Universität zu Köln

Kaschner, Marco, Loeschcke, Anita, Krause, Judith, Heck, Achim ORCID: 0000-0002-4975-9961, Endres, Stephan, Svensson, Vera, Wirtz, Astrid ORCID: 0000-0003-2159-3717, von Haeseler, Arndt, Jaeger, Karl-Erich, Drepper, Thomas ORCID: 0000-0002-0096-8084 and Krauss, Ulrich ORCID: 0000-0003-2219-7388 (2014). Discovery of the first light-dependent protochlorophyllide oxidoreductase in anoxygenic phototrophic bacteria. Mol. Microbiol., 93 (5). S. 1066 - 1079. HOBOKEN: WILEY. ISSN 1365-2958

Full text not available from this repository.

Abstract

In all photosynthetic organisms, chlorophylls function as light-absorbing photopigments allowing the efficient harvesting of light energy. Chlorophyll biosynthesis recurs in similar ways in anoxygenic phototrophic proteobacteria as well as oxygenic phototrophic cyanobacteria and plants. Here, the biocatalytic conversion of protochlorophyllide to chlorophyllide is catalysed by evolutionary and structurally distinct protochlorophyllide reductases (PORs) in anoxygenic and oxygenic phototrophs. It is commonly assumed that anoxygenic phototrophs only contain oxygen-sensitive dark-operative PORs (DPORs), which catalyse protochlorophyllide reduction independent of the presence of light. In contrast, oxygenic phototrophs additionally (or exclusively) possess oxygen-insensitive but light-dependent PORs (LPORs). Based on this observation it was suggested that light-dependent protochlorophyllide reduction first emerged as a consequence of increased atmospheric oxygen levels caused by oxygenic photosynthesis in cyanobacteria. Here, we provide experimental evidence for the presence of an LPOR in the anoxygenic phototrophic -proteobacterium Dinoroseobacter shibaeDFL12T. In vitro and in vivo functional assays unequivocally prove light-dependent protochlorophyllide reduction by this enzyme and reveal that LPORs are not restricted to cyanobacteria and plants. Sequence-based phylogenetic analyses reconcile our findings with current hypotheses about the evolution of LPORs by suggesting that the light-dependent enzyme of D. shibaeDFL12T might have been obtained from cyanobacteria by horizontal gene transfer.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Kaschner, Marco UNSPECIFIED UNSPECIFIED UNSPECIFIED Loeschcke, Anita UNSPECIFIED UNSPECIFIED UNSPECIFIED Krause, Judith UNSPECIFIED UNSPECIFIED UNSPECIFIED Heck, Achim UNSPECIFIED orcid.org/0000-0002-4975-9961 UNSPECIFIED Endres, Stephan UNSPECIFIED UNSPECIFIED UNSPECIFIED Svensson, Vera UNSPECIFIED UNSPECIFIED UNSPECIFIED Wirtz, Astrid UNSPECIFIED orcid.org/0000-0003-2159-3717 UNSPECIFIED von Haeseler, Arndt UNSPECIFIED UNSPECIFIED UNSPECIFIED Jaeger, Karl-Erich UNSPECIFIED UNSPECIFIED UNSPECIFIED Drepper, Thomas UNSPECIFIED orcid.org/0000-0002-0096-8084 UNSPECIFIED Krauss, Ulrich UNSPECIFIED orcid.org/0000-0003-2219-7388 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-430218
DOI:	10.1111/mmi.12719
Journal or Publication Title:	Mol. Microbiol.
Volume:	93
Number:	5
Page Range:	S. 1066 - 1079
Date:	2014
Publisher:	WILEY
Place of Publication:	HOBOKEN
ISSN:	1365-2958
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language CYANOBACTERIUM LEPTOLYNGBYA-BORYANA; RHODOBACTER-CAPSULATUS; CHLOROPHYLL BIOSYNTHESIS; DINOROSEOBACTER-SHIBAE; DIVINYL PROTOCHLOROPHYLLIDE; OXYGENIC PHOTOSYNTHESIS; NITROGEN-FIXATION; ESCHERICHIA-COLI; REDUCTASE; EVOLUTION Multiple languages Biochemistry & Molecular Biology; Microbiology Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/43021