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At least 775 records · Page 43Linked to original sources
PubMed2006

[Ni(xbsms)Ru(CO)2Cl2]: a bioinspired nickel-ruthenium functional model of [NiFe] hydrogenase.

As a model of the active site of [NiFe] hydrogenases, a dinuclear nickel-ruthenium complex [Ni(xbsms)Ru(CO)2Cl2] was synthesized and fully characterized. The three-dimensional structure reveals a nickel center in a square-planar dithioether-dithiolate environment connected to a ruthenium moiety via a Ni(mu-SR)2Ru bridge. This complex catalyzes hydrogen evolution by electroreduction of the weakly acidic Et3NH+ ions in N,N-dimethylformamide and is therefore the first functional bioinspired model of [NiFe] hydrogenases.

Chromatium↗
PubMedDate not supplied

Selective staining of proteins with hydrophobic surface sites on a native electrophoretic gel.

Chemical proteomics aims to characterize all of the proteins in the proteome with respect to their function, which is associated with their interaction with other molecules. We propose the identification of a subproteomic library of expressed proteins whose native structures are typified by the presence of hydrophobic surface sites, which are often involved in interactions with small molecules, membrane lipids, and other proteins, pertaining to their functions. We demonstrate that soluble globular proteins with hydrophobic surface sites can be detected selectively by staining on an electrophoretic gel run under nondenaturing conditions. The application of these staining techniques may help elucidate new catalytic, transport, and regulatory functionalities in complex proteomic screenings.

Bacterial Proteins↗
PubMed1999

An unusual arrangement of pur and lpx genes in the photosynthetic purple sulfur bacterium Allochromatium vinosum.

The nucleotide sequence of a 1634 bp DNA fragment from the photosynthetic purple sulfur bacterium Allochromatium vinosum contains one complete and two partial open reading frames. Sequence comparisons to genes from other organisms suggest that this A. vinosum DNA fragment contains, starting from the 5' end, the following: (1) 234 bp at the 3' end of the A. vinosum purH gene, coding for 78 amino acids at the C-terminus of the bi-functional 5'-phosphoribosyl-5-aminoimidazole-4-carboxamide formyltransferase/IMP cyclohydrolase (EC 2.1.2.3), an enzyme involved in de novo purine biosynthesis; (2) 777 bp of the A. vinosum lpxA gene, coding for all 259 amino acids of the UDP-N-acetylglucosamine-O-acyltransferase, an enzyme involved in lipid A biosynthesis; and (3) 567 bp at the 5' end of the A. vinosum purD gene, coding for 189 amino acids at the N-terminus of 5'-phosphoribosyl glycinamide synthetase (EC 6.3.4.13), a second enzyme involved in de novo purine biosynthesis. The presence of a gene coding for an enzyme involved in lipid A biosynthesis between two genes coding for enzymes of the de novo purine biosynthesis pathway represents a unique arrangement of these genes.

Acyltransferases↗
PubMed1978

Location of O-methyl sugars in antigenic (lipo-)polysaccharides of photosynthetic bacteria and cyanobacteria.

An attempt was made to localize a number of O-methyl sugars in lipopolysaccharides and antigenic polysaccharides isolated from photosynthetic bacteria and from cyano-bacteria. Methylation analysis with [2H3]methyl iodide as methylating agent was the method of choice. One has to differentiate between (lipo-)polysaccharides having only trace amounts (less than 1% of polymer dry weight) of O-methyl sugars and those having them in larger amounts (more than 4% of polymer dry weight). In the former case O-methyl sugars occupy either non-reducing or reducing terminals. When present in larger quantities they may be present as part of each repeating unit either in chain-linked or in terminal positions or in both. A possible role of O-methyl sugars in biosynthesis of O-chains, and their contribution to the lipophilic character of the cell surface are discussed.

Antigens, Bacterial↗