Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Oxyallyl exposed: an open-shell singlet with picosecond lifetimes in solution but persistent in crystals of a cyclobutanedione precursor.

ABSTRACT: Photoinduced decarbonylation of 2,4-bis(spirocyclohexyl)-1,3-cyclobutanedione 1 in the crystalline solid state resulted in formation of a deep blue transient with ?(max) = 550 nm and a half-life of 42 min at 298 K, identified as kinetically stabilized oxyallyl. Support for an open-shell singlet species was obtained by spectroscopic analysis and (4/4) CASSCF calculations with the 6-31+G(d) basis set and multireference MP2 corrections. The electronic spectrum of the singlet biradical, confirmed by femtosecond pump-probe studies in solution, was matched by coupled cluster calculations with single and double corrections.

SUBMITTER: Kuzmanich G

PROVIDER: S-EPMC3048850 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Oxyallyl exposed: an open-shell singlet with picosecond lifetimes in solution but persistent in crystals of a cyclobutanedione precursor.

Kuzmanich Gregory G Spänig Fabian F Tsai Chao-Kuan CK Um Joann M JM Hoekstra Ryan M RM Houk K N KN Guldi Dirk M DM Garcia-Garibay Miguel A MA

Journal of the American Chemical Society 20110207 8

Photoinduced decarbonylation of 2,4-bis(spirocyclohexyl)-1,3-cyclobutanedione 1 in the crystalline solid state resulted in formation of a deep blue transient with λ(max) = 550 nm and a half-life of 42 min at 298 K, identified as kinetically stabilized oxyallyl. Support for an open-shell singlet species was obtained by spectroscopic analysis and (4/4) CASSCF calculations with the 6-31+G(d) basis set and multireference MP2 corrections. The electronic spectrum of the singlet biradical, confirmed by ...[more]

PMID: 21299211

Similar Datasets

Picosecond excitation energy transfer of allophycocyanin studied in solution and in crystals.

Project description:Cyanobacteria perform photosynthesis with the use of large light-harvesting antennae called phycobilisomes (PBSs). These hemispherical PBSs contain hundreds of open-chain tetrapyrrole chromophores bound to different peptides, providing an arrangement in which excitation energy is funnelled towards the PBS core from where it can be transferred to photosystem I and/or photosystem II. In the PBS core, many allophycocyanin (APC) trimers are present, red-light-absorbing phycobiliproteins that covalently bind phycocyanobilin (PCB) chromophores. APC trimers were amongst the first light-harvesting complexes to be crystallized. APC trimers have two spectrally different PCBs per monomer, a high- and a low-energy pigment. The crystal structure of the APC trimer reveals the close distance (~21 Å) between those two chromophores (the distance within one monomer is ~51 Å) and this explains the ultrafast (~1 ps) excitation energy transfer (EET) between them. Both chromophores adopt a somewhat different structure, which is held responsible for their spectral difference. Here we used spectrally resolved picosecond fluorescence to study EET in these APC trimers both in crystallized and in solubilized form. We found that not all closely spaced pigment couples consist of a low- and a high-energy pigment. In ~10% of the cases, a couple consists of two high-energy pigments. EET to a low-energy pigment, which can spectrally be resolved, occurs on a time scale of tens of picoseconds. This transfer turns out to be three times faster in the crystal than in the solution. The spectral characteristics and the time scale of this transfer component are similar to what have been observed in the whole cells of Synechocystis sp. PCC 6803, for which it was ascribed to EET from C-phycocyanin to APC. The present results thus demonstrate that part of this transfer should probably also be ascribed to EET within APC trimers.

| S-EPMC5783994 | biostudies-literature

Singlet Exciton Lifetimes in Conjugated Polymer Films for Organic Solar Cells.

Project description:The lifetime of singlet excitons in conjugated polymer films is a key factor taken into account during organic solar cell device optimization. It determines the singlet exciton diffusion lengths in polymer films and has a direct impact on the photocurrent generation by organic solar cell devices. However, very little is known about the material properties controlling the lifetimes of singlet excitons, with most of our knowledge originating from studies of small organic molecules. Herein, we provide a brief summary of the nature of the excited states in conjugated polymer films and then present an analysis of the singlet exciton lifetimes of 16 semiconducting polymers. The exciton lifetimes of seven of the studied polymers were measured using ultrafast transient absorption spectroscopy and compared to the lifetimes of seven of the most common photoactive polymers found in the literature. A plot of the logarithm of the rate of exciton decay vs. the polymer optical bandgap reveals a medium correlation between lifetime and bandgap, thus suggesting that the Energy Gap Law may be valid for these systems. This therefore suggests that small bandgap polymers can suffer from short exciton lifetimes, which may limit their performance in organic solar cell devices. In addition, the impact of film crystallinity on the exciton lifetime was assessed for a small bandgap diketopyrrolopyrrole co-polymer. It is observed that the increase of polymer film crystallinity leads to reduction in exciton lifetime and optical bandgap again in agreement with the Energy Gap Law.

| S-EPMC6432597 | biostudies-literature

Environmentally persistent free radicals and their lifetimes in PM2.5.

