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Balancing chloroplast redox status – regulation of FNR binding and release

LEA VOJTA ; Ruđer Bošković Institute, Division of Molecular Biology, Laboratory for Electron Microscopy, Bijenička 54, 10000 Zagreb, Croatia
LUCIJA HORVAT ; Ruđer Bošković Institute, Division of Molecular Biology, Laboratory for Electron Microscopy, Bijenička 54, 10000 Zagreb, Croatia
HRVOJE FULGOSI ; Ruđer Bošković Institute, Division of Molecular Biology, Laboratory for Electron Microscopy, Bijenička 54, 10000 Zagreb, Croatia

Puni tekst: engleski, pdf (163 KB) str. 25-31 preuzimanja: 493* citiraj
APA 6th Edition
VOJTA, L., HORVAT, L. i FULGOSI, H. (2012). Balancing chloroplast redox status – regulation of FNR binding and release. Periodicum biologorum, 114 (1), 25-31. Preuzeto s https://hrcak.srce.hr/80894
MLA 8th Edition
VOJTA, LEA, et al. "Balancing chloroplast redox status – regulation of FNR binding and release." Periodicum biologorum, vol. 114, br. 1, 2012, str. 25-31. https://hrcak.srce.hr/80894. Citirano 21.09.2020.
Chicago 17th Edition
VOJTA, LEA, LUCIJA HORVAT i HRVOJE FULGOSI. "Balancing chloroplast redox status – regulation of FNR binding and release." Periodicum biologorum 114, br. 1 (2012): 25-31. https://hrcak.srce.hr/80894
Harvard
VOJTA, L., HORVAT, L., i FULGOSI, H. (2012). 'Balancing chloroplast redox status – regulation of FNR binding and release', Periodicum biologorum, 114(1), str. 25-31. Preuzeto s: https://hrcak.srce.hr/80894 (Datum pristupa: 21.09.2020.)
Vancouver
VOJTA L, HORVAT L, FULGOSI H. Balancing chloroplast redox status – regulation of FNR binding and release. Periodicum biologorum [Internet]. 2012 [pristupljeno 21.09.2020.];114(1):25-31. Dostupno na: https://hrcak.srce.hr/80894
IEEE
L. VOJTA, L. HORVAT i H. FULGOSI, "Balancing chloroplast redox status – regulation of FNR binding and release", Periodicum biologorum, vol.114, br. 1, str. 25-31, 2012. [Online]. Dostupno na: https://hrcak.srce.hr/80894. [Citirano: 21.09.2020.]

Sažetak
Working in synchrony, photosynthetic charge separation, electron transfer, and redox reactions generate proton motive force necessary for the synthesis of ATP and funneling of electrons toward stromal reducing equivalent NADPH. The last step of electron transfer from ferredoxin to NADP+ is catalyzed by ferredoxin-NADP+ oxidoreductase (FNR). Two proteins, TROL (thylakoid rhodanese-like) and Tic62 (62 kDa component of the translocon at the inner envelope of chloroplasts), have been characterized and shown to form dynamic complexes with FNR. Inactivation of TROL leads to changes in efficiency of electron transfer and induction of non-photochemical quenching. TROL-deficient plants have changed nuclear gene expression with up-regulation of NADPH-dependent malic enzyme, which can form NADPH in an alternative pathway. Thus, NADPH synthesis, mediated by FNR-TROL interaction, may be the source element in metabolic retrograde signal-transduction pathway linking light reactions with nuclear gene expression.

Ključne riječi
photosynthesis; linear electron flow; retrograde signalling; electron partitioning; stromal redox status

Hrčak ID: 80894

URI
https://hrcak.srce.hr/80894

Posjeta: 774 *