Aplysia oxymyoglobin with an unusual stability property: kinetic analysis of the pH dependence
- 1 July 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (13) , 3898-3903
- https://doi.org/10.1021/bi00361a024
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- Aplysia oxymyoglobin with an unusual stability propertyJournal of Molecular Biology, 1984
- Stability properties of sperm whale oxymyoglobinArchives of Biochemistry and Biophysics, 1983
- Mechanism of autooxidation for hemoglobins and myoglobins. Promotion of superoxide production by protons and anions.Journal of Biological Chemistry, 1982
- Autoxidation of oxymyoglobin. A nucleophilic displacement mechanism.Journal of Biological Chemistry, 1981
- Neutron diffraction reveals oxygen–histidine hydrogen bond in oxymyoglobinNature, 1981
- Amino acid sequence of myoglobin from Aplysia kurodaiBiochimica et Biophysica Acta (BBA) - Protein Structure, 1981
- Autoxidation of Native OxymyoglobinEuropean Journal of Biochemistry, 1980
- Autoxidation of Native Oxymyoglobin. Kinetic Analysis of the pH ProfileEuropean Journal of Biochemistry, 1978
- Structure of hemoglobins Zürich [His E7(63)beta replaced by Arg] and Sydney [Val E11(67)beta replaced by Ala] and role of the distal residues in ligand binding.Proceedings of the National Academy of Sciences, 1978
- Generation of the Superoxide Radical during Autoxidation of OxymyoglobinThe Journal of Biochemistry, 1976