; Aspartic Acid; Cold Temperature; Electron Transport Complex IV; Enzyme Activation; Heme; Kinetics; Mutagenesis, Site-Directed; Oxidation-Reduction; Photolysis; Proton Pumps; Rhodobacter sphaeroides; Spectrophotometry, Ultraviolet

2002
Solution 1H NMR investigation of the active site molecular and electronic structures of substrate-bound, cyanide-inhibited HmuO, a bacterial heme oxygenase from Corynebacterium diphtheriae.
    The Journal of biological chemistry, 2003, Feb-28, Volume: 278, Issue:9

    Topics: Animals; Aspartic Acid; Bacterial Proteins; Binding Sites; Catalysis; Corynebacterium diphtheriae; Crystallography, X-Ray; Cyanides; Heme; Heme Oxygenase (Decyclizing); Humans; Hydrogen; Hydrogen Bonding; Hydrogen-Ion Concentration; Ligands; Magnetic Resonance Spectroscopy; Protein Binding; Protons; Water

2003
Distal site aspartate is essential in the catalase activity of catalase-peroxidases.
    Biochemistry, 2003, May-13, Volume: 42, Issue:18

    Topics: Amino Acid Sequence; Aspartic Acid; Bacterial Proteins; Catalase; Catalysis; Circular Dichroism; Cyanobacteria; Escherichia coli; Heme; Hydrogen Peroxide; Kinetics; Models, Chemical; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Peroxidases; Recombinant Proteins; Sequence Homology, Amino Acid; Spectrophotometry, Ultraviolet

2003
Asp274 and his346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase.
    The Journal of biological chemistry, 2003, Aug-08, Volume: 278, Issue:32

    Topics: Alanine; Amino Acid Sequence; Animals; Aspartic Acid; Blotting, Western; Catalysis; Cell Division; Circular Dichroism; Cytokines; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Heme; Histidine; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Interferon-gamma; Kinetics; Ligands; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Plasmids; Protein Binding; Protein Conformation; Rats; Sequence Homology, Amino Acid; Tryptophan; Tryptophan Oxygenase; Ultraviolet Rays; Up-Regulation

2003
Autophosphorylation of threonine 485 in the activation loop is essential for attaining eIF2alpha kinase activity of HRI.
    Biochemistry, 2003, Jun-03, Volume: 42, Issue:21

    Topics: Alanine; Amino Acid Sequence; Aspartic Acid; Blotting, Western; Cell Line; Chromatography, Thin Layer; Dose-Response Relationship, Drug; eIF-2 Kinase; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Eukaryotic Initiation Factor-2; Heme; Hemin; Humans; Models, Biological; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Peptides; Phosphorylation; Protein Structure, Tertiary; Threonine; Trypsin

2003
An electrical potential in the access channel of catalases enhances catalysis.
    The Journal of biological chemistry, 2003, Aug-15, Volume: 278, Issue:33

    Topics: Arginine; Aspartic Acid; Catalase; Catalysis; Electrochemistry; Escherichia coli; Heme; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Valine

2003
The low-spin heme of cytochrome c oxidase as the driving element of the proton-pumping process.
    Proceedings of the National Academy of Sciences of the United States of America, 2003, Dec-23, Volume: 100, Issue:26

    Topics: Animals; Aspartic Acid; Cattle; Electron Transport Complex IV; Heme; Humans; Kinetics; Mitochondria, Heart; Models, Molecular; Oxidation-Reduction; Protein Conformation; Protein Subunits; Protons; X-Ray Diffraction

2003
A conserved aspartate (Asp-1393) regulates NADPH reduction of neuronal nitric-oxide synthase: implications for catalysis.
    The Journal of biological chemistry, 2004, Apr-30, Volume: 279, Issue:18

    Topics: Amino Acid Substitution; Animals; Aspartic Acid; Catalysis; Conserved Sequence; Electron Transport; Flavins; Heme; Kinetics; NADP; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction; Protein Binding; Rats; Spectrometry, Fluorescence

