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Coherently addressing the 17 Sustainable Development Goals requires planning tools that guide policy makers. Given the integrative nature of the SDGs, we believe that integrative modelling techniques are especially useful for this purpose. In this paper, we present and demonstrate the use of the new System Dynamics based iSDG family of models. We use a national model for Tanzania to analyse impacts of substantial investments in photovoltaic capacity. Our focus is on the impacts on three SDGs: SDG 3 on healthy lives and well-being, SDG 4 on education, and SDG 7 on energy. In our simulations, the investments in photovoltaics positively affect life expectancy, years of schooling and access to electricity. More importantly, the progress on these dimensions synergizes and leads to broader system-wide impacts. While this one national example illustrates the anticipated impact of an intervention in one specific area on several SDGs, the iSDG model can be used to support similar analyses for policies related to all the 17 SDGs, both individually and concurrently. We believe that integrated models such as the iSDG model can bring interlinks to the forefront and facilitate a shift to a discussion on development grounded in systems thinking.
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http://dx.doi.org/10.1007/s11625-017-0457-x | DOI Listing |
Inorg Chem
November 2019
Department of Chemistry , University of Vermont, Burlington , Vermont 05405 , United States.
IsdG catalyzes a unique trioxygenation of heme to staphylobilin, and the data presented in this article elucidate the mechanism of the novel chemical transformation. More specifically, the roles of the second-sphere Asn and Trp residues in the monooxygenation of ferric-peroxoheme have been clarified via spectroscopic characterization of the ferric-azidoheme analogue. Analysis of UV/vis absorption data quantified the strength of the hydrogen bond that exists between the Asn7 side chain and the azide moiety of ferric-azidoheme.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
November 2019
The Millennium Institute, Washington, DC 20037;
As countries pursue sustainable development across sectors as diverse as health, agriculture, and infrastructure, sectoral policies interact, generating synergies that alter their effectiveness. Identifying those synergies ex ante facilitates the harmonization of policies and provides an important lever to achieve the sustainable development goals (SDGs) of the United Nations 2030 Agenda. However, identifying and quantifying these synergetic interactions are infeasible with traditional approaches to policy analysis.
View Article and Find Full Text PDFBiochemistry
November 2019
(Mtb), the causative agent of tuberculosis, requires iron for survival. In Mtb, MhuD is the cytosolic protein that degrades imported heme. MhuD is distinct, in both sequence and structure, from canonical heme oxygenases (HOs) but homologous with IsdG-type proteins.
View Article and Find Full Text PDFMycobacterium tuberculosis heme-degrading protein MhuD degrades heme to mycobilin isomers and iron, while its closest homologues from Staphylococcus aureus, IsdG and IsdI, degrade heme to staphylobilin isomers, formaldehyde, and iron. Superposition of the structures of the heme-bound complexes reveals that the heme molecule in the MhuD active site is rotated ∼90° about the tetrapyrrole plane with respect to IsdG and IsdI active site heme molecules. Therefore, the variation in IsdG/IsdI and MhuD chromophore products may be attributed to the different heme orientations.
View Article and Find Full Text PDFMol Microbiol
August 2018
Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal.
Haem is an essential cofactor in central metabolic pathways in the vast majority of living systems. Prokaryotes acquire haem via haem biosynthesis pathways, and some also utilize haem uptake systems, yet it remains unclear how they balance haem requirements with the paradox that free haem is toxic. Here, using the model pathogen Staphylococcus aureus, we report that IsdG, one of two haem oxygenase enzymes in the haem uptake system, inhibits the formation of haem via the internal haem biosynthesis route.
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