Project description:For the first time, an expansive study into the concentration and extended decay behavior of environmentally persistent free radicals in PM2.5 was performed. Results from this study revealed three types of radical decay-a fast decay, slow decay, and no decay-following one of four decay patterns: a relatively fast decay exhibiting a 1/e lifetime of 1-21 days accompanied by a slow decay with a 1/e lifetime of 21-5028 days (47% of samples); a single slow decay including a 1/e lifetime of 4-2083 days (24% of samples); no decay (18% of samples); and a relatively fast decay displaying an average 1/e lifetime of 0.25-21 days followed by no decay (11% of samples). Phenol correlated well with the initial radical concentration and fast decay rate. Other correlations for common atmospheric pollutants (ozone, NOx, SO2, etc.) as well as meteorological conditions suggested photochemical processes impact the initial radical concentration and fast decay rate. The radical signal in PM2.5 was remarkably similar to semiquinones in cigarette smoke. Accordingly, radicals inhaled from PM2.5 were related to the radicals inhaled from smoking cigarettes, expressed as the number of equivalent cigarettes smoked. This calculated to 0.4-0.9 cigarettes per day for nonextreme air quality in the United States.

| S-EPMC4309365 | biostudies-literature

Picosecond fluorescence of intact and dissolved PSI-LHCI crystals.

Project description:Over the past several years, many crystal structures of photosynthetic pigment-protein complexes have been determined, and these have been used extensively to model spectroscopic results obtained on the same proteins in solution. However, the crystal structure is not necessarily identical to the structure of the protein in solution. Here, we studied picosecond fluorescence of photosystem I light-harvesting complex I (PSI-LHCI), a multisubunit pigment-protein complex that catalyzes the first steps of photosynthesis. The ultrafast fluorescence of PSI-LHCI crystals is identical to that of dissolved crystals, but differs considerably from most kinetics presented in the literature. In contrast to most studies, the data presented here can be modeled quantitatively with only two compartments: PSI core and LHCI. This yields the rate of charge separation from an equilibrated core (22.5 +/- 2.5 ps) and rates of excitation energy transfer from LHCI to core (k(LC)) and vice versa (k(CL)). The ratio between these rates, R = k(CL)/k(LC), appears to be wavelength-dependent and scales with the ratio of the absorption spectra of LHCI and core, indicating the validity of a detailed balance relation between both compartments. k(LC) depends slightly but nonsystematically on detection wavelength, averaging (9.4 +/- 4.9 ps)(-1). R ranges from 0.5 (<690 nm) to approximately 1.3 above 720 nm.

| S-EPMC2599838 | biostudies-other

Quantitative Singlet Fission in Solution-Processable Dithienohexatrienes.

Project description:Singlet fission (SF) is a promising strategy to overcome thermalization losses and enhance the efficiency of single junction photovoltaics (PVs). The development of this field has been strongly material-limited, with a paucity of materials able to undergo SF. Rarer still are examples that can produce excitons of sufficient energy to be coupled to silicon PVs (>1.1 eV). Herein, we examine a series of a short-chain polyene, dithienohexatriene (DTH), with tailored material properties and triplet (T1) energy levels greater than 1.1 eV. We find that these highly soluble materials can be easily spin-cast to create thin films of high crystallinity that exhibit ultrafast singlet fission with near perfect triplet yields of up to 192%. We believe that these materials are the first solution-processable singlet fission materials with quantitative triplet formation and energy levels appropriate for use in conjunction with silicon PVs.

| S-EPMC9801381 | biostudies-literature

Core-Shell Crystals of Porous Organic Cages.

Project description:The first examples of core-shell porous molecular crystals are described. The physical properties of the core-shell crystals, such as surface hydrophobicity, CO2 ?/CH4 selectivity, are controlled by the chemical composition of the shell. This shows that porous core-shell molecular crystals can exhibit synergistic properties that out-perform materials built from the individual, constituent molecules.

| S-EPMC6120484 | biostudies-literature

Lifetimes and spatio-temporal response of protein crystals in intense X-ray microbeams.

