chlL (Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein)
FEATURES
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ORGANISM
Prochlorococcus marinus (strain MIT 9303)
FAMILY
DESCRIPTION
Also known as CHLL_PROM3, chlL. Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. Homodimer. Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB.
Also known as CHLL_PROM3, chlL. Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, an
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chlL

Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein

Molecular Synopsis