The cooperative binding of phenylalanine to phenylalanine 4-monooxygenase studied by 1H-NMR paramagnetic relaxation. Changes in water accessibility to the iron at the active site upon substrate binding
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1993.tb19894.x/fullpdf
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2. Resonance Raman studies on the blue-green-colored bovine adrenal tyrosine 3-monooxygenase (tyrosine hydroxylase). Evidence that the feedback inhibitors adrenaline and noradrenaline are coordinated to iron.
3. [17O]Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase. Evidence for binding of exogenous ligands to the active site Fe2+ of extradiol dioxygenases.
4. I. Bertini, and C. Luchinat (1986 ) inNMR of paramagnetic molecules in biological systems , pp47 -83 , The Benjamin/Cummings Publishing Company, California.
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1. Substituting Tyr138 in the active site loop of human phenylalanine hydroxylase affects catalysis and substrate activation;FEBS Open Bio;2017-06-12
2. PKU mutation p.G46S prevents the stereospecific binding ofl-phenylalanine to the dimer of human phenylalanine hydroxylase regulatory domain;FEBS Open Bio;2017-01-21
3. Jahn–Teller Dynamics in a Series of High-Symmetry Co(II) Chelates Determine Paramagnetic Relaxation Enhancements;The Journal of Physical Chemistry A;2012-11-05
4. Allosteric regulation of phenylalanine hydroxylase;Archives of Biochemistry and Biophysics;2012-03
5. Superstoichiometric binding of L-Phe to phenylalanine hydroxylase from Caenorhabditis elegans: evolutionary implications;Amino Acids;2010-05-18
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