Alternatively, exudation by ectomycorrhizal fungi could provide b

Alternatively, exudation by ectomycorrhizal fungi could provide bacterial denitrifiers within the mycorrhizosphere with C and stimulate N2O production. The quality of this C could have

implications on N2O : N2 product ratios (Firestone, 1982; Henry et al., 2008). (2) N availability: bacteria have a higher demand for nutrients due to their lower C : N ratio compared with fungi, but ectomycorrhizal fungi are more efficient at capturing nutrients (Schimel & Bennett, 2004); by competing for available N, ectomycorrhizal fungi could negatively affect N2O production. (3) Moisture content: fungal hyphae can penetrate into and drain water buy C59 wnt from fine soil pores, thus affecting anaerobic microsites. The mycelial network generally improves soil aeration, which would lower bacterial N2O production. However, at local microsites, N2O production http://www.selleckchem.com/products/MDV3100.html may be stimulated as a result of O2 limitation due to hyphal respiration or soil wetting from the release of fungal exudates. Thus, bacterial N2O production needs to be evaluated in light of the positive and negative impacts of ectomycorrhizal fungi. As ectomycorrhizal fungi may have both direct and indirect roles to play in forest N2O production, this will have implications for forest management practices seeking

to lower net emissions, particularly as the symbiotic nature of ectomycorrhizal fungi means that N2O production in these soils may be more closely coupled to the plant than previously thought. We thank Hedda Weitz for helpful discussions. This work was funded by the Natural Environment Research Council: a PhD studentship awarded to M.T.P.-M. and Advanced Research Fellowships awarded to E.M.B. and Tau-protein kinase D.J. “
“Institute of Marine Biochemistry, Vietnam Academy of Science and Technology, Cau Giay, Hanoi, Vietnam The O-demethylases of anaerobes are corrinoid-dependent, ether-cleaving methyltransferase enzyme systems consisting of four components. The interaction of the O-demethylase components of the acetogenic

bacterium Acetobacterium dehalogenans was studied by protein mobility on native PAGE, far-Western blot analysis and yeast two-hybrid screen. Using native PAGE and far-Western blot, the interaction of the activating enzyme (AE) with its substrate, the corrinoid protein (CP), could be observed. The interaction occurred with four different CPs of A. dehalogenans and a CP from Desulfitobacterium hafniense DCB-2, all involved in ether cleavage. In the corrinoid reduction assay, the AE reduced all CPs tested. This result indicates a broad substrate specificity of the AE of A. dehalogenans. In addition, an interaction of the A. dehalogenans CP of the vanillate-O-demethylase with the two methyltransferases of the same enzyme system was observed.

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