2004
Proton uptake upon anaerobic reduction of the Paracoccus denitrificans cytochrome c oxidase: a kinetic investigation of the K354M and D124N mutants.
    Biochemistry, 2004, Mar-16, Volume: 43, Issue:10

    Topics: Amino Acid Substitution; Anaerobiosis; Asparagine; Aspartic Acid; Calibration; Electron Transport Complex IV; Heme; Lysine; Methionine; Oxidation-Reduction; Paracoccus denitrificans; Phenolsulfonphthalein; Protein Subunits; Protons; Spectrophotometry

2004
Involvement of a Glu71-Arg64 couple in the access channel for NADH in cytochrome p450nor.
    Bioscience, biotechnology, and biochemistry, 2004, Volume: 68, Issue:5

    Topics: Amino Acid Substitution; Arginine; Aspartic Acid; Cytochrome P-450 Enzyme System; Fusarium; Glutamic Acid; Heme; Molecular Structure; NAD; Oxidoreductases; Point Mutation

2004
The role of the length and sequence of the linker domain of cytochrome b5 in stimulating cytochrome P450 2B4 catalysis.
    The Journal of biological chemistry, 2004, Aug-27, Volume: 279, Issue:35

    Topics: Amino Acid Sequence; Animals; Aryl Hydrocarbon Hydroxylases; Aspartic Acid; Catalysis; Cattle; Crystallography, X-Ray; Cytochrome P450 Family 2; Cytochromes b5; Databases as Topic; DNA, Complementary; Dose-Response Relationship, Drug; Electrons; Escherichia coli; Gene Deletion; Heme; Humans; Iron; Kinetics; Microsomes, Liver; Models, Chemical; Models, Molecular; Models, Statistical; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Plasmids; Protein Binding; Protein Conformation; Protein Isoforms; Protein Structure, Secondary; Protein Structure, Tertiary; Rabbits; Sequence Homology, Amino Acid; Serine; Spectrophotometry

2004
Critical roles of Asp40 at the haem proximal side of haem-regulated phosphodiesterase from Escherichia coli in redox potential, auto-oxidation and catalytic control.
    European journal of biochemistry, 2004, Volume: 271, Issue:19

    Topics: Aspartic Acid; Binding Sites; Catalysis; Catalytic Domain; Escherichia coli; Heme; Hydrogen Bonding; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Phosphoric Diester Hydrolases; Structure-Activity Relationship

2004
A relationship between heme binding and protein stability in cytochrome b5.
    Biochemistry, 2004, Sep-28, Volume: 43, Issue:38

    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
Roles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanism.
    The Journal of biological chemistry, 2005, Jan-28, Volume: 280, Issue:4

    Topics: Aspartic Acid; Binding Sites; Catalysis; Corynebacterium diphtheriae; Crystallography, X-Ray; Escherichia coli; Heme; Heme Oxygenase (Decyclizing); Hydrogen Peroxide; Iron; Models, Chemical; Mutagenesis, Site-Directed; Mutation; NADP; NADPH-Ferrihemoprotein Reductase; Oxygen; Plasmids; Spectrophotometry; Spectrum Analysis, Raman; Ultraviolet Rays; Water

2005
Role of the covalent glutamic acid 242-heme linkage in the formation and reactivity of redox intermediates of human myeloperoxidase.
    Biochemistry, 2005, May-03, Volume: 44, Issue:17

    Topics: Animals; Aspartic Acid; Binding Sites; Bromides; Chlorides; CHO Cells; Circular Dichroism; Cricetinae; Cyanides; Enzyme Stability; Eosinophil Peroxidase; Ferric Compounds; Glutamic Acid; Glutamine; Heme; Humans; Methionine; Oxidation-Reduction; Peroxidase; Recombinant Proteins

2005
Crystal structure of human cytochrome P450 2D6.
    The Journal of biological chemistry, 2006, Mar-17, Volume: 281, Issue:11

    Topics: Amino Acid Sequence; Aspartic Acid; Binding Sites; Carbon Monoxide; Crystallography, X-Ray; Cytochrome P-450 CYP2D6; Glutamic Acid; Heme; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Protein Conformation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Software; Subcellular Fractions; Substrate Specificity

