Thermomechanical design rules for photovoltaic modules

We present a set of thermomechanical design rules to support and accelerate future (PV) module developments. The design rules are derived from a comprehensive parameter sensitivity study of different PV module layers and material properties by finite element method simulations. We develop a three dimensional finite element method (FEM) model, which models the PV module geometry in detail from busbar and ribbons up to the frame including the adhesive. The FEM simulation covers soldering, lamination, and mechanical load at various temperatures. The FEM model is validated by mechanical load tests on three 60-cell PV modules. Here, for the first time, stress within a solar cell is measured directly using stress sensors integrated in solar cells (SenSoCells®). The results show good accordance with the simulations. The parameter sensitivity study reveals that there are two critical interactions within a PV module: (1) between ribbon and solar cell and (2) between front/back cover and interconnected solar cells. Here, the encapsulant plays a crucial role in how the single layers interact with each other. Therefore, its mechanical properties are essential, and four design rules are derived regarding the encapsulant. Also four design rules concern front and back sides, and three address the solar cells. Finally, two design rules each deal with module size and frame, respectively. Altogether we derive a set of 15 thermomechanical design rules. As a rule of thumb of how well a bill of material will work from a thermomechanical point of view, we introduce the concept of specific thermal expansion stiffness ${\hat{E}}_{\alpha }=E\cdotp \alpha \cdotp {A}_{\mathrm{j}}\cdotp h$ as the product of Young\u27s modulus E, coefficient of thermal expansion $\alpha$, joint area A$_{j}$, and materials height h. The difference between two materials is a measure of how much thermal strain one material can induce in another. A strong difference means that the material with the larger value will induce thermal strain in the other

Influence of association state and DNA binding on the O2-reactivity of [4Fe-4S] fumarate and nitrate reduction (FNR) regulator

The fumarate and nitrate reduction (FNR) regulator is the master switch for the transition between anaerobic and aerobic respiration in Escherichia coli. Reaction of dimeric [4Fe-4S] FNR with O2 results in conversion of the cluster into a [2Fe-2S] form, via a [3Fe-4S] intermediate, leading to the loss of DNA binding through dissociation of the dimer into monomers. In the present paper, we report studies of two previously identified variants of FNR, D154A and I151A, in which the form of the cluster is decoupled from the association state. In vivo studies of permanently dimeric D154A FNR show that DNA binding does not affect the rate of cluster incorporation into the apoprotein or the rate of O2-mediated cluster loss. In vitro studies show that O2-mediated cluster conversion for D154A and the permanent monomer I151A FNR is the same as in wild-type FNR, but with altered kinetics. Decoupling leads to an increase in the rate of the [3Fe-4S]1+ into [2Fe-2S]2+ conversion step, consistent with the suggestion that this step drives association state changes in the wild-type protein. We have also shown that DNA-bound FNR reacts more rapidly with O2 than FNR free in solution, implying that transcriptionally active FNR is the preferred target for reaction with O2

DNA binding shifts the redox potential of the transcription factor SoxR

Electrochemistry measurements on DNA-modified electrodes are used to probe the effects of binding to DNA on the redox potential of SoxR, a transcription factor that contains a [2Fe-2S] cluster and is activated through oxidation. A DNA-bound potential of +200 mV versus NHE (normal hydrogen electrode) is found for SoxR isolated from Escherichia coli and Pseudomonas aeruginosa. This potential value corresponds to a dramatic shift of +490 mV versus values found in the absence of DNA. Using Redmond red as a covalently bound redox reporter affixed above the SoxR binding site, we also see, associated with SoxR binding, an attenuation in the Redmond red signal compared with that for Redmond red attached below the SoxR binding site. This observation is consistent with a SoxR-binding-induced structural distortion in the DNA base stack that inhibits DNA-mediated charge transport to the Redmond red probe. The dramatic shift in potential for DNA-bound SoxR compared with the free form is thus reconciled based on a high-energy conformational change in the SoxR–DNA complex. The substantial positive shift in potential for DNA-bound SoxR furthermore indicates that, in the reducing intracellular environment, DNA-bound SoxR is primarily in the reduced form; the activation of DNA-bound SoxR would then be limited to strong oxidants, making SoxR an effective sensor for oxidative stress. These results more generally underscore the importance of using DNA electrochemistry to determine DNA-bound potentials for redox-sensitive transcription factors because such binding can dramatically affect this key protein property

Silicon solar cell–integrated stress and temperature sensors for photovoltaic modules

We propose silicon solar cell–integrated stress and temperature sensors as a new approach for the stress and temperature measurement in photovoltaic (PV) modules. The solar cell–integrated sensors enable a direct and continuous in situ measurement of mechanical stress and temperature of solar cells within PV modules. In this work, we present a proof of concept for stress and temperature sensors on a silicon solar cell wafer. Both sensors were tested in a conventional PV module setup. For the stress sensor, a sensitivity of (−47.41 ± 0.14)%/GPa has been reached, and for the temperature sensor, a sensitivity of (3.557 ± 0.008) × 10$^{-3}$ K$^{-1}$ has been reached. These sensors can already be used in research for increased measurement accuracy of the temperature and the mechanical stress in PV modules because of the implementation at the precise location of the solar cells within a laminate stack, for process evaluation, in‐situ measurements in reliability tests, and the correlation with real exposure to climates

