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- Kjær, Kasper Skov, et al.
(author)
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Luminescence and reactivity of a charge-transfer excited iron complex with nanosecond lifetime
- 2019
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In: Science. - : American Association for the Advancement of Science (AAAS). - 0036-8075 .- 1095-9203. ; 363:6424, s. 249-253
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Journal article (peer-reviewed)abstract
- Iron’s abundance and rich coordination chemistry are potentially appealing features for photochemical applications. However, the photoexcitable charge-transfer (CT) states of most Fe complexes are limited by picosecond or sub-picosecond deactivation through low-lying metal centered (MC) states, resulting in inefficient electron transfer reactivity and complete lack of photoluminescence. Here we show that octahedral coordination of Fe(III) by two mono-anionic facial tris-carbene ligands can suppress such deactivation dramatically. The resulting complex [Fe(phtmeimb)2]+, where phtmeimb is [phenyl(tris(3-methylimidazol-1-ylidene))borate]-, exhibits strong, visible, room temperature photoluminescence with a 2.0 ns lifetime and 2% quantum yield via spin-allowed transition from a ligand-to-metal charge-transfer (2 LMCT) state to the ground state (2 GS). Reductive and oxidative electron transfer reactions were observed for the2 LMCT state of [Fe(phtmeimb)2]+ in bimolecular quenching studies with methylviologen and diphenylamine.
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2. |
- Arnlund, David, et al.
(author)
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Visualizing a protein quake with time-resolved X-ray scattering at a free-electron laser
- 2014
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In: Nature Methods. - : Springer Science and Business Media LLC. - 1548-7091 .- 1548-7105. ; 11:9, s. 923-926
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Journal article (peer-reviewed)abstract
- We describe a method to measure ultrafast protein structural changes using time-resolved wide-angle X-ray scattering at an X-ray free-electron laser. We demonstrated this approach using multiphoton excitation of the Blastochloris viridis photosynthetic reaction center, observing an ultrafast global conformational change that arises within picoseconds and precedes the propagation of heat through the protein. This provides direct structural evidence for a 'protein quake': the hypothesis that proteins rapidly dissipate energy through quake-like structural motions.
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3. |
- Haldrup, Kristoffer, et al.
(author)
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Ultrafast X-Ray Scattering Measurements of Coherent Structural Dynamics on the Ground-State Potential Energy Surface of a Diplatinum Molecule
- 2019
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In: Physical Review Letters. - 0031-9007. ; 122:6
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Journal article (peer-reviewed)abstract
- We report x-ray free electron laser experiments addressing ground-state structural dynamics of the diplatinum anion Pt2POP4 following photoexcitation. The structural dynamics are tracked with <100 fs time resolution by x-ray scattering, utilizing the anisotropic component to suppress contributions from the bulk solvent. The x-ray data exhibit a strong oscillatory component with period 0.28 ps and decay time 2.2 ps, and structural analysis of the difference signal directly shows this as arising from ground-state dynamics along the PtPt coordinate. These results are compared with multiscale Born-Oppenheimer molecular dynamics simulations and demonstrate how off-resonance excitation can be used to prepare a vibrationally cold excited-state population complemented by a structure-dependent depletion of the ground-state population which subsequently evolves in time, allowing direct tracking of ground-state structural dynamics.
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5. |
- Sondergaard, Mads T., et al.
(author)
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Calmodulin mutations causing catecholaminergic polymorphic ventricular tachycardia confer opposing functional and biophysical molecular changes
- 2015
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In: The FEBS Journal. - : Wiley. - 1742-464X. ; 282:4, s. 803-816
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Journal article (peer-reviewed)abstract
- Calmodulin (CaM) is the central mediator of intracellular Ca2+ signalling in cardiomyocytes, where it conveys the intricate Ca2+ transients to the proteins controlling cardiac contraction. We recently linked two separate mutations in CaM (N53I and N97S) to dominantly inherited catecholaminergic polymorphic ventricular tachycardia (CPVT), an arrhythmic disorder in which exercise or acute emotion can lead to syncope and sudden cardiac death. Given the ubiquitous presence of CaM in all eukaryote cells, it is particular intriguing that carriers of either mutation show no additional symptoms. Here, we investigated the effects of the CaM CPVT mutations in a zebrafish animal model. Three-day-old embryos injected with either CaM mRNA showed no detectable pathologies or developmental abnormalities. However, embryos injected with CPVT CaM mRNA displayed increased heart rate compared to wild-type CaM mRNA under -adrenergic stimulation, demonstrating a conserved dominant cardiac specific effect between zebrafish and human carriers of these mutations. Motivated by the highly similar physiological phenotypes, we compared the effects of the N53I and N97S mutations on the biophysical and functional properties of CaM. Surprisingly, the mutations have opposing effects on CaM C-lobe Ca2+ binding affinity and kinetics, and changes to the CaM N-lobe Ca2+ binding are minor and specific to the N53I mutation. Furthermore, both mutations induce differential perturbations to structure and stability towards unfolding. Our results suggest different molecular disease mechanisms for the CPVT (N53I and N97S mutations) and strongly support that cardiac contraction is the physiological process most sensitive to CaM integrity.
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