2006
Linker chains of the gigantic hemoglobin of the earthworm Lumbricus terrestris: primary structures of linkers L2, L3, and L4 and analysis of the connectivity of the disulfide bonds in linker L1.
    Proteins, 2006, Apr-01, Volume: 63, Issue:1

    Topics: Amino Acid Sequence; Animals; Aspartic Acid; Base Sequence; Binding Sites; Calcium; Chromatography, High Pressure Liquid; Cysteine; Disulfides; Dithiothreitol; DNA, Complementary; Glutamic Acid; Heme; Hemoglobins; Histidine; Humans; Ligands; Mass Spectrometry; Models, Molecular; Molecular Sequence Data; Oligochaeta; Protein Binding; Protein Processing, Post-Translational; Protein Structure, Tertiary; Receptors, LDL; RNA, Messenger; Sequence Homology, Amino Acid; Sodium Dodecyl Sulfate; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Superoxide Dismutase

2006
Two alternative substrate paths for compound I formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei.
    Proteins, 2007, Jan-01, Volume: 66, Issue:1

    Topics: Aspartic Acid; Bacterial Proteins; Binding Sites; Burkholderia pseudomallei; Crystallography, X-Ray; Electron Spin Resonance Spectroscopy; Heme; Hydrogen Bonding; Hydrogen Peroxide; Kinetics; Models, Molecular; Mutation; Oxidation-Reduction; Peroxidases; Solvents; Substrate Specificity

2007
Loss of ATP hydrolysis activity by CcmAB results in loss of c-type cytochrome synthesis and incomplete processing of CcmE.
    The FEBS journal, 2007, Volume: 274, Issue:9

    Topics: Adenosine Triphosphate; Amino Acid Motifs; Aspartic Acid; ATP-Binding Cassette Transporters; Bacterial Outer Membrane Proteins; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Histidine; Hydrolysis; Lysine; Mutagenesis, Site-Directed; Protein Processing, Post-Translational; Protein Subunits; Sequence Deletion

2007
Disruption of the aspartate to heme ester linkage in human myeloperoxidase: impact on ligand binding, redox chemistry, and interconversion of redox intermediates.
    The Journal of biological chemistry, 2007, Jun-08, Volume: 282, Issue:23

    Topics: Animals; Aspartic Acid; CHO Cells; Cricetinae; Cricetulus; Electrochemistry; Esters; Heme; Humans; Kinetics; Ligands; Oxidation-Reduction; Peroxidase; Protein Binding; Spectrum Analysis

2007
What is the active species of cytochrome P450 during camphor hydroxylation? QM/MM studies of different electronic states of compound I and of reduced and oxidized iron-oxo intermediates.
    Journal of the American Chemical Society, 2007, Jul-25, Volume: 129, Issue:29

    Topics: Aspartic Acid; Camphor; Computational Biology; Crystallography, X-Ray; Cytochrome P-450 Enzyme System; Electrons; Free Radicals; Heme; Histidine; Hydroxylation; Iron; Oxidation-Reduction; Protons; Quantum Theory

2007
Mechanism of formation of the ester linkage between heme and Glu310 of CYP4B1: 18O protein labeling studies.
    Biochemistry, 2007, Oct-16, Volume: 46, Issue:41

    Topics: Amino Acid Sequence; Aryl Hydrocarbon Hydroxylases; Aspartic Acid; Binding Sites; Esters; Glutamic Acid; Heme; Kinetics; Mass Spectrometry; Peptide Fragments; Polymerase Chain Reaction; Recombinant Proteins; Trypsin

2007
Spectroscopic study on the communication between a heme a3 propionate, Asp399 and the binuclear center of cytochrome c oxidase from Paracoccus denitrificans.
    Biochimica et biophysica acta, 2008, Volume: 1777, Issue:2

    Topics: Amino Acid Sequence; Aspartic Acid; Electrochemistry; Electron Transport Complex IV; Heme; Hydrogen-Ion Concentration; Models, Molecular; Oxidation-Reduction; Paracoccus denitrificans; Propionates; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis

