2-β-d-Glucopyranosyloxy-2-methylpropanol in Acacia sieberana var. woodii

A new diol glucoside, 2-β-d-glucopyranosyloxy-2-methylpropanol, the first reported naturally occurring monoglucoside of an aliphatic dihydric alcohol, was isolated from pods of Acacia sieberana var. woodii. Structure elucidation was based on ¹ H and ¹³C NMR spectroscopy, and enzymatic analyses. The compound was hydrolysed very slowly by almond β-glucosidase, but cleaved by a β-glucuronidase enzyme complex from Helix pomatia.     

Contribution to the structural characterization of eucaryotic PSI reaction centre—I. Critical analysis of the polypeptidic composition of different P700 enriched fractions

In thylakoid membranes, several peptides of high MW are present which may interfere with the study of CP1's components. Modifying Cleveland's technique [7] for limited proteolysis, we have characterized the polypeptides found in the 60 kD region. Some may result from incomplete washing of the CF1 while others come from the CP1; indeed, this chlorophyll protein complex, which has a higher MW (above 100 kD), very often undergoes a dissociation into smaller components of about 60 KD MW.Analysis of the protein content of different preparations commonly used to obtain PSI reaction centre enriched fractions has been performed. The and subunits of CF1 are among the main contaminants of most of these preparations. A further purification step is described which can be applied to all these preparations, but numerous peptides are still present in the active fractions. It is most unlikely that all these polypeptides are required for the primary photochemical event, and this emphasizes the necessity to find a new simple method to purify PSI reaction centres.     

A spectroscopic study of metal ion and ligand binding to β-lactamase II

β-Lactamase II has two metal-binding sites. The electronic spectra of Cd(II)- and Co(II)-substituted β-lactamase II have been investigated. It is suggested that a thiol ligand is involved in metal binding at the first site. The stoichiometric dissociation constants for Co(II) binding to β-lactamase II were estimated to be 0.13 and 2.66 mM (pH 6.0, 4°C, 1 M NaCl) by equilibrium dialysis. Competition between Zn(II) and Co(II) for the first metal binding site suggests a value of 0.7 μM (pH 6.0, 30°C, 1 M NaCl) for the dissociation constant o Zn(II).The electronic spectra of the Co(II) enzyme lead to the suggestion that the coordination geometries around the metal ions in the first and second sites are related to those of a distorted tetrahedron and octahedron, respectively.     

Theoretical investigations on circular and chain-like hydrogen bonded structures found in two crystal forms of α-cyclodextrin hexahydrate: Models for hydration and water clusters

Hydration of macromolecules and the structure of water of crystallization are not understood in detail because in these complex systems. H-atoms cannot be located and the hydrogen bonding schemes are not known. X-ray and neutron diffraction studies on a hydrated oligosaccharide, α-cyclodextrin 6H₂O, ((C₆H₁₀O₅)₆·6H₂O), crystals forms A and B, gave insight into the chain-like and circular arrangement of hydrogen bonds. In the circles, homodromic (unidirectional) and antidromic (counter-running) orientation of five to six hydrogen bounds is observed. PCILO calculations showed that homodromic circles and chains are approx. 8% per hydrogen bond more stable than antidromic circles, that the changes in electronic charges on H and O atoms are greater in homo than in antidromic systems and that the dipole moments are only approx. 3 D in the homodromic circles but 6–8 D in chain-like and antidromic arrangement. These results have been interpreted in terms of cooperative effect. Circular systems are considered as structural elements in hydration shells of macromolecules and in the assembly of ‘flickering’ water clusters.     

The mitochondrial complex in cryptophyceae

The unitary nature of the mitochondrion and the characteristic flattened finger-like morphology of the cristae were demonstrated in the Cryptophyceae. Hemiselmis rufescens contained an unbranched vermi-form mitochondrion in contrast to the variously branched complex, comprising an interconnected peripheral and central reticulum, in Chroomonas sp. and strains of Cryptomonas. The systematic value of the shape and distribution of the mitochondria in the examined genera was suggested.     

Light-harvesting pigment-protein complex deficiency in Hosta (Liliaceae)

A yellow-leaved plastome mutant of Hosta (Hosta sieboldii Ingram complex, Liliaceae) known as Wogan Gold lacks normal granal stacks, but has numerous stroma lamellae extending throughout the chloroplast. The chlorophyll a/b ratio is 0.76 in the mutant and 2.9 in wild type. The mutant contains a qualitatively normal pattern of other photosynthetic co-pigments. SDS-polyacrylamide gel electrophoresis showed a deficiency in the photosystem (PS) II light-harvesting complex. Since PS II is localized mainly in the granal region, the absence of the light-harvesting complex may explain the loss of granal stacking in this mutant.Abbreviation PS photosystem     

Light-dependent conformational change at rhodopsin's cytoplasmic surface detected by increased susceptibility to proteolysis

Rhodopsin in bovine photoreceptor disk membranes was subjected to limited proteolysis by thermolysin, removing twelve amino acids from rhodopsin's carboxyl terminus. (1) The rate of proteolysis is significantly faster with rhodopsin following exposure to light than with unbleached rhodopsin, provided that the incubation conditions (pH, temperature) favor the formation of metarhodopsin II. (2) If the disk membranes are illuminated under conditions in which metarhodopsin I is the predominant photoproduct (pH 8.5, 0°C), no increase in the rate of proteolysis is observed compared to unilluminated membranes. (3) The light-induced increase in the rate of proteolysis is transient: it slowly decays in the dark to the original rate found for unbleached rhodopsin. The enhanced susceptibility to proteolysis appears to measure a conformational change at rhodopsin's cytoplasmic surface which is first exhibited at the metarhodopsin II stage. This and possibly other light-dependent changes may allow rhodopsin to mediate its signal as a light-receptor protein by binding to and activating certain rod cell enzymes.     

Restoration of membrane potential in mitochondria deenergized with carbonyl cyanide p-trifluoromethoxyphenylhydrazone (FCCP)

The membrane potential (Δψ) of rat liver mitochondria dropped upon addition of carbonyl cyanide p-trifluoromethoxyphenylhydrazone (FCCP) but was gradually and fully restored to the original value by the subsequent addition of dithioerythritol. Concomitantly, Ca²⁺ released from mitochondria was reaccumulated and the oxidative phosphorylation process completely recoupled. Neither of these effects has been observed with dinitro-o-cresol or 2,4-dinitrophenol, uncouplers which, unlike FCCP, do not react with thiols. Δψ abolished by FCCP was also restored, though incompletely, by albumin; a prompt and complete restoration was however achieved upon subsequent addition of dithioerythritol. Dithioerythritol also completely and rapidly restored the Δψ decreased by addition of diazene dicarboxylic acid bisdimethylamide (diamide).