Nuclear magnetic resonance studies on the spatial relationship of aromatic donor molecules to the heme iron of horseradish peroxidase.
Open Access
- 1 July 1986
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 261 (21), 9657-9662
- https://doi.org/10.1016/s0021-9258(18)67564-7
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- The active center of catalaseJournal of Molecular Biology, 1985
- Plant peroxidases. Their primary, secondary and tertiary structures, and relation to cytochrome c peroxidaseEuropean Journal of Biochemistry, 1985
- A molecular orbital study on the oxidation of hydrogen donor molecules by peroxidase compound IIJournal of Theoretical Biology, 1983
- Isolation of a heme crevice peptide from affinity-labeled horseradish peroxidaseBiochemical and Biophysical Research Communications, 1980
- Assignment of exchangeable proximal histidine resonances in high-spin ferric hemoproteins: Substrate binding in horseradish peroxidaseBiochemical and Biophysical Research Communications, 1979
- Equilibria between Horseradish Peroxidase and Aromatic Donors.Acta Chemica Scandinavica, 1978
- Optical, NMR and EPR properties of horseradish peroxidase and its donor complexesFEBS Letters, 1975
- Conformational studies of peroxidase–substrate complexes. Structure of the indolepropionic acid–horseradish peroxidase complexJournal of the Chemical Society, Chemical Communications, 1975
- Reaction Mechanisms of Indole-3-acetate Degradation by Peroxidases. A Stopped-Flow and Low-Temperature Spectroscopic StudyEuropean Journal of Biochemistry, 1974
- Relaxation Processes in a System of Two SpinsPhysical Review B, 1955