2008
Protonation of the proximal histidine ligand in heme peroxidases.
    The journal of physical chemistry. B, 2008, Feb-28, Volume: 112, Issue:8

    Topics: Aspartic Acid; Heme; Histidine; Ligands; Models, Chemical; Peroxidase; Protons; Quantum Theory; Solvents; Thermodynamics

2008
Why do cysteine dioxygenase enzymes contain a 3-His ligand motif rather than a 2His/1Asp motif like most nonheme dioxygenases?
    The journal of physical chemistry. A, 2009, Mar-05, Volume: 113, Issue:9

    Topics: Amino Acid Motifs; Aspartic Acid; Biocatalysis; Catalytic Domain; Cysteine; Cysteine Dioxygenase; Heme; Histidine; Humans; Ligands; Models, Chemical; Models, Molecular

2009
Active site of cytochrome cbb3.
    The Journal of biological chemistry, 2009, Apr-24, Volume: 284, Issue:17

    Topics: Aspartic Acid; Biological Transport; Catalysis; Catalytic Domain; Copper; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Glutamine; Heme; Ions; Mutagenesis; Mutation; Oxidation-Reduction; Protons; Rhodobacter sphaeroides

2009
Stringency of the 2-His-1-Asp active-site motif in prolyl 4-hydroxylase.
    PloS one, 2009, Nov-05, Volume: 4, Issue:11

    Topics: Alanine; Amino Acid Motifs; Aspartic Acid; Carbon; Catalysis; Catalytic Domain; Collagen; Glycine; Heme; Histidine; Humans; Hydrogen; Iron; Ligands; Procollagen-Proline Dioxygenase

2009
Aspartate 102 in the heme domain of soluble guanylyl cyclase has a key role in NO activation.
    Biochemistry, 2011, May-24, Volume: 50, Issue:20

    Topics: Alanine; Animals; Aspartic Acid; Chlorocebus aethiops; COS Cells; Enzyme Activation; Guanylate Cyclase; Heme; Indazoles; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Nitric Oxide; Protein Structure, Tertiary; Protein Subunits; Rats; Receptors, Cytoplasmic and Nuclear; Sequence Homology, Amino Acid; Soluble Guanylyl Cyclase

2011
The catalytic mechanism of dye-decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residue.
    The FEBS journal, 2011, Volume: 278, Issue:13

    Topics: Aspartic Acid; Binding Sites; Catalysis; Coloring Agents; Crystallography, X-Ray; Heme; Hydrogen Peroxide; Mutation; Oxidants; Peroxidases; Protein Binding

2011
Signal transduction and phosphoryl transfer by a FixL hybrid kinase with low oxygen affinity: importance of the vicinal PAS domain and receiver aspartate.
    Biochemistry, 2013, Jan-22, Volume: 52, Issue:3

    Topics: Amino Acid Substitution; Aspartic Acid; Bacterial Proteins; Heme; Hemeproteins; Histidine; Histidine Kinase; Kinetics; Ligands; Mutant Proteins; Oxidation-Reduction; Oxygen; Peptide Fragments; Phosphorylation; Protein Binding; Protein Interaction Domains and Motifs; Protein Processing, Post-Translational; Protein Serine-Threonine Kinases; Recombinant Proteins; Rhizobium; Signal Transduction

2013
Post-translational transformation of methionine to aspartate is catalyzed by heme iron and driven by peroxide: a novel subunit-specific mechanism in hemoglobin.
    The Journal of biological chemistry, 2014, Aug-08, Volume: 289, Issue:32

    Topics: Adult; Amino Acid Sequence; Amino Acid Substitution; Aspartic Acid; Crystallography, X-Ray; Fetal Hemoglobin; Heme; Hemoglobin A; Hemoglobins; Hemoglobins, Abnormal; Humans; Hydrogen Peroxide; Iron; Methionine; Models, Molecular; Molecular Sequence Data; Mutation, Missense; Oxidation-Reduction; Protein Processing, Post-Translational; Protein Subunits; Proteomics; Static Electricity

