The seasonally of both rainfall and solar irradiance might influence the evolution of flowering and fruiting in tropical forests. In seasonally dry forests, to the degree that soil moisture limits plant productivity, community-wide peaks in reproduction are expected during the rainy season, with seedfall and germination timed to allow seedlings to become well established while soil moisture is available. Where soil moisture is never seasonally limiting, seasonal changes in light availability caused by periods of cloudiness or seasonally low zenithal sun angles should favour reproduction during seasons when irradiance levels are high. To evaluate these predictions, we documented the timing of flower and fruit fall for 10 and 15 y at El Verde, Puerto Rico, and Barro Colorado Island (BCI), Panama. At El Verde, rainfall is abundant year-round and solar declination largely determines seasonal variation in irradiance. At BCI, rainfall is abundant throughout the 8-mo wet season while drought develops and average solar irradiance increases by 40-50% over the 4-mo dry season. Seasonal variation in the number of species flowering and fruiting at both sites was generally consistent with the hypothesis that seasonal variation in irradiance limits the evolution of reproductive phenologies. Community-level metrics provided no evidence for a similar role for moisture availability at BCI. Seasonal variation in irradiance also strongly influenced seed development times at both sites. Thus, communitywide phenologies reveal a strong signature of seasonal changes in irradiance, even in those forests that exhibit some degree of seasonally in rainfall.
The effect of modulating the structural dynamics by incremental glycosylation on enzyme activity and thermostability has thus far only been investigated in detail for the serine protease α-chymotrypsin (for a recent review see Solá et al., Cell. Mol. Life Sci. 2007, 64(16):2133-2152. Herein, we extend this type of study to a structurally unrelated serine protease, specifically, subtilisin Carlsberg. The protease was glycosylated with activated lactose and various lactose-subtilisin conjugates were obtained and characterized. Near UV-CD spectroscopy revealed that the tertiary structure was unaffected by the procedure. H/D exchange FT-IR spectroscopy was performed to assess the structural dynamics of the enzyme. It was found that increasing the level of glycosylation caused a linearly dependent reduction in structural dynamics. This led to an increase in thermostability and a decrease in the catalytic turnover rate for both, acylation and de-acylation step. These data highlight the possibility that a structural dynamics -activity relationship might be a phenomenon generally found in serine proteases.
We constructed lactate biosensors by immobilization of lactate oxidase (LOx) onto a single-walled carbon nanotube (SWCNT) electrode. The first step of the sensor construction was the immobilization of oxidized SWCNT onto a platinum electrode modified with 4-aminothiophenol (4-ATP). Two enzyme immobilization methods were used to construct the biosensors, i.e., covalent immobilization using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride (EDC) and physical adsorption. Atomic force microscopy (AFM) experiments confirmed the immobilization of SWCNT during the biosensor construction and X-ray photoelectron spectroscopy (XPS) experiments confirmed covalent immobilization of LOx onto the SWCNT in the first method. The biosensor based on covalent enzyme immobilization showed a sensitivity of 5.8 μA/mM, a linearity up to 0.12 mM of L-lactate, and a detection limit of 4.0 μM. The biosensor based on protein adsorption displayed a sensitivity of 9.4 μA/mM, retaining linearity up to 0.18 mM of L-lactate with a detection limit of 3.0 μM. The difference in the biosensor response can be attributed to protein conformational or dynamical changes during covalent immobilization. The stability of the biosensors was tested at different temperatures and after different storage periods. The thermostability of the biosensors after incubation at 60°C demonstrated that the biosensor with covalently immobilized LOx retained a higher response compare with the adsorbed protein. Long-term stability experiments show a better residual activity of 40% for the covalently immobilized protein compared to 20% of residual activity for the adsorbed protein after 25 d storage. Covalent protein immobilization was superior compared to adsorption in preserving biosensor functionality over extended time period.
In this study, electrochemical impedance spectroscopy was used for the first time to study the adsorption of dopamine in carbon fiber microelectrodes. In order to show a proof-of-concept, static and dynamic measurements were taken at potentials ranging from -0.4 to 0.8 V versus Ag|AgCl to demonstrate the versatility of this technique to study dopamine without the need of its oxidation. We used electrochemical impedance spectroscopy and single frequency electrochemical impedance to measure different concentrations of dopamine as low as 1 nM. Moreover, the capacitance of the microelectrodes surface was found to decrease due to dopamine adsorption, which is dependent on its concentration. The effect of dissolved oxygen and electrochemical oxidation of the surface in the detection of dopamine was also studied. Nonoxidized and oxidized carbon fiber microelectrodes were prepared and characterized by optical microscopy, scanning electron microscopy, cyclic voltammetry, and electrochemical impedance spectroscopy. Optimum working parameters of the electrodes, such as frequency and voltage, were obtained for better measurement. Electrochemical impedance of dopamine was determined at different concentration, voltages, and frequencies. Finally, dynamic experiments were conducted using a flow cell and single frequency impedance in order to study continuous and real-time measurements of dopamine.
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