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
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SYSNO ASEP 0362757 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název 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 Tvůrce(i) Sobotka, Roman (MBU-M) RID, ORCID
Tichý, Martin (MBU-M) RID
Wilde, A. (DE)
Hunter, C. N. (GB)Zdroj.dok. Plant Physiology. - : Oxford University Press - ISSN 0032-0889
Roč. 155, č. 4 (2011), 1735-1747Poč.str. 13 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova TRANSFER-RNA REDUCTASE ; DELTA-AMINOLEVULINIC-ACID ; PHOTOSYSTEM-II Vědní obor RIV EE - Mikrobiologie, virologie CEP GAP501/10/1000 GA ČR - Grantová agentura ČR CEZ AV0Z50200510 - MBU-M (2005-2011) UT WOS 000289095500025 DOI 10.1104/pp.110.167528 Anotace 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 Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2012
Počet záznamů: 1