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  • 1
    Publication Date: 2020-10-09
    Language: English
    Type: article , doc-type:article
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  • 2
    Publication Date: 2020-11-17
    Language: English
    Type: article , doc-type:article
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  • 3
    Publication Date: 2020-11-17
    Language: English
    Type: conferenceobject , doc-type:conferenceObject
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  • 4
    ISSN: 1432-0495
    Keywords: Key words Transport ; Bacteria ; Iron ; Groundwater
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences
    Notes: Abstract  Among the demonstrated processes influencing the transport of bacteria through aquifers, the deposition of cells on mineral surfaces is one of the most important. For example, understanding the transport of introduced bacteria through aquifers is essential to designing some in situ bioremediation schemes. The impact of the presence and distribution of Fe(III)-oxyhydroxide-coated sand grains on bacterial transport through porous media was evaluated in column experiments in which bacteria (short rods; 1.2 μm length) were eluted through columns of quartz sand (0.5–0.6 mm in diameter) for several conditions of chemical heterogeneity of mineral substrate. Fe(III)-oxyhydroxide-coated sand was present as 10% of the mass, and it was arranged in three treatments: (1) homogeneously distributed, and present as a discrete layer (2) at the top and (3) at the bottom of 14-cm-long sand columns. A pulse input of 108 cells ml–1 was introduced in an artificial groundwater solution flowing at 14 cm h–1 through the column, and eluted cells were counted. Peak breakthrough occurred at 1.0 pore volume. A large proportion of cells were retained; 14.7–15.8% of the cells were recovered after three pore volumes of solution had eluted through clean quartz sand, and only 2.1–4.0% were recovered from the Fe(III)-oxyhydroxide-coated sand mixtures. The three physical arrangements of the chemical heterogeneity resulted in essentially the same breakthrough of cells, indicating that the spatial distribution of iron coating does not affect the transport of bacteria. The results of the column transport experiments, which mimic hydrogeological conditions encountered in field problems, are consistent with our mechanistic understanding of bacterial sorption.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 48 (1970), S. 1243-1244 
    ISSN: 1432-1440
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Summary In the course of hemodialysis, free plasma cortisol is excreted into the dialysate, provoking a considerable decrease of plasma cortisol levels. A counterregulation mechanism results which, in turn, leads to increased ACTH secretion and subsequently increased cortisol production at an approximately 4 hours' rhythm.
    Notes: Zusammenfassung Durch die extracorporale Hämodialyse kommt es zu einer Ausscheidung des freien Plasmacortisols in das Dialysat. Dies bewirkt ein stärkeres Absinken des Plasmacortisolspiegels, was einen Gegenregulationsmechanismus auslöst, der über vermehrte ACTH-Ausschüttung zur vermehrten Cortisolproduktion in einem ungefähr vierstündigen Rhythmus führt.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-1017
    Keywords: Key words Bacterial photosynthesis ; Electron transfer ; Protein electrostatics ; Poisson-Boltzmann equation ; Conformational flexibility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The conventional method to determine protonation patterns of proteins was extended by explicit consideration of structural relaxation. The inclusion of structural relaxation was achieved by alternating energy minimization with the calculation of protonation pattern in an iterative manner until consistency of minimized structure and protonation pattern was reached. We applied this method to the bacterial photosynthetic reaction center (bRC) of Rps. viridis and could show that the relaxation procedure accounts for the nuclear polarization and therefore allows one to lower the dielectric constant for the protein from the typically chosen value of ɛ p = 4 to a value of ɛ p = 2 without fundamentally changing the results. Owing to the lower dielectric shielding at ɛ p = 2, the charges of the titratable groups interact more strongly, which leads to sampling problems during Monte Carlo titration. We solved this problem by introducing triple moves in addition to the conventional single and double moves. We also present a new method that considers ensembles of protein conformations for the calculation of protonation patterns. Our method was successfully applied to calculate the redox potential differences of the quinones in the bRC using the relaxed structures for the different redox states of the quinones.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-1017
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 89 (1988), S. 3394-3395 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 90 (1989), S. 354-365 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: A description of electron transfer processes is presented which makes use of the concept of solitary states for the construction of the initial and the final state wave functions. Even though this concept is closely related to an adiabatic description in the sense that it provides partial delocalization of these states it also assures localization for a symmetric donor–acceptor system. The theory can be applied to arbitrary values of the internal parameters characterizing the system, that is the electronic donor–acceptor coupling V, the free energy change ΔE, and the coupling of the electron to nuclear motions represented by a Stokes shift S. This way the theory of nonadiabatic electron transfer processes is put on equal footing with the theory of adiabatic transitions and even more interestingly the same concept unifies the common electron transfer theory and the theory of internal conversion processes if ||ΔE|| and (or) ||V|| exceed S. It is shown analytically how the results of the conventional treatments for adiabatic, nonadiabatic, and internal conversion processes fall out of this theory as special cases. It is further examplified how the system develops from the so-called normal regime with ||ΔE||〈S into the inverted regime with ||ΔE||〉S as function of ΔE for fixed parameters of V and S and as function of V for fixed parameters of ΔE and S.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 87 (1987), S. 3880-3887 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The electron transfer process from cytochrome c to the special pair is revisited. In the present model the transfer rate in photosynthetic reaction centers of Chromatium vinosum is modulated by fluctuations of the dielectric constant of the protein environment between the donor and acceptor site. The fluctuations enter the rate expression as the inverse of a Lamb–Mössbauer factor. The strong temperature dependence of the transfer rate can thus be related to protein specific dynamics. Experimental evidence about such dynamics is provided by recently recorded Mössbauer spectra of iron containing proteins [Parak et al., J. Mol. Biol. 161, 177 (1982)].
    Type of Medium: Electronic Resource
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