Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase.

A crystal structure of the anaerobic Ni-Fe-S carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum has been determined to 2.8-A resolution. The CODH family, for which the R. rubrum enzyme is the prototype, catalyzes the biological oxidation of CO at an unusual Ni-Fe-S cluster called the C-cluster. The Ni-Fe-S C-cluster contains a mononuclear site and a four-metal cubane. Surprisingly, anomalous dispersion data suggest that the mononuclear site contains Fe and not Ni, and the four-metal cubane has the form [NiFe(3)S(4)] and not [Fe(4)S(4)]. The mononuclear site and the four-metal cluster are bridged by means of Cys(531) and one of the sulfides of the cube. CODH is organized as a dimer with a previously unidentified [Fe(4)S(4)] cluster bridging the two subunits. Each monomer is comprised of three domains: a helical domain at the N terminus, an alpha/beta (Rossmann-like) domain in the middle, and an alpha/beta (Rossmann-like) domain at the C terminus. The helical domain contributes ligands to the bridging [Fe(4)S(4)] cluster and another [Fe(4)S(4)] cluster, the B-cluster, which is involved in electron transfer. The two Rossmann domains contribute ligands to the active site C-cluster. This x-ray structure provides insight into the mechanism of biological CO oxidation and has broader significance for the roles of Ni and Fe in biological systems.

Ionic liquids based on FeCl(3) and FeCl(2). Raman scattering and ab initio calculations.

We have prepared ionic liquids by mixing either iron(II) chloride or iron(III) chloride with 1-butyl-3-methylimidazolium chloride (BMIC). Iron(II) chloride forms ionic liquids from a mole ratio of 1 FeCl(2)/3 BMIC to almost 1 FeCl(2)/1 BMIC. Both Raman scattering and ab initio calculations indicate that FeCl(4)(2-) is the predominant iron-containing species in these liquids. Iron(III) chloride forms ionic liquids from a mole ratio of 1 FeCl(3)/1.9 BMIC to 1.7 FeCl(3)/1 BMIC. When BMIC is in excess, Raman scattering indicates the presence of FeCl(4-). When FeCl(3) is in excess, Fe(2)Cl(7-) begins to appear and the amount of Fe(2)Cl(7-) increases with increasing amounts of FeCl(3). Ionic liquids were also prepared from a mixture of FeCl(2) and FeCl(3) and are discussed. Finally, we have used both Hartree-Fock and density functional theory methods to compute the optimized structures and vibrational spectra for these species. An analysis of the results using an all-electron basis set, 6-31G, as well as two different effective core potential basis sets, LANL2DZ and CEP-31G is presented.

Inhibitory and stimulating effects of various types and series of prostaglandins on in vitro biosynthesis of proteochondroitin-4,6-sulfate and protein and anaerobic glycolysis in calf rib cartilage.

The effect of various types of prostaglandins (PGs) have been studied in a semi-in-vitro system with cartilage slices of calf ribs. 0.1 mmol/1 PG B1, D2, E1, E2, F1 alpha, F2 alpha inhibit biosynthesis of Ch-4,6-S protein to a higher extent than 10 mumol/l; 1 and 2 series PG E and F (but not B) inhibit similarly, PG A2 inhibits twice as much. With biosynthesis of total protein 2-series PG A, B, E, F act more inhibitorily than 1-series PG. 10 mumol/l PG A2, E1, E2 produce cAMP-like effects, e.g. acceleration of biosynthesis of Ch-4,6-S protein and total protein as well as of anaerobic glycolysis; PG F2 alpha stimulates the first two anabolic processes, PG B1 only the second one. PG A1 stimulates Ch-4,6-S protein biosynthesis and anaerobic glycolysis, a cGMP-like effect. 20 mumol/l diBu-cAMP or cAMP (together with 0.1 mmol/l theophylline) produce stimulating and inhibitory effects on these three anabolic processes; both compounds produce additively positive or additively negative effects in connection with the inhibitory PG effects on these three anabolic processes.

[Methods of induction of a coronary thrombosis by means of direct current in the closed dog and dwarf swine thorax]. / Zur Methodik der Induktion einer Koronarthrombose mittels elektrischem Gleichstrom am geschlossenen Thorax beim Hund und Zwergschwein.

Coronary thrombosis is a perilous disease. Animal experiments may contribute to investigate its pathogenesis and treatment. The development of an experimental model of coronary thrombosis on closed thorax is important. In this report the methodics of such model is entered into, pointing at its dangers and possible complications.