The Accessibility of Iron at the Active Site of Recombinant Human Phenylalanine Hydroxylase to Water As Studied by 1H NMR Paramagnetic Relaxation
Open Access
- 1 March 1999
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (10) , 6280-6284
- https://doi.org/10.1074/jbc.274.10.6280
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Spectroscopic Characterization of the Catalytically Competent Ferrous Site of the Resting, Activated, and Substrate-Bound Forms of Phenylalanine HydroxylaseJournal of the American Chemical Society, 1997
- The cooperative binding of phenylalanine to phenylalanine 4‐monooxygenase studied by 1H‐NMR paramagnetic relaxationEuropean Journal of Biochemistry, 1993
- EPR and 1H‐NMR spectroscopic studies on the paramagnetic iron at the active site of phenylalanine hydroxylase and its interaction with substrates and inhibitorsEuropean Journal of Biochemistry, 1991
- Cooperative homotropic interaction of l‐noradrenaline with the catalytic site of phenylalanine 4‐monooxygenaseEuropean Journal of Biochemistry, 1990
- Phosphorus-31 and proton NMR studies of the structure of enzyme-bound substrate complexes of lobster muscle arginine kinase: relaxation measurements with manganese(II) and cobalt(II)Biochemistry, 1989
- Reductive activation of phenylalanine hydroxylase and its effect on the redox state of the non-heme ironBiochemistry, 1984
- Proton relaxation enhancement (PRE) in biochemistry: A critical surveyProgress in Nuclear Magnetic Resonance Spectroscopy, 1979
- Optical and magnetic resonance studies of formate binding to horse liver catalase and sperm whale myoglobinBiochemistry, 1975
- The determination of iron with 1,10-phenanthrolineTalanta, 1961
- Bathophenanthrolinedisulphonic acid and bathocuproinedisulphonic acid, water soluble reagents for iron and copperTalanta, 1961