Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.18.1.2 extracted from

  • Yacoby, I.; Pochekailov, S.; Toporik, H.; Ghirardi, M.L.; King, P.W.; Zhang, S.
    Photosynthetic electron partitioning between [FeFe]-hydrogenase and ferredoxin:NADP+-oxidoreductase (FNR) enzymes in vitro (2011), Proc. Natl. Acad. Sci. USA, 108, 9396-9401.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.18.1.2

Localization

Localization Comment Organism GeneOntology No. Textmining
thylakoid
-
 Chlamydomonas reinhardtii 9579
-

Organism

Organism UniProt Comment Textmining
Chlamydomonas reinhardtii A8J6Y8
-
-

Synonyms

Synonyms Comment Organism
FNR1
-
 Chlamydomonas reinhardtii

General Information

General Information Comment Organism
physiological function ferredoxin:NADP+-oxidoreductase-mediated NADPH production limits the efficient hydrogen production by [FeFe]-hydrogenase HydA in both purified photosystem I and isolated thylakoids. Ferredoxin:NADP+-oxidoreductase is physically bound to the photosynthetic membrane in both plant and algal thylakoids. Exogenous ferredoxin:NADP+-oxidoreductase is able to form a tight-binding complex with photosystem I. Replacing the hydrogenase with a ferredoxin-hydrogenase fusion switches the bias of electron transfer from the enzyme to the hydrogenase and results in an increased rate of hydrogen photoproduction Chlamydomonas reinhardtii