2014
Dendrimeric template of Plasmodium falciparum histidine rich protein II repeat motifs bearing Asp→Asn mutation exhibits heme binding and β-hematin formation.
    PloS one, 2014, Volume: 9, Issue:11

    Topics: Amino Acid Motifs; Amino Acid Sequence; Antigens, Protozoan; Asparagine; Aspartic Acid; Bicarbonates; Binding Sites; Chromatography, High Pressure Liquid; Chromatography, Reverse-Phase; Dendrimers; Heme; Hemeproteins; Kinetics; Mass Spectrometry; Molecular Sequence Data; Mutation; Plasmodium falciparum; Protein Binding; Protein Stability; Protozoan Proteins; Repetitive Sequences, Amino Acid; Spectrum Analysis; Structure-Activity Relationship; Titrimetry

2014
Structural characterization of the heme-based oxygen sensor, AfGcHK, its interactions with the cognate response regulator, and their combined mechanism of action in a bacterial two-component signaling system.
    Proteins, 2016, Volume: 84, Issue:10

    Topics: Aeromonas salmonicida; Aspartic Acid; Bacterial Proteins; Cloning, Molecular; Deuterium Exchange Measurement; Escherichia coli; Heme; Histidine; Histidine Kinase; Iron; Myxococcales; Oxygen; Phosphorylation; Protein Domains; Protein Structure, Secondary; Recombinant Proteins; Signal Transduction; Structural Homology, Protein

2016
Structural basis of haem-iron acquisition by fungal pathogens.
    Nature microbiology, 2016, Sep-12, Volume: 1, Issue:11

    Topics: Aspartic Acid; Biological Transport; Candida albicans; Crystallography, X-Ray; Cysteine; Fungal Proteins; Heme; Hemeproteins; Histidine; Iron; Membrane Proteins; Molecular Conformation

2016
Structure of bovine lactoperoxidase with a partially linked heme moiety at 1.98Å resolution.
    Biochimica et biophysica acta. Proteins and proteomics, 2017, Volume: 1865, Issue:3

    Topics: Animals; Aspartic Acid; Binding Sites; Cattle; Crystallography, X-Ray; Glutamic Acid; Heme; Lactoperoxidase; Mammals; Models, Molecular; Peroxidase; Protein Conformation

2017
Crystal structure and biochemical features of dye-decolorizing peroxidase YfeX from Escherichia coli O157 Asp
    Biochemical and biophysical research communications, 2017, 02-26, Volume: 484, Issue:1

    Topics: Arginine; Aspartic Acid; Calorimetry; Catalytic Domain; Cation Transport Proteins; Color; Crystallography, X-Ray; Escherichia coli O157; Escherichia coli Proteins; Heme; Hydrogen Peroxide; Substrate Specificity

2017
Heme Proximal Hydrogen Bonding between His170 and Asp132 Plays an Essential Role in the Heme Degradation Reaction of HutZ from Vibrio cholerae.
    Biochemistry, 2017, 05-30, Volume: 56, Issue:21

    Topics: Aspartic Acid; Bacterial Proteins; Heme; Histidine; Hydrogen Bonding; Molecular Structure; Vibrio cholerae

2017
[The content of N-acetylaspartate in depressed elderly patients during therapy with antidepressants and actovegin].
    Zhurnal nevrologii i psikhiatrii imeni S.S. Korsakova, 2019, Volume: 119, Issue:4

    Topics: Aged; Antidepressive Agents; Aspartic Acid; Depression; Female; Heme; Humans; Male

2019
Heat shock protein 90 enhances the electron transfer between the FMN and heme cofactors in neuronal nitric oxide synthase.
    FEBS letters, 2020, Volume: 594, Issue:17

    Topics: Animals; Aspartic Acid; Binding Sites; Cloning, Molecular; Electrons; Escherichia coli; Ficoll; Flavin Mononucleotide; Gene Expression; Genetic Vectors; Heme; HSP90 Heat-Shock Proteins; Humans; Lysine; Molecular Docking Simulation; Mutation; NADP; Nitric Oxide Synthase Type I; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Rats; Recombinant Proteins; Static Electricity

2020