Comparison of two methods characterising the seed bank of amphibious plants in submerged sediments

We analysed the submerged soil seed bank of three fishponds in the Waldviertel region in Austria. We aimed our study at comparing the efficiency of two methods in detecting seeds quantitatively from soil samples of four characteristic mud-flat species, i.e. Carex bohemica, Coleanthus subtilis, Elatine hexandra, and Eleocharis ovata: the seedling-emergence and the rinsing method. Additionally, the actual vegetation was described based on 65 phytosociological relevés. Soil seed bank analyses were based on 31 samples representing the vegetation zonation. Mixed soil samples were portioned into 62 subsamples further treated with the two methods in parallel.     

Single channel gating events in tracer flux experiments. II. Flux amplitude analysis

Measurement of tracer ion flux from or into a collection of closed membrane structures (CMS) constitutes a broadly applicable technique for studying ion channel gating by specialized gating molecules in biological membranes. The amplitudes for the flux process reflect the overall change in tracer content due to flux during a period in which channels on at least some of the CMS were open. In practice, the attainment of a time-invariant, finite overall tracer content, indicating a cessation of flux, need not imply that flux has reached completion, i.e., that the CMS internal and external tracer concentrations have fully reached equilibrium. Less than maximum flux amplitudes arise when binding of control ligands leads to an inhibition or inactivation of the channel gating molecules prior to a complete equilibration of tracer. Analysis of the dependence of the flux amplitudes on control ligand concentration permits determination of characteristic parameters of the CMS that may vary with the methods of preparation (e.g., the distributions of CMS size and CMS content of gating units). Knowledge of these parameters in turn permits evaluation of the mean single channel flux amplitude contribution, which is functionally dependent on the rate constant ratio (k'eff/ki), where k'eff and ki are, respectively, the effective rate constants for tracer flux and for gating unit inactivation.     

Triangle Consortium for Reproductive Biology 22nd Annual Meeting

Mol. Reprod. Dev. 80: 504–507, 2013. © 2013 Wiley Periodicals, Inc. This article is a US government work and, as such, is in the public domain in the United States of America.     

Degradation of dioxane,tetrahydrofuran and other cyclic ethers by an environmental Rhodococcus strain

Summary By enrichment and isolation techniques bacterial strains with the capacity to grow on aliphatic cyclic ethers (dioxane, tetrahydrofuran, 1,3-dioxolane) have been isolated. Six strains that degrade tetrahydrofuran were classified as belonging to the genus Rhodococcus. One of two strains that degrade dioxane instead of or in combination with tetrahydrofuran was further characterized and a hypothetical catabolic pathway comprising an initial 2-hydroxylation and several oxidation steps is postulated. Offsprint requests to: H. Diekmann     

Dioxygen-activating iron center in putidamonooxin. Electron spin resonance investigation of the nitrosylated putidamonooxin

The mononuclear non-haem iron center is the dioxygen-binding site of putidamonooxin which is the dioxygen-activating component of the 4-methoxybenzoate monooxygenase. Replacement of dioxygen by nitrosyl leads to the formation of a rather stable Fe3+ X NO- complex which is characterized by electron spin resonance (ESR) at g approximately equal to 4 and g approximately equal to 2. The ESR features can be composed by two spectral components which are characterized by different tetragonal distortions of the axial symmetry. Binding of 4-hydroxybenzoate, which is the product of the enzymatic reaction, leads to the formation of an ESR spectrum with pure axial symmetry. After binding of 4-methoxybenzoate, i.e. the physiological substrate of the monooxygenase, only one spectral component, i.e. that with a small tetragonal distortion, is observed. Binding of substrate analogues, like 4-aminobenzoate and 4-trifluoromethylbenzoate, leads to a spectral heterogeneity with variable amounts of the ESR component with a large tetragonal distortion. Benzoate induces an ESR spectrum with only that spectral component with large tetragonal distortion. The iron-depleted substrate-free form of the enzyme, ligated with NO, also shows ESR heterogeneity, i.e. both spectral components overlap, with 60% of the component with large tetragonal distortion. Binding of 4-methoxybenzoate leads to the occurrence of a pure spectrum, i.e. with small tetragonal distortion, whereas binding of benzoate leads to a pure spectrum with large tetragonal distortion. Thus, the structural heterogeneity is removed by binding of both the ligand (NO) and substrate. The Fe3+ X NO- complex is discussed as an analogue of the native oxy complex Fe3+ X O2-.