Photoinduced reactivity of titanium dioxide

The increasing energy demand in the near future will force us to seek environmentally clean alternative energy resources. The emergence of nanomaterials as the new building blocks to construct light energy harvesting assemblies has opened up new ways to utilize renewable energy sources. This article discusses three major ways to utilize nanostructures for the design of solar energy conversion devices:  (i) Mimicking photosynthesis with donor−acceptor molecular assemblies or clusters, (ii) semiconductor assisted photocatalysis to produce fuels such as hydrogen, and (iii) nanostructure semiconductor based solar cells. This account further highlights some of the recent developments in these areas and points out the factors that limit the efficiency optimization. Strategies to employ ordered assemblies of semiconductor and metal nanoparticles, inorganic-organic hybrid assemblies, and carbon nanostructures in the energy conversion schemes are also discussed. Directing the future research efforts toward utiliza...

Meeting the Clean Energy Demand: Nanostructure Architectures for Solar Energy Conversion

The semiconductor and the surface-adsorbed antenna molecule (dyes or other color species) can constitute efficient photochemical systems for environmental remediation. The major advantage of these systems is that they are able to achieve the degradation of organic pollutants by using visible light from the sun as energy and O2 in the air as the oxidant under ambient conditions. In this tutorial review, the unique mechanistic characteristics, the constitution of photodegradation systems and their performance are described. The involved radical reactions during the degradation are also discussed.

Semiconductor-mediated photodegradation of pollutants under visible-light irradiation

III. Foldamer Research 3910 A. Overview 3910 B. Motivation 3910 C. Methods 3910 D. General Scope 3912 IV. Peptidomimetic Foldamers 3912 A. The R-Peptide Family 3913 1. Peptoids 3913 2. N,N-Linked Oligoureas 3914 3. Oligopyrrolinones 3915 4. Oxazolidin-2-ones 3916 5. Azatides and Azapeptides 3916 B. The â-Peptide Family 3917 1. â-Peptide Foldamers 3917 2. R-Aminoxy Acids 3937 3. Sulfur-Containing â-Peptide Analogues 3937 4. Hydrazino Peptides 3938 C. The γ-Peptide Family 3938 1. γ-Peptide Foldamers 3938 2. Other Members of the γ-Peptide Family 3941 D. The δ-Peptide Family 3941 1. Alkene-Based δ-Amino Acids 3941 2. Carbopeptoids 3941 V. Single-Stranded Abiotic Foldamers 3944 A. Overview 3944 B. Backbones Utilizing Bipyridine Segments 3944 1. Pyridine−Pyrimidines 3944 2. Pyridine−Pyrimidines with Hydrazal Linkers 3945

A field guide to foldamers.

Oxygenic photosynthesis in plants, algae and cyanobacteria is initiated at photosystem II, a homodimeric multisubunit protein-cofactor complex embedded in the thylakoid membrane. Photosystem II captures sunlight and powers the unique photo-induced oxidation of water to atmospheric oxygen. Crystallographic investigations of cyanobacterial photosystem II have provided several medium-resolution structures (3.8 to 3.2 A) that explain the general arrangement of the protein matrix and cofactors, but do not give a full picture of the complex. Here we describe the most complete cyanobacterial photosystem II structure obtained so far, showing locations of and interactions between 20 protein subunits and 77 cofactors per monomer. Assignment of 11 beta-carotenes yields insights into electron and energy transfer and photo-protection mechanisms in the reaction centre and antenna subunits. The high number of 14 integrally bound lipids reflects the structural and functional importance of these molecules for flexibility within and assembly of photosystem II. A lipophilic pathway is proposed for the diffusion of secondary plastoquinone that transfers redox equivalents from photosystem II to the photosynthetic chain. The structure provides information about the Mn4Ca cluster, where oxidation of water takes place. Our study uncovers near-atomic details necessary to understand the processes that convert light to chemical energy.

Towards complete cofactor arrangement in the 3.0 Å resolution structure of photosystem II

Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment.