Biochemical properties of Paracoccus denitrificans FnrP:Reactions with molecular oxygen and nitric oxide

In Paracoccus denitrificans, three CRP/FNR family regulatory proteins, NarR, NnrR and FnrP, control the switch between aerobic and anaerobic (denitrification) respiration. FnrP is a [4Fe-4S] cluster containing homologue of the archetypal O2 sensor FNR from E. coli and accordingly regulates genes encoding aerobic and anaerobic respiratory enzymes in response to O2, and also NO, availability. Here we show that FnrP undergoes O2-driven [4Fe-4S] to [2Fe-2S] cluster conversion that involves up to 2 O2 per cluster, with significant oxidation of released cluster sulfide to sulfane observed at higher O2 concentrations. The rate of the cluster reaction was found to be ~6-fold lower than that of E. coli FNR, suggesting that FnrP can remain transcriptionally active under microaerobic conditions. This is consistent with a role for FnrP in activating expression of the high O2 affinity cytochrome c oxidase under microaerobic conditions. Cluster conversion resulted in dissociation of the transcriptionally active FnrP dimer into monomers. Therefore, along with E. coli FNR, FnrP belongs to the subset of FNR proteins in which cluster type is correlated with association state. Interestingly, two key charged residues, Arg140 and Asp154, that have been shown to play key roles in the monomer-dimer equilibrium in E. coli FNR are not conserved in FnrP, indicating that different protomer interactions are important for this equilibrium. Finally, the FnrP [4Fe-4S] cluster is shown to undergo reaction with multiple NO molecules, resulting in iron nitrosyl species and dissociation into monomers

Small-volume potentiometric titrations: EPR investigations of Fe-S cluster N2 in mitochondrial complex

EPR-based potentiometric titrations are a well-established method for determining the reduction potentials of cofactors in large and complex proteins with at least one EPR-active state. However, such titrations require large amounts of protein. Here, we report a new method that requires an order of magnitude less protein than previously described methods, and that provides EPR samples suitable for measurements at both X- and Q-band microwave frequencies. We demonstrate our method by determining the reduction potential of the terminal [4Fe-4S] cluster (N2) in the intramolecular electron-transfer relay in mammalian respiratory complex I. The value determined by our method, Em7 = − 158 mV, is precise, reproducible, and consistent with previously reported values. Our small-volume potentiometric titration method will facilitate detailed investigations of EPR-active centres in non-abundant and refractory proteins that can only be prepared in small quantities

Comments on "the interpretation of the EPR and Mossbauer spectra of two-iron, one-electron iron-sulfur proteins"

Evidence is presented indicating that the note mentioned in the title is incorrect in two important aspects. 1.) According to our results of ENDOR spectroscopy and computer simulations of Mossbauer spectra, the conclusions drawn are based on an erroneous interpretation of the Mossbauer spectra. 2.) According to quotations from the literature, previous interpretations of experimental data on iron-sulfur proteins are incorrectly represented.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/33508/1/0000005.pd

Structure and Molecular Evolution of CDGSH Iron-Sulfur Domains

The recently discovered CDGSH iron-sulfur domains (CISDs) are classified into seven major types with a wide distribution throughout the three domains of life. The type 1 protein mitoNEET has been shown to fold into a dimer with the signature CDGSH motif binding to a [2Fe-2S] cluster. However, the structures of all other types of CISDs were unknown. Here we report the crystal structures of type 3, 4, and 6 CISDs determined at 1.5 Å, 1.8 Å and 1.15 Å resolution, respectively. The type 3 and 4 CISD each contain one CDGSH motif and adopt a dimeric structure. Although similar to each other, the two structures have permutated topologies, and both are distinct from the type 1 structure. The type 6 CISD contains tandem CDGSH motifs and adopts a monomeric structure with an internal pseudo dyad symmetry. All currently known CISD structures share dual iron-sulfur binding modules and a β-sandwich for either intermolecular or intramolecular dimerization. The iron-sulfur binding module, the β-strand N-terminal to the module and a proline motif are conserved among different type structures, but the dimerization module and the interface and orientation between the two iron-sulfur binding modules are divergent. Sequence analysis further shows resemblance between CISD types 4 and 7 and between 1 and 2. Our findings suggest that all CISDs share common ancestry and diverged into three primary folds with a characteristic phylogenetic distribution: a eukaryote-specific fold adopted by types 1 and 2 proteins, a prokaryote-specific fold adopted by types 3, 4 and 7 proteins, and a tandem-motif fold adopted by types 5 and 6 proteins. Our comprehensive structural, sequential and phylogenetic analysis provides significant insight into the assembly principles and evolutionary relationship of CISDs