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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F11%3A00362757" target="_blank" >RIV/61388971:_____/11:00362757 - isvavai.cz</a>

Alternative codes found

RIV/60076658:12640/11:43882333

Result on the web

<a href="http://dx.doi.org/10.1104/pp.110.167528" target="_blank" >http://dx.doi.org/10.1104/pp.110.167528</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1104/pp.110.167528" target="_blank" >10.1104/pp.110.167528</a>

Result language

angličtina

Original language name

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

Original language description

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

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EE - Microbiology, virology

OECD FORD branch

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Project

<a href="/en/project/GAP501%2F10%2F1000" target="_blank" >GAP501/10/1000: Identification and localization of protein complexes involved in the regulation of chlorophyll biosynthesis</a><br>

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2011

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Plant Physiology

ISSN

0032-0889

e-ISSN

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Volume of the periodical

155

Issue of the periodical within the volume

4

Country of publishing house

US - UNITED STATES

Number of pages

13

Pages from-to

1735-1747

UT code for WoS article

000289095500025

EID of the result in the Scopus database

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