Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP.

Photosynthetic electron transfers occur through multiple components ranging from small soluble proteins to large integral membrane protein complexes. Co-crystallization of a bacterial photosynthetic electron transfer complex that employs weak hydrophobic interactions was achieved by using high-molar-ratio mixtures of a soluble donor protein (high-potential iron-sulfur protein, HiPIP) with a membrane-embedded acceptor protein (reaction center, RC) at acidic pH. The structure of the co-complex offers a snapshot of a transient bioenergetic event and revealed a molecular basis for thermodynamically unfavorable interprotein electron tunneling.

Cooperative Photoprotection by Multicompositional Carotenoids in the LH1 Antenna from a Mutant Strain of Rhodobacter sphaeroides.

To explore the photoprotection role of multicompositional carotenoid (Car) in photosynthetic purple bacteria, we investigated, by means of triplet excitation profile (TEP) combined with steady-state optical spectroscopies, the core light-harvesting complex-reaction center of a mutant strain of Rhodobacter sphaeroides (m-LH1-RC) at room temperature. TEP spectra revealed that spheroidene and derivative (Spe) preferentially protect bacteriochlorophylls (BChls) of relatively lower site energy by quenching the triplet excitation (BChl*); however, spirilloxanthin (Spx) does so irrespective to the site energy of BChls. Triplet excitation results showed the triplet excitation energy-transfer (EET) reaction in a timescale of ∼0.

New Insights into the Mechanism of Uphill Excitation Energy Transfer from Core Antenna to Reaction Center in Purple Photosynthetic Bacteria.

The uphill excitation energy transfer (EET) from the core antenna (LH1) to the reaction center (RC) of purple photosynthetic bacteria was investigated at room temperature by comparing the native LH1-RC from Thermochromatium ( Tch.) tepidum with the hybrid LH1-RC from a mutant strain of Rhodobacter ( Rba.) sphaeroides.

Probing structure-function relationships in early events in photosynthesis using a chimeric photocomplex.

The native core light-harvesting complex (LH1) from the thermophilic purple phototrophic bacterium requires Ca for its thermal stability and characteristic absorption maximum at 915 nm. To explore the role of specific amino acid residues of the LH1 polypeptides in Ca-binding behavior, we constructed a genetic system for heterologously expressing the LH1 complex in an engineered mutant strain. This system contained a chimeric gene cluster ( from and from ) and was subsequently deployed for introducing site-directed mutations on the LH1 polypeptides.

C-terminal cleavage of the LH1 α-polypeptide in the Sr-cultured Thermochromatium tepidum.

The light-harvesting 1 reaction center (LH1-RC) complex in the thermophilic purple sulfur bacterium Thermochromatium (Tch.) tepidum binds Ca ions as cofactors, and Ca-binding is largely involved in its characteristic Q absorption at 915 nm and enhanced thermostability. Ca can be biosynthetically replaced by Sr in growing cultures of Tch.

Imaging individual neurons in the retinal ganglion cell layer of the living eye.

Although imaging of the living retina with adaptive optics scanning light ophthalmoscopy (AOSLO) provides microscopic access to individual cells, such as photoreceptors, retinal pigment epithelial cells, and blood cells in the retinal vasculature, other important cell classes, such as retinal ganglion cells, have proven much more challenging to image. The near transparency of inner retinal cells is advantageous for vision, as light must pass through them to reach the photoreceptors, but it has prevented them from being directly imaged in vivo. Here we show that the individual somas of neurons within the retinal ganglion cell (RGC) layer can be imaged with a modification of confocal AOSLO, in both monkeys and humans.

Structural Basis for the Unusual Q Red-Shift and Enhanced Thermostability of the LH1 Complex from Thermochromatium tepidum.

While the majority of the core light-harvesting complexes (LH1) in purple photosynthetic bacteria exhibit a Q absorption band in the range of 870-890 nm, LH1 from the thermophilic bacterium Thermochromatium tepidum displays the Q band at 915 nm with an enhanced thermostability. These properties are regulated by Ca ions. Substitution of the Ca with other divalent metal ions results in a complex with the Q band blue-shifted to 880-890 nm and a reduced thermostability.

Characterization of the quinones in purple sulfur bacterium Thermochromatium tepidum.

Quinone distributions in the thermophilic purple sulfur bacterium Thermochromatium tepidum have been investigated at different levels of the photosynthetic apparatus. Here we show that, on average, the intracytoplasmic membrane contains 18 ubiquinones (UQ) and 4 menaquinones (MQ) per reaction center (RC). About one-third of the quinones are retained in the light-harvesting-reaction center core complex (LH1-RC) with a similar ratio of UQ to MQ.

Structure of the LH1-RC complex from Thermochromatium tepidum at 3.0 Å.

The light-harvesting core antenna (LH1) and the reaction centre (RC) of purple photosynthetic bacteria form a supramolecular complex (LH1-RC) to use sunlight energy in a highly efficient manner. Here we report the first near-atomic structure, to our knowledge, of a LH1-RC complex, namely that of a Ca(2+)-bound complex from Thermochromatium tepidum, which reveals detailed information on the arrangement and interactions of the protein subunits and the cofactors. The RC is surrounded by 16 heterodimers of the LH1 αβ-subunit that form a completely closed structure.

Drying process in a solvent-based paint analyzed by phase-shifting digital holography and an estimation of time for tack free.

A technique to study the drying of paints, based on phase-shifting digital holography, is presented. The technique is applied to the drying process of solvent-based paint on a three-dimensional surface at different substrate temperatures. For processing the data, a cross-correlation function and phase change derived from reconstructed complex amplitudes are calculated to visualize and to evaluate the local variations in the dryness of paint.