Correction: Perylene-derivative singlet exciton fission in water solution.

[This corrects the article DOI: 10.1039/D4SC04732J.].

Perylene-derivative singlet exciton fission in water solution.

We provide direct evidence of singlet fission occurring with water-soluble compounds. We show that perylene-3,4,9,10-tetracarboxylate forms dynamic dimers in aqueous solution, with lifetimes long enough to allow intermolecular processes such as singlet fission. As these are transient dimers rather than stable aggregates, they retain a significant degree of disorder.

Molecular events accompanying aggregation-induced energy quenching in fucoxanthin-chlorophyll proteins.

In high light, the antenna system in oxygenic photosynthetic organisms switches to a photoprotective mode, dissipating excess energy in a process called non-photochemical quenching (NPQ). Diatoms exhibit very efficient NPQ, accompanied by a xanthophyll cycle in which diadinoxanthin is de-epoxidized into diatoxanthin. Diatoms accumulate pigments from this cycle in high light, and exhibit faster and more pronounced NPQ.

Second Coordination Sphere Effect Shifts CO to CO Reduction by Iron Porphyrin from Fe to Fe.

Iron porphyrins are among the most studied molecular catalysts for carbon dioxide (CO ) reduction and their reactivity is constantly being enhanced through the implementation of chemical functionalities in the second coordination sphere inspired by the active sites of enzymes. In this study, we were intrigued to observe that a multipoint hydrogen bonding scheme provided by embarked urea groups could also shift the redox activation step of CO from the well-admitted Fe(0) to the Fe(I) state. Using EPR, resonance Raman, IR and UV-Visible spectroscopies, we underpinned a two-electron activation step of CO starting from the Fe(I) oxidation state to form, after protonation, an Fe(III)-COOH species.

Resonance Raman: A powerful tool to interrogate carotenoids in biological matrices.

Resonance Raman spectroscopy is one of the most powerful techniques in analytical science due to its molecular selectivity, high sensitivity, and the fact that, in contrast to IR absorption spectroscopy, the presence of water does not hamper or mask the results. Originating in physics and chemistry, the use of Raman spectroscopy has spread and now includes a variety of applications in different disciplines, including biology. In this chapter, we introduce the basic principles of Raman and resonance Raman scattering, and show resonance Raman can be applied to study carotenoid molecules, in complex biological or chemical matrices.

Electronic and Vibrational Properties of Allene Carotenoids.

Carotenoids are conjugated linear molecules built from the repetition of terpene units, which display a large structural diversity in nature. They may, in particular, contain several types of side or end groups, which tune their functional properties, such as absorption position and photochemistry. We report here a detailed experimental study of the absorption and vibrational properties of allene-containing carotenoids, together with an extensive modeling of these experimental data.

Singlet fission in naturally-organized carotenoid molecules.

We have investigated the photophysics of aggregated lutein/violaxanthin in daffodil chromoplasts. We reveal the presence of three carotenoid aggregate species, the main one composed of a mixture of lutein/violaxanthin absorbing at 481 nm, and two secondary populations of aggregated carotenoids absorbing circa 500 and 402 nm. The major population exhibits an efficient singlet fission process, generating μs-lived triplet states on an ultrafast timescale.

Pigment structure in the light-harvesting protein of the siphonous green alga Codium fragile.

The siphonaxanthin-siphonein-chlorophyll-a/b-binding protein (SCP), a trimeric light-harvesting complex isolated from photosystem II of the siphonous green alga Codium fragile, binds the carotenoid siphonaxanthin (Sx) and/or its ester siphonein in place of lutein, in addition to chlorophylls a/b and neoxanthin. SCP exhibits a higher content of chlorophyll b (Chl-b) than its counterpart in green plants, light-harvesting complex II (LHCII), increasing the relative absorption of blue-green light for photosynthesis. Using low temperature absorption and resonance Raman spectroscopies, we reveal the presence of two non-equivalent Sx molecules in SCP, and assign their absorption peaks at 501 and 535 nm.

