Color constancy investigated via partial hue-matching.

Each hue is believed to be made up of the four component hues (yellow, blue, red, and green). A hue consisting of just one component hue is called unitary (or unique). A new technique--partial hue-matching--has been used to reveal the component and unitary hues for a sample of 32 Munsell papers, which were illuminated by neutral, yellow, blue, green, and red lights and assessed by four normal trichromatic observers.

INFLUENCE OF DIFFERENT LIGHT INTENSITIES AND DIFFERENT IRON NUTRITION ON THE PHOTOSYNTHETIC APPARATUS IN THE DIATOM CYCLOTELLA MENEGHINIANA (BACILLARIOPHYCEAE)(1).

The diatom Cyclotella meneghiniana Kütz. (SAG 1020-a) was cultured under high-light (HL) and low-light (LL) conditions with either high (12 μM) or low (1 μM) iron in the media. Changes in cell morphology, especially cell volume and chloroplast size, were observed in cells grown under low iron.

Pigment organization in fucoxanthin chlorophyll a/c(2) proteins (FCP) based on resonance Raman spectroscopy and sequence analysis.

Chlorophylls (Chls)-a and -c(2) are identified and characterized in fucoxanthin chlorophyll-a/c(2) protein (FCP) complexes in the trimeric (FCPa(trim)) and oligomeric (FCPb(olig)) forms of FCP from the diatom Cyclotella meneghiniana using resonance Raman (RR) spectroscopy. Importantly, two different Chl-c(2)s are identified in both FCPa(trim) and FCPb(olig) from their signature ring-breathing modes at approximately 1360 cm(-1). In addition, the C13(1)-keto carbonyl peaks indicate the presence of more than four Chl-a's in both FCP complexes and are broadly classified into three groups with strong, medium and weak external hydrogen bonds.

Oligomerization and pigmentation dependent excitation energy transfer in fucoxanthin-chlorophyll proteins.

The ultrafast carotenoid to chlorophyll a energy transfer dynamics of the isolated fucoxanthin-chlorophyll proteins FCPa and FCPb from the diatom Cyclotella meneghiniana was investigated in a comprehensive study using transient absorption in the visible and near infrared spectral region as well as static fluorescence spectroscopy. The altered oligomerization state of both antenna systems results in a more efficient energy transfer for FCPa, which is also reflected in the different chlorophyll a fluorescence quantum yields. We therefore assume an increased quenching in the higher oligomers of FCPb.

Carotenoid structures and environments in trimeric and oligomeric fucoxanthin chlorophyll a/c2 proteins from resonance Raman spectroscopy.

Resonance Raman (RR) spectroscopy is used to characterize the structures and environments of the carotenoid fucoxanthin (Fx), the primary light harvester in the membrane-intrinsic fucoxanthin chlorophyll a/c2 proteins(FCP) from the diatom Cyclotella meneghiniana, thereby building on the findings from Stark spectroscopy and calculations (J. Phys. Chem.

Subunit composition and pigmentation of fucoxanthin-chlorophyll proteins in diatoms: evidence for a subunit involved in diadinoxanthin and diatoxanthin binding.

Two different fucoxanthin-chlorophyll protein complexes (FCP) were purified from the centric diatom Cyclotella meneghiniana and characterized with regard to their polypeptide and pigment composition. Whereas the oligomeric FCPb complex is most probably composed of fcp5 gene products, the trimeric FCPa has subunits encoded by fcp1-3 and fcp6/7. The amount of the latter polypeptide is enhanced when FCPa is isolated from algae grown under HL conditions.