Počet záznamů: 1

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

  1. 1.
    0362757 - MBU-M 2012 RIV US eng J - Článek v odborném periodiku
    Sobotka, Roman - Tichý, Martin - Wilde, A. - Hunter, C. N.
    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.
    Plant Physiology. Roč. 155, č. 4 (2011), 1735-1747 ISSN 0032-0889
    Grant CEP: GA ČR GAP501/10/1000
    Výzkumný záměr: CEZ:AV0Z50200510
    Klíčová slova: TRANSFER-RNA REDUCTASE * DELTA-AMINOLEVULINIC-ACID * PHOTOSYSTEM-II
    Kód oboru RIV: EE - Mikrobiologie, virologie
    Impakt faktor: 6.535, rok: 2011

    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
    Trvalý link: http://hdl.handle.net/11104/0198992