Wheat, canola and grain legume access to soil phosphorus fractions differs in soils with contrasting phosphorus dynamics

Despite the high phosphorus (P) mobilizing capacity of many legumes, recent studies have found that, at least in calcareous soils, wheat is also able to access insoluble P fractions through yet unknown mechanism(s). We hypothesized that insoluble P fractions may be more available to non-legume plants in alkaline soils due to increased dissolution of the dominant calcium(Ca)-P pool into depleted labile P pools, whereas non-legumes may have limited access to insoluble P fractions in iron(Fe)- and aluminium(Al)-P dominated acid soils. Four crop species (faba bean, chickpea, wheat and canola) were grown on two acid and one alkaline soil under glasshouse conditions to examine rhizosphere processes and soil P fractions accessed. While all species generally depleted the H2O-soluble inorganic P (water Pi) pool in all soils, there was no net depletion of the labile NaHCO3-extractable inorganic P fraction (NaHCO3 Pi) by any species in any soil. The NaOH-extractable P fraction (NaOH Pi) in the alkaline soil was the only non-labile Pi fraction depleted by all crops (particularly canola), possibly due to increases in rhizosphere pH. Chickpea mobilized the insoluble HCl Pi and residual P fractions; however, rhizosphere pH and carboxylate exudation could not fully explain all of the observed Pi depletion in each soil. All organic P fractions appeared highly recalcitrant, with the exception of some depletion of the NaHCO3 Po fraction by faba bean in the acid soils. Chickpea and faba bean did not show a higher capacity than wheat or canola to mobilize insoluble P pools across all soil types, and the availability of various P fractions to legume and non-legume crops differed in soils with contrasting P dynamics

A comparison of the properties of manufactured soils produced from composting municipal green waste alone or with poultry manure or grease trap/septage waste

Manufactured soil for landscaping purposes was produced by composting for 6 weeks (1) municipal green waste alone, (2) green waste amended with 25% v/v poultry manure, or (3) green waste immersed in, and then removed from, a mixture of liquid grease trap waste/septage. Composting temperatures increased most rapidly and reached highest values (78°C) in the grease trap/septage-amended green waste. In comparison with green waste alone, addition of poultry manure prolonged the period of elevated temperatures and increased the maximum temperature attained from 52°C to 61°C. Following composting, each of the materials was split into (1) 100% compost, (2) 80% compost plus 20% v/v soil, and (3) 70% compost plus 20% soil plus 10% coal fly ash. Addition of poultry manure or grease trap/septage to green waste prior to composting increased bulk density and reduced total porosity of the composted product. Addition of soil, or soil and ash, to composts increased bulk density, reduced total porosity, decreased percentage macropores, and increased percentage mesopores and available water-holding capacity. Bicarbonate-extractable P, exchangeable NH and NO, electrical conductivity (EC), soluble C, soluble C as a percentage of organic C, basal respiration, and metabolic quotient were all markedly greater in the grease trap/septage-amended than poultry manure-amended or green waste alone treatments. Values for extractable P and EC were considered large enough to be damaging to plant growth and germination index (GI) of watercress was less than 60% for all grease trap/septage composts. Extractable P and EC were also high, and GI was 100%

Allosteric activation transitions in enzymes and biomolecular motors: insights from atomistic and coarse-grained simulations

The chemical step in enzymes is usually preceded by a kinetically distinct activation step that involves large-scale conformational transitions. In simple enzymes this step corresponds to the closure of the active site; in more complex enzymes, such as biomolecular motors, the activation step is more complex and may involve interactions with other biomolecules. These activation transitions are essential to the function of enzymes and perturbations in the scale and/or rate of these transitions are implicated in various serious human diseases; incorporating key flexibilities into engineered enzymes is also considered a major remaining challenge in rational enzyme design. Therefore it is important to understand the underlying mechanism of these transitions. This is a significant challenge to both experimental and computational studies because of the allosteric and multi-scale nature of such transitions. Using our recent studies of two enzyme systems, myosin and adenylate kinase (AK), we discuss how atomistic and coarse-grained simulations can be used to provide insights into the mechanism of activation transitions in realistic systems. Collectively, the results suggest that although many allosteric transitions can be viewed as domain displacements mediated by flexible hinges, there are additional complexities and various deviations. For example, although our studies do not find any evidence for cracking in AK, our results do underline the contribution of intra-domain properties (e.g., dihedral flexibility) to the rate of the transition. The study of mechanochemical coupling in myosin highlights that local changes important to chemistry require stabilization from more extensive structural changes; in this sense, more global structural transitions are needed to activate the chemistry in the active site. These discussions further emphasize the importance of better understanding factors that control the degree of co-operativity for allosteric transitions, again hinting at the intimate connection between protein stability and functional flexibility. Finally, a number of topics of considerable future interest are briefly discussed