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Functional assignments for the carboxyl-terminal domains of the ferrochelatase from Synechocystis PCC 6803: The CAB domain plays a regulatory role, and region II is essential for catalysis
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SYSNO ASEP 0362757 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Functional assignments for the carboxyl-terminal domains of the ferrochelatase from Synechocystis PCC 6803: The CAB domain plays a regulatory role, and region II is essential for catalysis Author(s) Sobotka, Roman (MBU-M) RID, ORCID
Tichý, Martin (MBU-M) RID
Wilde, A. (DE)
Hunter, C. N. (GB)Source Title Plant Physiology. - : Oxford University Press - ISSN 0032-0889
Roč. 155, č. 4 (2011), 1735-1747Number of pages 13 s. Language eng - English Country US - United States Keywords TRANSFER-RNA REDUCTASE ; DELTA-AMINOLEVULINIC-ACID ; PHOTOSYSTEM-II Subject RIV EE - Microbiology, Virology R&D Projects GAP501/10/1000 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z50200510 - MBU-M (2005-2011) UT WOS 000289095500025 DOI 10.1104/pp.110.167528 Annotation Ferrochelatase (FeCH) catalyses the insertion of Fe2+ into protoporphyrin forming protoheme. In photosynthetic organisms FeCH and Mg-chelatase lie at a biosynthetic branchpoint where partitioning down the heme and chlorophyll pathways occurs. Unlike their mammalian, yeast and other bacterial counterparts cyanobacterial and algal FeCHs as well as FeCH2 isoform from plants possess a C-terminal CAB domain with a putative chlorophyll-binding motif. We found that the CAB domain in the cyanobacterium Synechocystis 6803 is not required for catalytic activity but is essential for dimerization of FeCH and its absence causes aberrant accumulation of chlorophyll-protein complexes under high light accompanied by high levels of the chlorophyll precursor chlorophyllide Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2012
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