Hydroperoxidases in cyanobacteria.
Abstract
Cyanobacteria are the most primitive, oxygenic photosynthetic organisms. The advent of primordial cyanobacteria marked the decisive point in evolution, because these organisms were (most probably) the first to liberate bulk amounts of oxygen gas into an anoxic biosphere. It seems likely that cyanobacteria were (among) the first to elaborate mechanisms for aerobic respiration, consequently being the only organisms which have accommodated both oxygenic photosynthesis and aerobic respiration within a single prokaryotic cell. It is known that reduced oxygen species (e.g. superoxide and hydrogen peroxide) are byproducts of these types of electron transport chains. So it is assumed that cyanobacteria have developed first strategies of adapting to oxidative stress by developing the corresponding scavenging enzymes (e.g. superoxide dismutases and hydroperoxidases). But hydrogen peroxide scavenging enzymes (hydroperoxidases, namely peroxidases and catalases) in cyanobacteria have not been investigated down to detail so far. It seems likely that one type of peroxidase in these organisms is the most likely ancestor of the hydrogen peroxide-scavenging peroxidases and that catalase activities are exhibited by typical prokaryotic catalase-peroxidases. It is the aim of this project to purify, characterize and finally localize hydrogen peroxide scavenging enzymes (hydroperoxidases) from two unicellular cyanobacterial species Anacystis nidulans (Synechococcus PCC 6301), Synechocystis PCC 6803 and one filamentous species, namely Anabaena variabilis PCC 7937. The present project should help to push forward efforts in establishing cyanobacteria as simple prokaryotic models for studying the interaction of photosynthetic and/or respiratory electron transport and the response hydrogen peroxide scavenging enzymes as a result of endogenously or exogenously induced oxidative stress situations.
Publications
Purification and characterization of a hydroperoxidase from the cyanobacterium Synechocystis PCC 6803: identification of its gene by peptide mass mapping using matrix assisted laser desorption ionization time-of-flight mass spectrometry.
Autoren: Regelsberger, G; Obinger, C; Zoder, R; Altmann, F; Peschek, GA Jahr: 1999
Journal articles
A monofunctional catalase from Chlorogloeopsis fritschii.
Autoren: Zoder, R; Maghakian, B; Jandrasits, W; Regelsberger, G; Obinger, C; Ahorn, H; Peschek, G A Jahr: 2001
Journal articles
external links and characteristics of the publication:Catalase-peroxidase from synechocystis is capable of chlorination and bromination reactions.
Autoren: Jakopitsch, C; Regelsberger, G; Furtmüller, PG; Rüker, F; Peschek, GA; Obinger, C Jahr: 2001
Journal articles
Occurrence and biochemistry of hydroperoxidases in oxygenic phototrophic prokaryotes (cyanobacteria)
Autoren: Regelsberger, G., Jakopitsch, C., Plasser, L., Schwaiger, H., Furtmüller, P. G., Peschek, G. A., Zámocky, M. and Obinger, C. Jahr: 2002
Journal articles
Turning points in the complex evolution of the peroxidase-catalase superfamily: Molecular phylogeny of hybrid peroxidases
Autoren: Zamocky, M. Furtmüller, P.G. & Obinger, C. Jahr: 2012
Conference & Workshop proceedings, paper, abstract
external links and characteristics of the publication:The cyanobacterial aa3-type cytochrome c oxidase: Strategies for overexpression of Synechocystis sp. PCC6803 cta genes in Rhodobacter sphaeroides.
Autoren: Paumann, M., Hiser, C., Rueker, F., Obinger, C., Ferguson-Miller, S., Peschek, G.A. Jahr: 2000
Conference & Workshop proceedings, paper, abstract
external links and characteristics of the publication:The 2.0A resolution structure of the catalytic portion of a cyanobacterial membrane-bound manganese superoxide dismutase.
Autoren: Atzenhofer, W; Regelsberger, G; Jacob, U; Peschek, G; Furtmüller, P; Huber, R; Obinger, C Jahr: 2002
Journal articles
Hydroperoxidases in oxygenic phototrophic organelles and organisms: a comparison of chloroplasts and cyanobacteria
Autoren: Regelsberger, G., Jakopitsch, C., Plasser, L., Furtmüller, P.G., Paumann, M., Peschek, G.A., Obinger, C. Jahr: 2003
Chapter in collected volumes
external links and characteristics of the publication:DE NOVO designed heme peroxidase base on the C-terminal domain of bifunctional catalase-peroxidase
Autoren: Zamocky, M. Gasselhuber, B. Furtmüller, P.G. & Obinger, C. Jahr: 2012
Conference & Workshop proceedings, paper, abstract
external links and characteristics of the publication:
Project staff
Christian Obinger
Univ.Prof. Mag.rer.nat. Dr.rer.nat. Christian Obinger
christian.obinger@boku.ac.at
Tel: +43 1 47654-10011
Project Leader
01.08.1997 - 30.10.2000

dx.doi.org