Abstract
Plastids contain an NAD(P)H dehydrogenase (NAD(P)H DH) complex which is homologous to the mitochondrial complex I (EC 1.6.5.3). We describe the isolation and partial characterization of the chloroplast NAD(P)H DH complex of Hordeum vulgare L. When chloroplasts were fractionated the stromal thylakoids had a specific NADH-ferricyanide oxidoreductase (NADH-FeCNR) activity seven times higher than that of granal thylakoids and contained abundant polypeptide which reacted with the antibody raised against barley NdhA polypeptide. Native PAGE resolved three NADH-nitroblue tetrazolium (NBT)-staining enzyme bands from detergent-solubilized stroma thylakoids and one from the stroma fraction of chloroplasts. The two major thylakoid enzymes and the stromal enzyme showed NAD(P)H-FeCNR and ferredoxin-NADP oxidoreductase (FNR) (EC 1.18.1.2) activities, and the presence of FNR protein was confirmed by Western blotting. Only the major thylakoid enzyme of high molecular weight was found to contain the NdhA polypeptide, a core subunit of the NAD(P)H DH complex. Analysis by SDS–PAGE of the enzyme complex revealed nine polypeptides with molecular masses ranging from 18 to 63 kDa.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
