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The photoelectron (PE) spectra of dicyano methane and of its dimethyl derivative are tentatively assigned on the basis of a simple MO model. The interactions defined therein between the two cyano groups as well as with the R2C-framework can be parametrized using the PE data. Thus the hyperconjugation πCN/πCR₂ is estimated to amount to 1.7 eV in both compounds. Hyperconjugative effects in methane derivatives H3CX and H2CX2 with X = Br, Cl and CN are compared.
In view of new high-precision experiments in atomic physics it seems necessary to reexamine nonlinear theories of electrodynamics. The precise calculation of electronic and muonic atomic energies has been used to determine the possible size of the upper limit Emax to the electric field strength, which has been assumed to be a parameter. This is opposed to Born's idea of a purely electromagnetic origin of the electron's mass which determines Emax. We find Emax≥1.7×1020 V/cm.
Am Rande der Westfälischen Bucht liegen bei Versmold und Gütersloh zwei Drumlinfelder. Die zusammen über 60 Rücken, die aus Sand und Geschiebelehm bestehen, wurden durch einen Gletscher des Inlandeises geformt, der aus der Westfälischen Bucht gegen die Randhöhen des Teutoburger Waldes vordrang. Es handelt sich um die Erstbeschreibung von Drumlins im Altmoränengebiet Nordwestdeutschlands.
The spectral properties of binary complexes of NAD-analogues and fragments therefrom with I.DH from pig heart or ADH from liver and yeast have been investigated. The NADH-analogues were modified by replacing adenine through benzimidazole, benzene or dihydronicotinamide. Additionally adenosine diphosphate ribose, dihydronicotinamide and dihydronicotinamide- ribose pyrophosphate-5"-ribose have been studied.
It has been shown by means of difference spectra that complexes between ADH from horse liver and analogues cause spectral changes in the region of aromatic absorption at 280 nm even when adenine is absent in the analogues. Spectral changes in the other enzymes mentioned are probably due to changes of the n-π* absorption of the adenine ring. The spectral changes upon complexing indicate hydrophobic interaction of the adenine with the enzyme protein. Fluorescence spectra vary in the intensity of the energy transfer band as well as in coenzyme emission depending on variation of the coenzym analogue. Changing of complex formation between protein and analogues at different pH-values are investigated. ADH from yeast, especially, shows a pK around 6 which suggests interaction with histidine imidazole.