A new, unquenched intermediate of LHCII.

When plants are exposed to high-light conditions, the potentially harmful excess energy is dissipated as heat, a process called non-photochemical quenching. Efficient energy dissipation can also be induced in the major light-harvesting complex of photosystem II (LHCII) in vitro, by altering the structure and interactions of several bound cofactors. In both cases, the extent of quenching has been correlated with conformational changes (twisting) affecting two bound carotenoids, neoxanthin, and one of the two luteins (in site L1).

An engineered extraplastidial pathway for carotenoid biofortification of leaves.

Carotenoids are lipophilic plastidial isoprenoids highly valued as nutrients and natural pigments. A correct balance of chlorophylls and carotenoids is required for photosynthesis and therefore highly regulated, making carotenoid enrichment of green tissues challenging. Here we show that leaf carotenoid levels can be boosted through engineering their biosynthesis outside the chloroplast.

Discovery of a heme-binding domain in a neuronal voltage-gated potassium channel.

The EAG () family of voltage-gated K channels are important regulators of neuronal and cardiac action potential firing (excitability) and have major roles in human diseases such as epilepsy, schizophrenia, cancer, and sudden cardiac death. A defining feature of EAG (Kv10-12) channels is a highly conserved domain on the N terminus, known as the eag domain, consisting of a Per-ARNT-Sim (PAS) domain capped by a short sequence containing an amphipathic helix (Cap domain). The PAS and Cap domains are both vital for the normal function of EAG channels.

Modeling Dynamic Conformations of Organic Molecules: Alkyne Carotenoids in Solution.

Calculating the spectroscopic properties of complex conjugated organic molecules in their relaxed state is far from simple. An additional complexity arises for flexible molecules in solution, where the rotational energy barriers are low enough so that nonminimum conformations may become dynamically populated. These metastable conformations quickly relax during the minimization procedures preliminary to density functional theory calculations, and so accounting for their contribution to the experimentally observed properties is problematic.

Tuning antenna function through hydrogen bonds to chlorophyll a.

We describe a molecular mechanism tuning the functional properties of chlorophyll a (Chl-a) molecules in photosynthetic antenna proteins. Light-harvesting complexes from photosystem II in higher plants - specifically LHCII purified with α- or β-dodecyl-maltoside, along with CP29 - were probed by low-temperature absorption and resonance Raman spectroscopies. We show that hydrogen bonding to the conjugated keto carbonyl group of protein-bound Chl-a tunes the energy of its Soret and Q absorption transitions, inducing red-shifts that are proportional to the strength of the hydrogen bond involved.

Pigment configuration in the light-harvesting protein of the xanthophyte alga Xanthonema debile.

The soil chromophyte alga Xanthonema (X.) debile contains only non-carbonyl carotenoids and Chl-a. X.

Electronic Structure and Triplet-Triplet Energy Transfer in Artificial Photosynthetic Antennas.

Three Pd(II) phthalocyanine-carotenoid dyads featuring chromophores linked by amide bonds were prepared in order to investigate the rate of triplet-triplet (T-T) energy transfer from the tetrapyrrole to the covalently attached carotenoid as a function of the number of conjugated double bonds in the carotenoid. Carotenoids having 9, 10 and 11 conjugated double bonds were studied. Transient absorption measurements show that intersystem crossing in the Pd(II) phthalocyanine takes place in 10 ps in each case and that T-T energy transfer occurs in 126, 81 and 132 ps in the dyads bearing 9, 10 and 11 double bond carotenoids, respectively.

Binding of pigments to the cyanobacterial high-light-inducible protein HliC.

Cyanobacteria possess a family of one-helix high-light-inducible proteins (HLIPs) that are widely viewed as ancestors of the light-harvesting antenna of plants and algae. HLIPs are essential for viability under various stress conditions, although their exact role is not fully understood. The unicellular cyanobacterium Synechocystis sp.

