Multidimensional reaction coordinate for the excited-state H-atom transfer in perylene quinones: importance of the 7-membered ring in hypocrellins A and B

The excited-state intramolecular H-atom transfer reactions of hypocrellins B and A are compared by using time-resolved absorption and fluorescence upconversion techniques. The hypocrellin B photophysics are well described by a simple model involving one ground-state species and excited-state forward and reverse H-atom transfer with a nonfluorescent excited state. We suggest that excited-state conformational changes are coupled to the H-atom transfer in hypocrellin B just as gauche/anti changes are coupled to the H-atom transfer in hypocrellin A.     

Picosecond dynamics of a peptide from the acetylcholine receptor interacting with a neurotoxin probed by tailored tryptophan fluorescence

A tryptophan analog, dehydro-N-acetyl-L-tryptophanamide (delta-NATA), which is produced enzymatically via L-tryptophan 2',3'-oxidase from Chromobacterium violaceum, is newly used for time-resolved fluorescence. The absorption and emission maxima of delta-NATA at 332 and 417 nm, respectively, in 20% dimethylformamide-water are significantly shifted to the red with respect to those of tryptophan in water, permitting us to measure its fluorescence in the presence of tryptophan residues. We demonstrate that the steady-state spectra and the fluorescence decay of delta-NATA are very sensitive to environment, changing dramatically with solvent as the chromophore is localized within a protein and when this tagged protein binds to a peptide. The tryptophan oxidase was also used to modify the single Trp of a neurotoxin from snake (Naja nigricollis) venom. Modification of the toxin alpha (dehydrotryptophan-toxin alpha) permitted its investigation in complex with a synthetic 15-amino acid peptide corresponding to a loop of the agonist-binding site of acetylcholine receptor (AchR) from Torpedo marmorata species. The peptide alpha-185 possesses a single Trp at the third position (Trp187 of AchR) and a disulfide bridge between Cys192 and Cys193. A single-exponential rotational diffusion time with a constant of 1.65 ns is measured for the isolated 15-amino acid peptide. This suggests that Trp motion in the peptide in solution is strongly correlated with the residues downstream the peptide sequence, which may in part be attributed to long-range order imposed by the disulfide bond. The dynamics of the bound peptide are very different: the presence of two correlation times indicates that the Trp187 of the peptide has a fast motion (taur1 = 140 ps and r(0)1 = 0.14) relative to the overall rotation of the complex (taur2 = 3.4 ns and r(0)2 = 0.04). The correlation of the Trp residue with its neighboring amino acid residues and with the overall motion of the peptide is lost, giving rise to its rapid restricted motion. Thus, the internal dynamics of interacting peptides change on binding.     

Fluorescence properties of recombinant tropomyosin containing tryptophan, 5-hydroxytryptophan and 7-azatryptophan

Tropomyosin mutants containing either tryptophan (122W), 5-hydroxytryptophan (5OH122W) or 7-azatryptophan (7N122W) have been expressed in Escherichia coli and their fluorescence properties studied. The fluorescent amino acids were located at position 122 of the tropomyosin primary sequence, corresponding to a solvent-exposed position c of the coiled-coil heptapeptide repeat. The emission spectrum of the probe in each mutant is blue-shifted slightly with respect to that of the probe in water. The fluorescence anisotropy decays are single exponential, with a time constant of 2-3 ns while the fluorescence lifetimes of the probes incorporated into the proteins, in water, are nonexponential. Because tryptophan in water has an intrinsic nonexponential fluorescence decay, it is not surprising that the fluorescence decay of 122W is well described by a triple exponential. The fluorescence decays in water of the nonnatural amino acids 5-hydroxytryptophan and 7-azatryptophan (when emission is collected from the entire band) are single exponential. Incorporation into tropomyosin induces triple-exponential fluorescence decay in 5-hydroxytryptophan and double-exponential fluorescence decay in 7-azatryptophan. The range of lifetimes observed for 5-hydroxyindole and 5-hydroxytryptophan at high pH and in the nonaqueous solvents were used as a base with which to interpret the lifetimes observed for the 5OH122W and indicate that the chromophore exists in several solvent environments in both its protonated and unprotonated forms in 5OH122W.     

On congruences on \mathcal{T} -regular semigroups

A nontrivial regular semigroup S with zero in which every interval of idempotents is a finite chain is said to be -regular. The structure of these semigroups is described in terms of trees of completely 0-simple semigroups. For S in this form, we study congruences which we express in terms of congruence aggregates. We determine the inclusion relation, meet and join of congruences, their kernel and trace, and the ends of the intervals which form their classes. We characterize those S for which the kernel relation on the congruence lattice is a congruence, and those for which the operators and are homomorphisms.     

On some intervals of varieties of completely regular semigroups

Semigroup Forum - Completely regular semigroups with the unary operation of inversion within their maximal subgroups form a variety under inclusion denoted by $$mathcal {C}mathcal {R}$$. The...     

{\sl M}-classification of Regular Semigroups

Abstract. On any regular semigroup S, the least group congruence σ, the greatest idempotent pure congruence τ and the least band congruence β are used to give the M -classification of regular semigroups as follows. These congruences generate a sublattice Λ of the congruence lattice C (S) of S. We consider the triples (Λ,K,T), where K and T are the restrictions of the K - and T -relations on {C (S) to Λ. Such triples are characterized abstractly and form the objects of a category M whose morphisms are surjective T -preserving homomorphisms subject to a mild condition. The class of regular semigroups is made into a category M whose morphisms are fairly restricted homomorphisms. The main result of the paper is the existence of a representative functor from M to M. Several properties of the classification of regular semigroups induced by this functor are established.