Zipping up 'the crushed fullerene' C60H30:C60 by fifteen-fold,consecutive intramolecular H2 losses

MALDI TOF-MS of tribenzo[l:1':1"]benzo[1,2-e:3,4-e':5,6-e"]triacephenanthrylene (1a, C60H30) gives C60.+ by multiple intramolecular cyclodehydrogenation reactions.     

PROTON TRANSLOCATION and CONFORMATIONAL CHANGES DURING THE BACTERIORHODOPSIN PHOTOCYCLE: TIME-RESOLVED STUDIES WITH MEMBRANE-BOUND OPTICAL PROBES and X-RAY DIFFRACTION*

Abstract– For the first time, we monitored time-resolved conformational changes inherent in bacterio-rhodopsin's reaction cycle as well as the H⁺-release events directly at the surface of bacteriorhodopsin (bR) at room temperature. Signals of optical pH-indicators in the aqueous bulk phase were compared with those of probes covalently linked to bR. The kinetics of H⁺-translocation and the correlation of the photocycle with the pumping cycle can only be determined with indicators bound to bR. The proton appears at the extracellular surface during the L₅₅₀ to M₄₁₂ transition. Upon short photo-excitation, diffraction patterns were obtained from both guanidine hydrochloride-treated wild type bR and an Asp96Asn mutant with millisecond time resolution by x-ray synchrotron radiation. The measured time course and location of the structural changes confirm and extend our previous static neutron diffraction study at -180°C. The temporal correlation of photocycle intermediates and proton translocation steps with structural changes in the protein under similar environmental conditions strongly contribute to the understanding of the pumping mechanism.     

Resolving the EPR Spectra in the Cytochrome bc 1 Complex from Saccharomyces cerevisiae

Quinone molecules are ubiquitous in living organisms. They are found either within the lipid phase of the biological membrane (quinone pool) or are bound in specific binding sites within membrane-bound protein complexes. The biological function of such bound quinones is determined by their ability to be reduced and/or oxidized in two successive one-electron steps. As a result, quinones are involved as one- or two-electron donors or acceptors in a large number of biological electron-transfer steps occurring during respiratory or photosynthetic processes. The intermediate formed by a one-electron reduction step is a semiquinone, which is paramagnetic and can be studied by electron paramagnetic resonance (EPR) spectroscopy. Detailed studies of such states can provide important structural information on these intermediates in such electron-transfer processes. In this study, we focus on the redox-active ubiquinone-6 of the yeast cytochrome bc ₁ complex (QCR, ubiquinol: cytochrome c oxidoreductase) from Saccharomyces cerevisiae at the so-called Q_i site. Although the location of the Q_i binding pocket is quite well known, details about its exact binding are less clear. Currently, three different X-ray crystallographic studies suggest three different binding geometries for Q_i. Recent studies in the bacterial system (Rhodobacter sphaeroides) have suggested a direct coordination to histidine as proposed in the chicken heart crystal structure model. Using the yeast system we apply EPR and especially relaxation filtered hyperfine (REFINE) spectroscopy to study the Q_i binding site. ¹⁴N-electron spin-echo envelope modulation spectroscopy together with an inversion-recovery filter (REFINE) is applied to resolve the question of whether ¹⁴N modulations arise from interactions to Q _i ^·? or to the Rieske iron–sulphur center. These results are discussed with regard to the location and potential function of Q_i in the enzyme.     

Chemiluminescence associated with singlet oxygen reactions with amino acids, peptides and proteins

Low level chemiluminescence (CL) is observed after protein oxidation mediated by singlet oxygen produced in Rose Bengal (RB) irradiation. This CL lasts for several minutes after the end of the photolysis. In this work, the mechanism of the process was assessed from the spectral characteristics of the CL and the effect of antioxidants (Trolox or ascorbate), Ebselen (a compound with peroxidase-like activity), azide (a singlet oxygen scavenger) and D2O, added prior to or after RB irradiation. It is concluded that most of the light emission is due to formation of excited states generated in the decomposition of peroxides and/or hydroperoxides accumulated during the photolysis. Experiments carried out in the presence of several amino acids (Cys, Met, His, Tyr and Trp) and di- and tripeptides suggest that peroxides (and/or hydroperoxides) of Trp residues are mainly responsible for the CL observed after singlet oxygen-mediated protein oxidation. The much weaker CL observed after the oxidation of proteins without Trp residues supports this conclusion. A comparison of the results obtained employing free Trp, Ala-Trp and Trp-Ala dipeptides, Ala-Trp-Ala tripeptide and Trp-containing proteins supports the conclusion that blocking the amino group of the Trp moiety strongly increases the efficiency of the chemiluminescent process, producing approximately 2.5x10(-8) photons per oxidized Trp group in Ala-Trp. A mechanism comprising two chemiluminescent oxidation pathways of Trp residues is proposed to explain the results.     

Experimental and Numerical Investigations of Al/Mg Compounds

Al/Mg compounds produced by hydrostatic extrusion exhibit unique characteristics regarding high strength and low weight, which are required by safety part applications in lightweight constructions. Between the two materials an interface in form of a brittle intermetallic phase consisting of Al₂Mg₃ and Al₁₂Mg₁₇ arises during the production process. However, a certain plastic deformability of the semi-finished product is essential for further forming processes. Even under multi-axle load during a radial upsetting process, the interface maintains a full material joint although a fragmentation and a new secondary interface between the fragments can be observed. Due to the evaluations of light microscopy images and Eulerian Hencky strain values at the interface, which are obtained with the help of the Digital Image Correlation, a relation between the strain and the boundary layer's appearance seems reasonable. (© 2014 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim)     

Regioselective Acylations of Aldono-1,4-lactones

Abstract

Partial benzoylation or pivaloylation of D-gulono-l,4-lactone (1) with 3.3-3.6 molar equivalents of the acyl chloride afforded 2,5,6-tri-O-benzoyl- (3) or 2,5,6-tri-O-pivaloyl-D-gulono-1,4-lactone (5), which were isolated crystalline from the reaction mixture in yields of 54% and 84.5 %, respectively. Similarly, partial pivaloylation of L-mannono-1,4-lactone (6) gave crystalline 2,5,6-tri-O-pivaloyl-L-mannono-l,4-lactone (9) in 50% yield. Under the same conditions of acylation, D-galactono-l,4-lactone (11) gave a mixture of products, which were separated by column chromatography. On benzoylation, 2,3,5,6-tetra-O-benzoyl- (12); 2,5,6-tri-O-benzoyl- (13); 2,3,6-tri-O-benzoyl- (14) and 2,6-di-O-benzoyl-D-galactono-l,4-lactone (15) were obtained in 47%, 16.4%, 8%, and 14% yield, respectively. Pivaloylation of 11 afforded 2,3,5,6-tetra-O-pivaloyl- (16), 2,5,6-tri-O-pivaloyl- (17), 2,3,6-tri-O-pivaloyl (18) and 2,6-di-O-pivaloyl-D-galactono-l,4-lactone (19) in 21.6%, 9.7%, 2.6%, and 30.0%, respectively.     

Synthetic Utility of α-Stannyl α,β-Unsaturated Esters as Reagents for β-Substituted Acrylate α-Anion Synthons: Tin-Lithium Exchange and Palladium-Catalized Coupling Reactions

The tin-lithium exchange and the palladium-catalized coupling reactions of the title compounds have been studied. The latter reaction was found to be more efficient for functionalizing the α-carbon of these esters.