Search results for "photosynthetic bacteria"
showing 3 items of 13 documents
Antifungal activity improved by coproduction of cyclodextrins and anabaenolysins in Cyanobacteria
2015
Department of Chemistry, Nanoscience Center, University of Jyväskylä, FI-40014, Jyväskylä, Finland Cyclodextrins are cyclic oligosaccharides widely used in the pharmaceutical industry to improve drug delivery and to increase the solubility of hydrophobic compounds. Anabaenolysins are lipopeptides produced by cyanobacteria with potent lytic activity in cholesterolcontaining membranes. Here, we identified the 23- To 24-kb gene clusters responsible for the production of the lipopeptide anabaenolysin. The hybrid nonribosomal peptide synthetase and polyketide synthase biosynthetic gene cluster is encoded in the genomes of three anabaenolysin-producing strains of Anabaena.We detected previously u…
Mössbauer spectroscopy on the reaction center of Rhodopseudomonas viridis
1992
Proteins called “reaction centers” (RC) can be isolated from many photosynthetic bacteria. They have one non-heme iron in a quinone acceptor region. The RC of Rhodopseudomonas viridis contains an additional tightly bound tetra-heme cytochrome c subunit. The electronic configuration of both cytochrome and the non-heme iron has been studied in the crystallized protein by Mossbauer spectroscopy at different redox potentials, pH-values, and with an addition of o-phenanthroline. At high potentials (Eh=+500mV) all heme irons are in the low spin Fe3+-state, and at low potential (Eh=−150mV) they are low spin Fe2+ with the same Mossbauer parameters for all hemes independent of pH. Redox titrations c…
Mössbauer Spectroscopy on Photosynthetic Bacteria: Investigation of Reaction Centers of Rhodopseudomonas Viridis
1990
Crystals of 57Fe enriched reaction centers have been investigated by Mossbauer spectroscopy. The cytochrome irons are in the low spin ferric state. The non-heme iron of the electron accepting side is partly ferrous high spin and partly ferrous low spin (or ferric high spin). Under the conditions of the experiment sodium ascorbate reduces only one cytochrome iron into the ferrous low spin state. Membrane bound proteins become flexible at higher temperatures than proteins with a hydrophilic surface. They are also less flexible, at least up to temperatures of about 250 K.