Journal ArticleDOI
Letter: alpha-aminoacrylate schiff base in nonenzymatic pyridoxal catalysis.
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This article is published in Journal of the American Chemical Society.The article was published on 1976-06-09. It has received 10 citations till now. The article focuses on the topics: Pyridoxal & Schiff base.read more
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Journal ArticleDOI
Turnover of thylakoid photosystem II proteins during photoinhibition of Chlamydomonas reinhardtii.
TL;DR: It is proposed that the light-dependent turnover of the D1 protein is a protective mechanism against photoinhibition as far as the removal and replacement of D1 is compatible with the photoinactivation incurred by photosystem II.
Journal ArticleDOI
The catalytic mechanism of tryptophan synthase from Escherichia coli. Kinetics of the reaction of indole with the enzyme--L-serine complexes.
Andrew N. Lane,Kasper Kirschner +1 more
TL;DR: The mechanism by which indole condenses with L-serine in the active site of tryptophan synthase was studied by the stopped-flow technique and provides a detailed framework for explaining all available information, including the activating effect of the alpha subunit on the reaction catalyzed by the beta 2 subunit.
Journal ArticleDOI
Detection and identification of intermediates in the reaction of L-serine with Escherichia coli tryptophan synthase via rapid-scanning ultraviolet-visible spectroscopy.
TL;DR: Findings identify the serine Schiff base (the external aldimine) as the 420 nm absorbing, highly fluorescent transient; the species with lambda max congruent to 460 nm is the delocalized carbanion (quinoidal) species derived from abstraction of the alpha proton from the external a Aldimine.
Journal ArticleDOI
Spectroscopic studies of quinonoid species from pyridoxal 5'-phosphate.
TL;DR: The analysis establishes that in all species a proton remains on either the phenolic oxygen or the imine nitrogen, and suggests that the latter may, in fact, be a quinonoid form, either alone or in rapid equilibrium with the Schiff base.
Journal ArticleDOI
Intersubunit communication in tryptophan synthase by carbon-13 and fluorine-19 REDOR NMR.
TL;DR: The beta subunits of the 143-kDa alpha2 beta2beta2 tetrameric enzyme tryptophan synthase have been labeled by L-[ring-4-19F]phenylalanine and L-[phenol- 4-13C]tyrosine in an effort to monitor the positions of these residues on ligand binding.
Related Papers (5)
The Role of Axial Chirality in Schiff Bases of Pyridoxal Phosphate and Amino Acids in the Mechanism of Racemase Enzymes. A Quantum-Chemical Study
M.H.P. van Genderen,HM Henk Buck +1 more