Equilibrium and water proton relaxation rate enhancement properties of formyltetrahydrofolate synthetase-manganous ion-substrate complexes.
Open Access
- 1 January 1975
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 250 (1) , 254-260
- https://doi.org/10.1016/s0021-9258(19)42008-5
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Magnetic resonance studies of substrate and inhibitor binding to porcine muscle adenylate kinaseBiochemistry, 1973
- Formyltetrahydrofolate synthetase. Substrate binding to monomeric subunitsBiochemistry, 1972
- Analog approaches to the structure of the transition state in enzyme reactionsAccounts of Chemical Research, 1972
- The subunit structure of formyltetrahydrofolate synthetaseBiochimica et Biophysica Acta (BBA) - Protein Structure, 1971
- Analysis of Equilibrium Data from Proton Magnetic Relaxation Rates of Water for Manganese-Nucleotide-Kinase Ternary ComplexesJournal of Biological Chemistry, 1970
- Evidence against the Folate-mediated Formylation of Formyl-accepting Methionyl Transfer Ribonucleic Acid in Streptococcus faecalis RJournal of Biological Chemistry, 1970
- Magnetic Resonance Investigations of the Metal Complexes Formed in the Manganese-activated Creatine Kinase ReactionJournal of Biological Chemistry, 1966
- Formyltetrahydrofolate synthetase: Mechanism of cation activationBiochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1965
- A Study of Manganous Complexes by Paramagnetic Resonance AbsorptionNature, 1954
- Effects of Diffusion on Free Precession in Nuclear Magnetic Resonance ExperimentsPhysical Review B, 1954