Compounds > asparagine

asparagine and carbon monoxide

asparagine has been researched along with carbon monoxide in 8 studies

Research

Studies (8)

TimeframeStudies, this research(%)All Research%
pre-19902 (25.00)18.7374
1990's4 (50.00)18.2507
2000's2 (25.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Bonaventura, C; Bonaventura, J; Ferruzzi, G; Fox, J; McCurdy, PR; Moo-Penn, WF; Sullivan, B1
Charache, S; Winslow, RM1
Brzozowski, AM; Gibson, QH; Jaskolski, M; Klizas, SA; Krzywda, S; Murshudov, GN; Olson, JS; Scott, EE; Wilkinson, AJ1
Ariga, Y; Egawa, T; Hishiki, T; Hori, H; Ishimura, Y; Masuya, F; Nagano, S; Obata, T; Shimada, H; Unno, M1
Adelroth, P; Brzezinski, P; Gennis, RB; Smirnova, IA1
Hendrich, MP; Ho, C; Ho, NT; Jeong, ST1
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

Other Studies

8 other study(ies) available for asparagine and carbon monoxide

ArticleYear
Hemoglobin providence. Functional consequences of two alterations of the 2,3-diphosphoglycerate binding site at position beta 82.
    The Journal of biological chemistry, 1976, Dec-10, Volume: 251, Issue:23

    Topics: Adult; Asparagine; Aspartic Acid; Binding Sites; Carbon Monoxide; Diphosphoglyceric Acids; Female; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Lysine; Molecular Conformation; Osmolar Concentration; Oxygen; Phytic Acid; Protein Conformation; Sodium Chloride

1976
Hemoglobin Richmond. Subunit dissociation and oxygen equilibrium properties.
    The Journal of biological chemistry, 1975, Sep-10, Volume: 250, Issue:17

    Topics: Amino Acid Sequence; Asparagine; Binding Sites; Carbon Monoxide; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Kansas; Kinetics; Lysine; Macromolecular Substances; Oxygen; Threonine; Virginia

1975
Stabilizing bound O2 in myoglobin by valine68 (E11) to asparagine substitution.
    Biochemistry, 1998, Nov-10, Volume: 37, Issue:45

    Topics: Amino Acid Substitution; Animals; Asparagine; Binding Sites; Carbon Monoxide; Crystallization; Crystallography, X-Ray; Mutagenesis, Insertional; Mutagenesis, Site-Directed; Myoglobin; Nitric Oxide; Oxygen; Swine; Valine; Whales

1998
Putidaredoxin-cytochrome p450cam interaction. Spin state of the heme iron modulates putidaredoxin structure.
    The Journal of biological chemistry, 1999, Apr-02, Volume: 274, Issue:14

    Topics: Amino Acid Substitution; Asparagine; Bacterial Proteins; Camphor 5-Monooxygenase; Carbon Monoxide; Electron Spin Resonance Spectroscopy; Ferredoxins; Glycine; Ligands; Macromolecular Substances; Mutagenesis, Site-Directed; NADH, NADPH Oxidoreductases; Nitric Oxide; Oxidation-Reduction; Oxygen; Potassium Chloride

1999
Aspartate-132 in cytochrome c oxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during oxo-ferryl formation.
    Biochemistry, 1999, May-25, Volume: 38, Issue:21

    Topics: Amino Acid Substitution; Arachidonic Acid; Asparagine; Aspartic Acid; Carbon Monoxide; Electrochemistry; Electron Transport; Electron Transport Complex IV; Iron; Oxidation-Reduction; Proton Pumps; Protons; Rhodobacter sphaeroides

1999
Recombinant hemoglobin(alpha 29leucine --> phenylalanine, alpha 96valine --> tryptophan, beta 108asparagine --> lysine) exhibits low oxygen affinity and high cooperativity combined with resistance to autoxidation.
    Biochemistry, 1999, Oct-05, Volume: 38, Issue:40

    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
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