Electronic and vibrational properties of carotenoids: from to .

Carotenoids are among the most important organic compounds present in Nature and play several essential roles in biology. Their configuration is responsible for their specific photophysical properties, which can be tailored by changes in their molecular structure and in the surrounding environment. In this review, we give a general description of the main electronic and vibrational properties of carotenoids.

Pigment structure in the violaxanthin-chlorophyll-a-binding protein VCP.

Resonance Raman spectroscopy was used to evaluate pigment-binding site properties in the violaxanthin-chlorophyll-a-binding protein (VCP) from Nannochloropsis oceanica. The pigments bound to this antenna protein are chlorophyll-a, violaxanthin, and vaucheriaxanthin. The molecular structures of bound Chl-a molecules are discussed with respect to those of the plant antenna proteins LHCII and CP29, the crystal structures of which are known.

Metal Cations Induced αβ-BChl a Heterogeneity in LH1 as Revealed by Temperature-Dependent Fluorescence Splitting.

Two spectral forms of the core light-harvesting complex (LH1) of the purple bacterium Thermochromatium (Tch.) tepidum, the native Ca -binding and the Ba -substituted one, exhibit different fluorescence (FL) emission spectra at low temperature (T). While Ca-LH1 exhibits one emission band, an unusual splitting of the fluorescence is observed for Ba-LH1.

Design of porphyrin-based ligands for the assembly of [d-block metal : calcium] bimetallic centers.

The association of different metals in stable, well-defined molecular assemblies remains a great challenge of supramolecular chemistry. In such constructs, the emergence of synergism, or cooperative effects between the different metal centers is particularly intriguing. These effects can lead to uncommon reactivity or remarkable physico-chemical properties that are not otherwise achievable.

Twisting a β-Carotene, an Adaptive Trick from Nature for Dissipating Energy during Photoprotection.

Cyanobacteria possess a family of one-helix high light-inducible proteins (Hlips) that are homologous to light-harvesting antenna of plants and algae. An Hlip protein, high light-inducible protein D (HliD) purified as a small complex with the Ycf39 protein is evaluated using resonance Raman spectroscopy. We show that the HliD binds two different β-carotenes, each present in two non-equivalent binding pockets with different conformations, having their (0,0) absorption maxima at 489 and 522 nm, respectively.

Pigment structure in the FCP-like light-harvesting complex from Chromera velia.

Resonance Raman spectroscopy was used to evaluate pigment structure in the FCP-like light-harvesting complex of Chromera velia (Chromera light-harvesting complex or CLH). This antenna protein contains chlorophyll a, violaxanthin and a new isofucoxanthin-like carotenoid (called Ifx-l). We show that Ifx-l is present in two non-equivalent binding pockets with different conformations, having their (0,0) absorption maxima at 515 and 548nm respectively.

Probing the pigment binding sites in LHCII with resonance Raman spectroscopy: The effect of mutations at S123.

Resonance Raman spectroscopy was used to evaluate the structure of light-harvesting chlorophyll (Chl) a/b complexes of photosystem II (LHCII), reconstituted from wild-type (WT) and mutant apoproteins over-expressed in Escherichia coli. The point mutations involved residue S123, exchanged for either P (S123P) or G (S123G). In all reconstituted proteins, lutein 2 displayed a distorted conformation, as it does in purified LHCII trimers.

Controlling surface defects and photophysics in TiO2 nanoparticles.

Titanium dioxide (TiO2) is widely used for photocatalysis and solar cell applications, and the electronic structure of bulk TiO2 is well understood. However, the surface structure of nanoparticulate TiO2, which has a key role in properties such as solubility and catalytic activity, still remains controversial. Detailed understanding of surface defect structures may help explain reactivity and overall materials performance in a wide range of applications.