Download Cytochrome Systems: Molecular Biology and Bioenergetics by E. C. Slater (auth.), S. Papa, B. Chance, L. Ernster (eds.) PDF

By E. C. Slater (auth.), S. Papa, B. Chance, L. Ernster (eds.)

This quantity relies at the lawsuits of a world Symposium on "Cytochrome structures: Molecular Biology and Bioenergetics" that used to be held at Selva di Fasano close to Bari, Italy, among April 7 and 11,1987. It comprises papers masking the themes mentioned on the Symposium, contributed either through individuals of the assembly and by means of a few invited audio system who weren't capable of attend. the purpose of the Symposium was once to compile specialists in a number of rese­ arch innovations at the moment being utilized to the examine of cytochrome structures, together with molecular genetics, protein chemistry, enzymology of electron move and protonmotive job in energy-transducing organic mem­ branes. as a result of excessive measure of complexity of cytochrome structures and the expanding sophistication lately of different experimen­ tal methods, there was a becoming specialization - occasionally even an inclination to "over-specialization" - between scientists operating during this box. This in itself looked as if it would justify a gathering the place representatives of assorted disciplines may possibly alternate their effects and talk about their conclusions. moreover, and maybe even extra importantly, it was once felt that conferences of this sort provide a chance for a "cross-fertilization" of ways and ideas between representatives of assorted fields of technology. the current assembly proved to be an abundant representation of the luck of such an inter­ action.

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Mitchell,P. Biol. 62, 327-367. G. Chem. 255, 9828-9837. , Feher,G. press. New York. ) pp. 3-18, Plenum, New York. Saraste,M. (1984) FEBS Lett. 166, 367-372. , (1984) EMBO J. 3, 2137-2143. Acad. Sci. 81, 674-678. 40 GENES AND SEQUENCES FOR SUBUNITS OF RESPIRATORY COMPLEXES IN Paracoccus denitrificans Bernd Ludwig, Barbara Kurowski, Gunnar Panskus, and Peter Steinrucke Institute of Biochemistry, Medical University D 2400 Lubeck, West Germany INTRODUCTION The bacterium Paracoccus denitrificans has long been discussed in context of the evolutIonary origin Of mitochondria (1) based on a number of features suggesting its ancestral role in organelle formation.

Shows considerable overall homology to corresponding proteins from Neurospora crassa and Saccharomyces cereviciae, especially at its COOH-terminal region where several cysteines thought to be the ligands for the 2Fe-2S cluster are located. The hydropathy profile for this protein is compatible with the current thinking that the Rieske Fe-S protein is located almost entirely in the periplasm, with the exception of an NH2 -terminal membrane-spanning helix anchoring it to the membrane. It may De folded in such a way that the Fe-S cluster positioned in an hydrophobic pocket is not too far fjgm the membrane/aqueous interface at the periplasmic side of the membrane .

An additional bond with the heme iron is established through the sulfur atom of a conserved methionine residue (met-Z05). The topology of the heme ligands suggests that the membrane bound cytochrome C1 and the water-soluble cytochrome c are folded in a similar way (Dickerson and Timkovich 1975). The cytochrome C1 of Rhodobacter is synthesized as a larger precursor. The N-terminal sequence of the mature subunit starts from the asn-ZZ of the DNA deduced sequence (Gabellini and Sebald 1986). The pre-apo-cytochrome c1 , includes a hydrophobic pre-sequence that leads the secretion of the polypeptide to the outer side of the cytoplasmic membrane.

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