Project description:Serial synchrotron-based crystallography using intense microfocused X-ray beams, fast-framing detectors and protein microcrystals held at 300 K promises to expand the range of accessible structural targets and to increase overall structure-pipeline throughputs. To explore the nature and consequences of X-ray radiation damage under microbeam illumination, the time-, dose- and temperature-dependent evolution of crystal diffraction have been measured with maximum dose rates of 50 MGy s-1. At all temperatures and dose rates, the integrated diffraction intensity for a fixed crystal orientation shows non-exponential decays with dose. Non-exponential decays are a consequence of non-uniform illumination and the resulting spatial evolution of diffracted intensity within the illuminated crystal volume. To quantify radiation-damage lifetimes and the damage state of diffracting crystal regions, a revised diffraction-weighted dose (DWD) is defined and it is shown that for Gaussian beams the DWD becomes nearly independent of actual dose at large doses. An apparent delayed onset of radiation damage seen in some intensity-dose curves is in fact a consequence of damage. Intensity fluctuations at high dose rates may arise from the impulsive release of gaseous damage products. Accounting for these effects, data collection at the highest dose rates increases crystal radiation lifetimes near 300 K (but not at 100 K) by a factor of ∼1.5-2 compared with those observed at conventional dose rates. Improved quantification and modeling of the complex spatio-temporal evolution of protein microcrystal diffraction in intense microbeams will enable more efficient data collection, and will be essential in improving the accuracy of structure factors and structural models.

| S-EPMC5668864 | biostudies-literature

Conformational Substates of Myoglobin Intermediate Resolved by Picosecond X-ray Solution Scattering.

Project description:Conformational substates of proteins are generally considered to play important roles in regulating protein functions, but an understanding of how they influence the structural dynamics and functions of the proteins has been elusive. Here, we investigate the structural dynamics of sperm whale myoglobin associated with the conformational substates using picosecond X-ray solution scattering. By applying kinetic analysis considering all of the plausible candidate models, we establish a kinetic model for the entire cycle of the protein transition in a wide time range from 100 ps to 10 ms. Four structurally distinct intermediates are formed during the cycle, and most importantly, the transition from the first intermediate to the second one (B → C) occurs biphasically. We attribute the biphasic kinetics to the involvement of two conformational substates of the first intermediate, which are generated by the interplay between the distal histidine and the photodissociated CO.

| S-EPMC3985870 | biostudies-literature

cAAC-Stabilized 9,10-diboraanthracenes-Acenes with Open-Shell Singlet Biradical Ground States.

Project description:Narrow HOMO-LUMO gaps and high charge-carrier mobilities make larger acenes potentially high-efficient materials for organic electronic applications. The performance of such molecules was shown to significantly increase with increasing number of fused benzene rings. Bulk quantities, however, can only be obtained reliably for acenes up to heptacene. Theoretically, (oligo)acenes and (poly)acenes are predicted to have open-shell singlet biradical and polyradical ground states, respectively, for which experimental evidence is still scarce. We have now been able to dramatically lower the HOMO-LUMO gap of acenes without the necessity of unfavorable elongation of their conjugated ??system, by incorporating two boron atoms into the anthracene skeleton. Stabilizing the boron centers with cyclic (alkyl)(amino)carbenes gives neutral 9,10-diboraanthracenes, which are shown to feature disjointed, open-shell singlet biradical ground states.

| S-EPMC7589216 | biostudies-literature

Two-dimensional crystals of carboxysome shell proteins recapitulate the hexagonal packing of three-dimensional crystals.

Project description:Bacterial microcompartments (BMCs) are large intracellular bodies that serve as simple organelles in many bacteria. They are proteinaceous structures composed of key enzymes encapsulated by a polyhedral protein shell. In previous studies, the organization of these large shells has been inferred from the conserved packing of the component shell proteins in two-dimensional (2D) layers within the context of three-dimensional (3D) crystals. Here, we show that well-ordered, 2D crystals of carboxysome shell proteins assemble spontaneously when His-tagged proteins bind to a monolayer of nickelated lipid molecules at an air-water interface. The molecular packing within the 2D crystals recapitulates the layered hexagonal sheets observed in 3D crystals. The results reinforce current models for the molecular design of BMC shells.

| S-EPMC2821281 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data