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- Lecerof, David, et al.
(författare)
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Metal binding to Bacillus subtilis ferrochelatase and interaction between metal sites.
- 2003
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Ingår i: Journal of Biological Inorganic Chemistry. - : Springer Science and Business Media LLC. - 1432-1327 .- 0949-8257. ; 8:4, s. 452-458
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Tidskriftsartikel (refereegranskat)abstract
- Ferrochelatase, the terminal enzyme in heme biosynthesis, catalyses metal insertion into protoporphyrin IX. The location of the metal binding site with respect to the bound porphyrin substrate and the mode of metal binding are of central importance for understanding the mechanism of porphyrin metallation. In this work we demonstrate that Zn2+, which is commonly used as substrate in assays of the ferrochelatase reaction, and Cd2+, an inhibitor of the enzyme, bind to the invariant amino acids His183 and Glu264 and water molecules, all located within the porphyrin binding cleft. On the other hand, Mg2+, which has been shown to bind close to the surface at 7 Å from His183, was largely absent from its site. Activity measurements demonstrate that Mg2+ has a stimulatory effect on the enzyme, lowering KM for Zn2+ from 55 to 24 µM. Changing one of the Mg2+ binding residues, Glu272, to serine abolishes the effect of Mg2+. It is proposed that prior to metal insertion the metal may form a sitting-atop (SAT) complex with the invariant His-Glu couple and the porphyrin. Metal binding to the Mg2+ site may stimulate metal release from the protein ligands and its insertion into the porphyrin.
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- Olsson, Emma, 1974-
(författare)
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Many-body Problems in the Theory of Stellar Collapse and Neutron Stars
- 2004
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Doktorsavhandling (övrigt vetenskapligt/konstnärligt)abstract
- When modelling the collapse of massive stars leading to supernova explosions and the cooling of neutron stars, understanding the microphysical processes, such as the interaction of neutrinos within a dense medium are of vital importance. The interaction of neutrinos with nucleons (neutrons and protons) is altered by the presence of the medium, compared to the same process with free nucleons. Neutrino scattering and production processes may be characterized in terms of the excitations that are created or destroyed in the nuclear medium. One way to analyse the effects of the medium is by using Landau's theory of normal Fermi liquids. This theory gives simple relationships between physical quantities such as the spin susceptibility or the response to a weak interaction probe in terms of Landau parameters, that are measures of the interaction between quasiparticles. One problem when using Landau Fermi liquid theory for nucleon matter is that the interaction has a tensor component. The tensor interaction does not conserve the total spin and, as a consequence, there are generally contributions to long-wavelength response functions from states that have more than one quasiparticle-quasihole pair in the intermediate state. Such contributions cannot be calculated in terms of Landau parameters alone, since in the usual formulation of Landau theory, only singlepair excitations are considered. In this thesis three problems are addressed. First, we obtain bounds on the contributions from more than one quasiparticle-quasihole pair by using sum-rule arguments. Second, we derive expressions for static response functions allowing for the tensor components of the interaction. We analyse which the most important effects are on the static response of nucleon matter, and find that the major contributions comes from renormalization of coupling constants and transitions to states with more than one quasiparticle-quasihole pair. Third, we show how contributions to the dynamical response coming from states containing two quasiparticle-quasihole pairs may be evaluated in terms of Landau theory if one allows for the effect of collisions in the Landau kinetic equation. We consider the case of asymmetric nuclear matter, and our work goes beyond earlier works in that they contain the effects of collisions in addition to those of the mean field.
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- Sernland, Emma, et al.
(författare)
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Does information sharing promote group foraging?
- 2003
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Ingår i: Royal Society of London. Proceedings B. Biological Sciences. - : The Royal Society. - 1471-2954. ; 270:1520, s. 1137-1141
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Tidskriftsartikel (refereegranskat)abstract
- Individuals may join groups for several reasons, one of which is the possibility of sharing information about the quality of a foraging area. Sharing information in a patch-foraging scenario gives each group member an opportunity to make a more accurate estimate of the quality of the patch. In this paper we present a mathematical model in which we study the effect of group size on patch-leaving policy and per capita intake rate. In the model, group members share information equally in a random search for food. Food is distributed in patches according to a negative binomial distribution. A prediction from our model is that, the larger the group, the earlier each group member should leave the current patch. We also find that the benefit from enhanced exchange of information does not exceed the cost of sharing food with group members. The per capita intake rate decreases as the group size increases. Therefore, animals should only form groups when other factors outweigh the costs, which is easiest to achieve when the travelling time is short.
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| 10. |
- Sigfridsson, Emma, et al.
(författare)
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A comparison of the inner-sphere reorganization energies of cytochromes, iron-sulphur clusters, and blue copper proteins
- 2001
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Ingår i: The Journal of Physical Chemistry Part B. - : American Chemical Society (ACS). - 1520-5207 .- 1520-6106. ; 105:23, s. 5546-5552
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Tidskriftsartikel (refereegranskat)abstract
- Inner-sphere reorganization energies have been calculated for a number of models of six-coordinate iron porphyrins (with varying axial ligands), using the density functional B3LYP method. If the axial ligands are uncharged, the reorganization energy is very low, 5-9 kJ/mol. If one of the axial ligands is charged, the reorganization energy is higher, 20-47 kJ/mol, but such sites are normally not used in electron carriers. The former reorganization energies are appreciably smaller than what was found for blue copper proteins (62-90 kJ/mol), the dimeric CuA site in cytochrome c oxidase and nitrous oxide reductase (43 kJ/mol), and six different types of iron-sulfur clusters with one, two, or four iron atoms (40-75 kJ/mol), even if these vacuum energies are typically halved inside the protein (as a result of hydrogen bonds and solvation effects). Therefore, the cytochromes seem to have the inherently lowest inner-sphere reorganization energy of the three commonly used electron carriers. All three types of sites have reduced the reorganization energy by using a delocalized charge and N- and S-donors (rather than O-donors) as metal ligands. Moreover, iron is a more appropriate metal for electron transfer than copper because Fe(II) and Fe(III) prefer the same coordination number and geometry and give bonds weaker than those of copper. The low-spin state of the cytochrome has a ∼20 kJ/mol lower reorganization energy than that of the corresponding high-spin site. Moreover, ring strain in the porphyrin reduce the changes in the Fe-NPor distances by 5 pm and therefore the reorganization energy by 8 kJ/mol.
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