Biochemical data have shown that specific, tightly bound phospholipids are essential for activity of the cytochrome bc1 complex (QCR), an integral membrane protein of the respiratory chain. However, the structure and function of such phospholipids are not yet known. Here we describe five phospholipid molecules and one detergent molecule in the X-ray structure of yeast QCR at 2.3 Å resolution. Their individual binding sites suggest specific roles in facilitating structural and functional integrity of the enzyme. Interestingly, a phosphatidylinositol molecule is bound in an unusual interhelical position near the flexible linker region of the Rieske iron–sulfur protein. Two possible proton uptake pathways at the ubiquinone reduction site have been identified: the E/R and the CL/K pathway. Remarkably, cardiolipin is positioned at the entrance to the latter. We propose that cardiolipin ensures structural integrity of the proton-conducting protein environment and takes part directly in proton uptake. Site-directed mutagenesis of ligating residues confirmed the importance of the phosphatidylinositol- and cardiolipin-binding sites.

/pdf/specific-roles-of-protein-phospholipid-interactions-in-the-3bwtdohggu.pdf

Specific roles of protein-phospholipid interactions in the yeast cytochrome bc1 complex structure.

Small diffusible redox proteins facilitate electron transfer in respiration and photosynthesis by alternately binding to integral membrane proteins. Specific and transient complexes need to be formed between the redox partners to ensure fast turnover. In respiration, the mobile electron carrier cytochrome c shuttles electrons from the cytochrome bc1 complex to cytochrome c oxidase. Despite extensive studies of this fundamental step of energy metabolism, the structures of the respective electron transfer complexes were not known. Here we present the crystal structure of the complex between cytochrome c and the cytochrome bc1 complex from Saccharomyces cerevisiae. The complex was crystallized with the help of an antibody fragment, and its structure was determined at 2.97-Å resolution. Cytochrome c is bound to subunit cytochrome c1 of the enzyme. The tight and specific interactions critical for electron transfer are mediated mainly by nonpolar forces. The close spatial arrangement of the c-type hemes unexpectedly suggests a direct and rapid heme-to-heme electron transfer at a calculated rate of up to 8.3 × 106 s−1. Remarkably, cytochrome c binds to only one recognition site of the homodimeric multisubunit complex. Interestingly, the occupancy of quinone in the Qi site is higher in the monomer with bound cytochrome c, suggesting a coordinated binding and reduction of both electron-accepting substrates. Obviously, cytochrome c reduction by the cytochrome bc1 complex can be regulated in response to respiratory conditions.

https://www.pnas.org/content/pnas/99/5/2800.full.pdf

Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c.

Amorphous, microporous TiO2 hybrid semiconductors modified with transition metals induce generation of a photocurrent and photocatalytic degradation of the water contaminant 4-chlorophenol through photoinduced charge separation (the postulated mechanism is shown in the picture, Ar=4-ClC6 H4 ). In contrast to the previously known crystalline titania photocatalysts, which are active only when excited with UV light, the amorphous semiconductors modified with platinum, rhodium, and gold chloride enable both processes also with visible light.

Modified, Amorphous Titania—A Hybrid Semiconductor for Detoxification and Current Generation by Visible Light

Amorphous microporous metal oxides of titanium (AMM-Ti) modified with chlorides of Pt IV ,I r IV ,R h III ,A u III ,P d II ,C o II , and Ni II have been prepared by the sol - gel method and characterized by various surface analytical methods. These hybrid AMM-Ti powders are catalysts for the photodegradation of 4-chlorophenol (4-CP) in aqueous solution when illuminated with visible (l 400 or 455 nm) or UV (l 335 nm) light. The initial rate depends on the dopant level and is highest at 3.0 % Pt in the case of Pt IV /AMM-Ti. When employed in a photoelectrochemical cell, the activity spectrum of the photocurrent extends downward to about 600 nm, as does the photodegradation of 4-CP. It is suggested that the metal salt acts as a redox-active chromophore, transmitting the photogenerated charges to the amorphous matrix.

Christian Lange

Papers

Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment.

Specific roles of protein-phospholipid interactions in the yeast cytochrome bc1 complex structure.

Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c.

Modified, Amorphous Titania—A Hybrid Semiconductor for Detoxification and Current Generation by Visible Light

Visible-light detoxification and charge generation by transition metal chloride modified titania.