On the formation of circulating patterns of excitation in anisotropic excitable media

We present a model of excitable media with the feature that it has a vulnerable phase during which a premature current stimulus will result in the formation of a reentrant selfsustained wave of excitation. The model exploits anisotropic coupling of identical cells, and is therefore useful as a model for the myocardium. We give rigorous verification that there is a vulnerable phase, and demonstrate numerically that permanently rotating waves are formed. Finally, it is shown that the direction of fastest propagation in myocardium is not necessarily the direction of highest safety factor, contrary to commonly accepted opinion.     

Sodium-coupled solute transport in charophyte algae: A general mechanism for transport energization in plant cells?

Ion-gradient-coupled transport systems in plants are normally electrophoretic and carry inward current. Rapid inward electrical currents elicited by K⁺, by urea and by lysine in the freshwater acidophilic alga Nitella translucens Agh. are all very strongly dependent on the presence of Na⁺ or (except in the case of K⁺) Li⁺. These results indicate that Na⁺-coupled solute transport in plants, which had previously been demonstrated only in an alkalophilic species (Chara australis), did not evolve recently as an alternative to H⁺-coupled transport in high-pH environments, and might therefore be more widely distributed than has hitherto been recognised.We are very grateful to Professor E.A.C. MacRobbie and Mr J. Banfield (Botany School, University of Cambridge) for supplies of Nitella translucens. Financial support for this work was obtained from the Australian Department of Industry, Technology and Commerce and the Joint Research Council's Biotechnology Collaboration Scheme between Britain and Australia (to N.A.W. and D.S.), and from an Agricultural and Food Research Council Grant (PG 87/501 to D.S.). D.S. was a Nuffield Foundation Science Research Fellow.     

Synthesis and characterization of phosphorescent iridium complexes containing trifluoromethyl-substituted phenyl pyridine based ligands

Several iridium complexes containing trifluoromethyl-substituted phenyl pyridine based ligands have been synthesized and characterized to try to investigate the effect of trifluoromethyl group and its position on physical properties. The complexes have the general structure of (C-N)₂Ir(LX), where the C-N are 2-phenylpyridine (ppy), 2-(3,5-bis-trifluoromethylphenyl)pyridine (fmppy), 2-(3,5-bis-trifluoromethylphenyl)-4-methylpyridine (fmpmpy), 2-(3,5-bis-trifluoromethylphenyl)-5-trifluoromethylpyridine (tfmppy) and the LX are 2-picolinic acid (pic) and acetylacetonate (acac). The (tfmppy)₂Ir(pic) was characterized using X-ray crystallography. The absorption, emission, and thermostability of the complexes were systematically investigated. Introduction of CF₃ substituents into 2-phenylpyridine in (ppy)₂Ir(pic) lead to some decrease in the sublimation temperature, which is more suitable to devices fabrication. The experimental results revealed that the emissive colors of these complexes could be finely tuned by suitable incorporation of trifluoromethyl substituents on the 2-phenylpyridine ligand, obtaining bright green-blue emission λ_max values from 471 to 489 nm in CH₂Cl₂ solution at room temperature, with high solution quantum efficiencies ranging from 0.37 to 1.89 relative to Ir(ppy)₃.     

The proximal N-terminal amino acid residues are required for the coupling activity of the bovine heart mitochondrial factor B

Treatment of the recombinant bovine factor B with trypsin yielded a fragment (amino acid residues 62-175) devoid of coupling activity. Removal of the N-terminal Trp2-Gly3-Trp4 peptide resulted in a significant loss of coupling activity in the FB_ΔW²_−W⁴ deletion mutant. Sucrose density gradient centrifugation demonstrated co-sedimentation of recombinant factor B with the ADP/ATP carrier, which is present in preparations of H⁺-translocating F₀F₁-ATPase, but not in preparations of complex V. The N-terminally truncated factor B mutant FB_ΔW²_−W⁴ did not co-sediment with the ADP/ATP carrier. Recombinant factor B co-sedimented with partially purified membrane sector F₀, extracted from F₁-stripped bovine submitochondrial particles with n-dodecyl-β-d-maltoside. Factor B inhibited the passive proton conductance catalyzed by F₀ reconstituted into asolectin liposomes. A factor B mutant, bearing a photoreactive unnatural amino acid pbenzoyl-l-phenylalanine (pBpa) substituted for Trp2, cross-linked with F₀ subunits e and g as well as the ADP/ATP carrier. These results suggest that the N-terminal domain and, in particular, the proximal N-terminal amino acids are important for the coupling activity and protein-protein interactions of bovine factor B.     

Structure and regulatory mechanism of Aquifex aeolicus NtrC4: variability and evolution in bacterial transcriptional regulation

Genetic changes lead gradually to altered protein function, making deduction of the molecular basis for activity from a sequence difficult. Comparative studies provide insights into the functional consequences of specific changes. Here we present structural and biochemical studies of NtrC4, a sigma-54 activator from Aquifex aeolicus, and compare it with NtrC1 (a paralog) and NtrC (a homolog from Salmonella enterica) to provide insight into how a substantial change in regulatory mechanism may have occurred. Activity assays show that assembly of NtrC4's active oligomer is repressed by the N-terminal receiver domain, and that BeF₃ ⁻ addition (mimicking phosphorylation) removes this repression. Observation of assembly without activation for NtrC4 indicates that it is much less strongly repressed than NtrC1. The crystal structure of the unactivated receiver-ATPase domain combination shows a partially disrupted interface. NMR structures of the regulatory domain show that its activation mechanism is very similar to that of NtrC1. The crystal structure of the NtrC4 DNA-binding domain shows that it is dimeric and more similar in structure to NtrC than NtrC1. Electron microscope images of the ATPase-DNA-binding domain combination show formation of oligomeric rings. Sequence alignments provide insights into the distribution of activation mechanisms in this family of proteins.     

Spatial and temporal distribution of fish and zooplankton in a shallow lake

Summary 1. We performed both a large- and a small-scale echo sounding study on the spatial and temporal distribution of fish (mainly roach, Rutilus rutilus and perch, Perca fluviatlis ), as well as a small-scale study of zooplankton distribution in the small, shallow and eutrophic Lake Hanebjerg in Denmark. In the small-scale study, sampling was conducted in open water as well as in the edge zone immediately outside two different types of vegetation.
2. Fish daytime abundances differed between the northern and the southern parts of the lake and, on a small scale, small fish aggregated in the edge zones during day, preferably outside dense emergent vegetation. Copepods avoided emergent vegetation, while cladocerans showed no habitat preference. Both small fish and cladoceran numbers were found to be higher during night than day.
3. The relative abundance (number per sample) of cladocerans in the edge zone immediately outside vegetation was negatively correlated with the relative abundance of fish in that zone. There was no correlation between cladoceran and fish abundance in open water, or between the relative abundance of copepods and fish.
4. The presence of pelagic piscivores in combination with avoidance behaviour of both fish and zooplankton is a likely explanation for the observed distribution of small fish and cladocerans in Lake Hanebjerg. Both small- and large-scale distribution patterns may be dependent on the type and distribution of complex structure in the lake. Even in a small lake, large-scale patterns may affect the interpretation of small-scale data.