The stereochemistry of NADH utilization by the flavoenzyme monooxygenase orcinol hydroxylase.
Open Access
- 1 June 1979
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 254 (11) , 4349-4351
- https://doi.org/10.1016/s0021-9258(17)30014-5
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- The structure of the flavoenzyme glutathione reductaseNature, 1978
- [14] The hydride transfer stereospecificity of nicotinamide adenine dinucleotide linked enzymes: A proton magnetic resonance techniquePublished by Elsevier ,1978
- On the Structure of Flavin‐Oxygen Intermediates Involved in Enzymatic ReactionsEuropean Journal of Biochemistry, 1977
- The stereospecificity of bacterial external flavoprotein monooxygenases for nicotinamide adenine dinucleotideArchives of Biochemistry and Biophysics, 1977
- Flavin-oxygen derivatives involved in hydroxylation by p-hydroxybenzoate hydroxylase.Journal of Biological Chemistry, 1976
- Metabolism of resorcinylic compounds by bacteria. Purification and properties of orcinol hydroxylase from Pseudomonas putida 01.Journal of Biological Chemistry, 1975
- Purification and Properties of p-Hydroxybenzoate Hydroxylase from Pseudomonas fluorescensJournal of Biological Chemistry, 1972
- Interactions of substrate and non-substrate effectors with p-hydroxybenzoate hydroxylase from psuedomonas fluorescensBiochemical and Biophysical Research Communications, 1971
- A Structure of Pyridine Nucleotides in SolutionProceedings of the National Academy of Sciences, 1971
- Use of Hydrogen Isotope Effects to Identify the Attacking Nucleophile in the Enolization of Ketones Catalyzed by Acetic Acid1-3Journal of the American Chemical Society, 1958