4 resultados para Washington (D.C.). Temple of the Scottish Rite.

em Brock University, Canada


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The origins of the Scottish Rite of Freemasonry can be traced to France around 1754, when a Chapter of Claremont was founded in Paris. Initially this chapter had seven degrees, but by 1758 there were twenty-five degrees, known as the Rite of Perfection. In 1761, Stephen Morin was appointed to introduce the Rite into the New World. He began with Kingston, Jamaica and San Domingo. Further establishments were made in New Orleans, LA(1763); Albany, NY (1767); Philadelphia, PA (1782); and Charleston, SC (1783). In order to improve the disorganized state of the degrees in Europe, “Grand Constitutions” were enacted in 1786. These Constitutions formally brought into existence the “Ancient and Accepted Scottish Rite. None of the degrees of the Scottish Rite would seem to have origins in Scotland. “Scottish” is translated from the French word “Ecossais”, which is found in some of the French titles of some of the degrees of the Rite of Perfection. It is possible that the Scottish connection is a result of the involvement of a Scotsman, Andrew Michael Ramsey, who may have devised some of the degrees.

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Catalase dismutes H20 2 to O2 and H20. In successive twoelectron reactions H20 2 induces both oxidation and reduction at the heme group. In the first step the protoheme prosthetic group of beef liver catalase forms compound I, in which the heme has been oxidized from Fe3+ to Fe4+=0 and a porphyrin radical has been created. Compound II is formed by the oneelectron reduction of comp I. It retains Fe4+=0 but lacks the porphyrin radical and is catalytically inert. Molecular structures are available for Escherichia coli Hydroperoxidase II, Micrococcus Iysodeiktus, Penicillium vitale and beef liver enzymes, which contain different hemes and heme pockets. In the present work, the pockets and substrate access channels of protoheme (beef liver & Micrococcus) and heme d (HPII of E. coli and Penicillium) catalases have been analysed using Quanta™ and CharmMTM molecular modeling packages on the Silicon Graphics Iris Indigo 2 computer. Experimental studies have been carried out with two catalases, HPII (and its mutants) and beef liver. Fluoride and formate' are inhibitors of both enzymes, and their binding is modulated by the heme and by distal residues N201 & H128. Both HPII and beef liver enzymes form compound I with H202 or peracetate. The reduction of beef liver enzyme compound I to II and the decay of compound II are accelerated by fluoride. The decay of compound II is also accelerated by formate, and this reagent acts as a 2-electron donor towards compound I of both enzymes. It is concluded that heme d enzymes (Penicillium and HPII of E. coli) are formed by autocatalytic transformation of protoheme in a modified pocket which contains a characteristic serine residue as well as a partially occluded heme channel. They are less active than protoheme enzymes but also do not form the inactive compound II species. Binding of peroxide as well as fluoride and formate is prevented by mutation of H128 and modulated by mutation of N201.

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At head of title: For the International Geological Congress.

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Reflectance measurements along the c-axis of La1.875 Bao.125CU04 at temperatures above(6K) and below(O.5K) the bulk superconducting transition temperature(3K) were performed using a Bruker rapid scan spectrometer and a Martin-Puplett polarizing spectrometer. It was found that when polarized light reflected from a sample the Bruker rapid scan spectrometer has a low frequency cutoff of lOcm-1 while the Martin-Puplett polarizing spectrometer has a low frequency cutoff of 6cm-1 A superconducting pla ma edge was absent in all measurements taken. It was concluded that if a superconducting plasma edge exists in La1.875Bao.125CU04 it is below 6cm-1.