Chlorophyll-binding subunits of photosystem I and II: Biosynthesis, chlorophyll incorporation and assembly
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F19%3A00518159" target="_blank" >RIV/61388971:_____/19:00518159 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/bs.abr.2019.02.001" target="_blank" >http://dx.doi.org/10.1016/bs.abr.2019.02.001</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/bs.abr.2019.02.001" target="_blank" >10.1016/bs.abr.2019.02.001</a>
Alternative languages
Result language
angličtina
Original language name
Chlorophyll-binding subunits of photosystem I and II: Biosynthesis, chlorophyll incorporation and assembly
Original language description
As an essential cofactor of photosystem I and photosystem II, chlorophyll plays a fundamental role in oxygenic photosynthesis. Chlorophyll molecules are responsible for both the absorption of visible light and its photochemical conversion during the process of charge separation. The vast majority of chlorophyll molecules located in photosystems is bound to six core subunits that appear to have a common evolutionary origin. Available data indicate that these large transmembrane proteins are synthesized on membrane-bound ribosomes and inserted into the thylakoid membrane with the assistance of SecY translocase and various protein factors. Newly synthesized chlorophyll-proteins associate with small transmembrane subunits, carotenoids, and other cofactors, and assemble in a stepwise manner into the final functional photosystems. This chapter summarizes our current knowledge of the individual events during photosystem biogenesis: apoprotein translation and membrane insertion, loading of chlorophyll molecules into the synthesized apoproteins, formation of assembly modules, and final assembly into the photosystems.
Czech name
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Czech description
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Classification
Type
C - Chapter in a specialist book
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Book/collection name
Metabolism, Structure and Function of Plant Tetrapyrroles: Control Mechanisms of Chlorophyll Biosynthesis and Analysis of Chlorophyll-Binding Proteins
ISBN
978-0-12-819982-4
Number of pages of the result
29
Pages from-to
195-223
Number of pages of the book
293
Publisher name
ACADEMIC PRESS LTD-ELSEVIER SCIENCE LTD
Place of publication
Londýn
UT code for WoS chapter
000500003000008