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Association of Ferredoxin-NADP Oxidoreductase with the
Chloroplastic Pyridine Nucleotide Dehydrogenase Complex in Barley
Leaves1
María José Quiles and
Juan Cuello*
Departamento de Biología Vegetal, Facultad de
Biología, Universidad de Murcia, Campus de Espinardo,
E-30100 Murcia, Spain
Barley (Hordeum
vulgare L.) leaves were used to isolate and characterize the
chloroplast NAD(P)H dehydrogenase complex. The stroma fraction and the
thylakoid fraction solubilized with sodium deoxycholate were analyzed
by native polyacrylamide gel electrophoresis, and the enzymes detected
with NADH and nitroblue tetrazolium were electroeluted. The enzymes
electroeluted from band S from the stroma fraction and from bands T1
(ET1) and T2 from the thylakoid fraction solubilized with sodium
deoxycholate had ferredoxin-NADP oxidoreductase (FNR; EC 1.18.1.2) and
NAD(P)H-FeCN oxidoreductase (NAD[P]H-FeCNR) activities. Their
NADPH-FeCNR activities were inhibited by
2 -monophosphoadenosine-5-diphosphoribose and by enzyme incubation
with p-chloromercuriphenylsulfonic acid (p-CMPS), NADPH,
and p-CMPS plus NADPH. They presented
Michaelis constant NADPH values that were similar to those of FNRs from
several sources. Their NADH-FeCNR activities, however, were not
inhibited by 2-monophosphoadenosine-5-diphosphoribose but were weakly
inhibited by enzyme incubation with NADH, p-CMPS, and p-CMPS plus NADH.
We found that only ET1 contained two polypeptides of 29 and 35 kD,
which reacted with the antibodies raised against the mitochondrial
complex I TYKY subunit and the chloroplast ndhA gene
product, respectively. However, all three enzymes contained two
polypeptides of 35 and 53 kD, which reacted with the antibodies raised
against barley FNR and the NADH-binding 51-kD polypeptide of the
mitochondrial complex I, respectively. The results suggest that ET1 is
the FNR-containing thylakoidal NAD(P)H dehydrogenase complex.
1
This work was supported by the Spanish
Dirección General de Investigación Científica y
Técnica (grant no. PB94-1141).
*
Corresponding author; e-mail jcuello{at}fcu.um.es; fax
34-68-363963.
Plant Physiol. (1998) 117: 235-244
Copyright Clearance Center: 0032-0889/98/117/0235/10
© 1998 American Society of Plant Physiologists
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