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Search: WFRF:(Marangon D)

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1.
  • Romagnoli, F, et al. (author)
  • Windstorm impacts on European forest-related systems: an interdisciplinary perspective
  • 2023
  • In: Forest Ecology and Management. - 1872-7042 .- 0378-1127. ; 541
  • Journal article (peer-reviewed)abstract
    • Windstorms are considered the main disturbing abiotic agent in European forests. They affect a multiplicity of forest-related dimensions, such as forest ecology, forest operations, geomorphology, economy, and socio-cultural aspects. Due to the complex dynamics set off by windstorms, the design of post-windstorm forest management should be characterized by an interdisciplinary approach able to address multiple environmental and social needs. However, scientific literature investigating the impacts of windstorms on forests appears mainly focused on specific aspects. An interdisciplinary and more comprehensive approach is needed to cope with such multi-facet phenomena and to address future forest research.We reviewed current literature analyzing consequences of windstorms on European forests focusing on interconnections and cascade effects among forest-related dimensions in post-windstorm dynamics. We performed an in-depth review of 111 articles to detect most recurrent direct and indirect impacts as well as cascade effects among ecological, geomorphological, operational, economic, socio-cultural, and institutional forest-related dimensions. Our analysis aimed at providing a detailed analysis of the state of the art of windstorm impacts on European forests reported in literature, and suggesting an innovative approach to analyze windstorm consequences at a systemic level to acquire a comprehensive overview of post-windstorm dynamics.Our results showed that most of the studies dealt with interactions among ecological components of forests, but links between ecology, geomorphology, and society have been poorly studied. These knowledge gaps reduce the comprehension of windstorm impacts in the short and long terms and overlook the influence of societal-related aspects in post-windstorm forest management. Moreover, our analysis suggested the need of a post-windstorm management acting at systemic and comprehensive level, supported by forest policies that promotes multifunctionality to overcome challenges derived by natural disturbances intensification.
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2.
  • Santos-Silva, Teresa, et al. (author)
  • Kinetic, Structural, and EPR Studies Reveal That Aldehyde Oxidoreductase from Desulfovibrio gigas Does Not Need a Sulfido Ligand for Catalysis and Give Evidence for a Direct Mo-C Interaction in a Biological System
  • 2009
  • In: Journal of the American Chemical Society. - : American Chemical Society (ACS). - 0002-7863 .- 1520-5126. ; 131, s. 7990-7998
  • Journal article (peer-reviewed)abstract
    • Aldehyde oxidoreductase from Desulfovibrio gigas (DgAOR) is a member of the xanthine oxidase (XO) family of mononuclear Mo-enzymes that catalyzes the oxidation of aldehydes to carboxylic acids. The molybdenum site in the enzymes of the XO family shows a distorted square pyramidal geometry in which two ligands, a hydroxyl/water molecule (the catalytic labile site) and a sulfido ligand, have been shown to be essential for catalysis. We report here steady-state kinetic studies of DgAOR with the inhibitors cyanide, ethylene glycol, glycerol, and arsenite, together with crystallographic and EPR studies of the enzyme after reaction with the two alcohols. In contrast to what has been observed in other members of the XO family, cyanide, ethylene glycol, and glycerol are reversible inhibitors of DgAOR. Kinetic data with both cyanide and samples prepared from single crystals confirm that DgAOR does not need a sulfido ligand for catalysis and confirm the absence of this ligand in the coordination sphere of the molybdenum atom in the active enzyme. Addition of ethylene glycol and glycerol to dithionite-reduced DgAOR yields rhombic Mo(V) EPR signals, suggesting that the nearly square pyramidal coordination of the active enzyme is distorted upon alcohol inhibition. This is in agreement with the X-ray structure of the ethylene glycol and glycerol-inhibited enzyme, where the catalytically labile OH/OH2 ligand is lost and both alcohols coordinate the Mo site in a η2 fashion. The two adducts present a direct interaction between the molybdenum and one of the carbon atoms of the alcohol moiety, which constitutes the first structural evidence for such a bond in a biological system.
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