Proton NMR Studies on the Conformation of the Pterin Cofactor Bound at the Active Site of Recombinant Human Tyrosine Hydroxylase
The binding of L-erythro-7,S-dihydrobiopterin (BH2) in the presence of L-Phe to recombinant human tyrosine hydroxylase was studied by 1H-NMR spectroscopy. The distances (± 1.3 A) from the active site metal were estimated to be 5 .3-6.4 A for observable protons of BH2 and 7 .0-7.9 A for L-Phe protons...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
De Gruyter
1998-02-01
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| Series: | Pteridines |
| Subjects: | |
| Online Access: | https://doi.org/10.1515/pteridines.1998.9.1.44 |