FURTHER CHARACTERIZATION OF THE CHLOROPLAST GRANA MARGINS - THE NON-DETERGENT PREPARATION OF GRANAL PHOTOSYSTEM-I CANNOT REDUCE FERREDOXIN IN THE ABSENCE OF NADP(+)REDUCTION
L. Wollenberger et al., FURTHER CHARACTERIZATION OF THE CHLOROPLAST GRANA MARGINS - THE NON-DETERGENT PREPARATION OF GRANAL PHOTOSYSTEM-I CANNOT REDUCE FERREDOXIN IN THE ABSENCE OF NADP(+)REDUCTION, Biochimica et biophysica acta. Bioenergetics, 1230(1-2), 1995, pp. 10-22
The chloroplast grana margins of spinach thylakoids were isolated by s
onication and aqueous-two-phase partitioning and their electron transp
ort properties examined. Photosystem II and I electron transport activ
ities were measured and compared to the appressed and non-appressed gr
ana core and stroma lamellae, respectively, as well as to whole thylak
oids. The results show that the PS II complexes in the grana margins a
re of the PS IIbeta subtype with respect to antenna size, but are Q(B)
reducing with respect to the acceptor side properties, while the PS I
centers in the grana margins have slightly larger antennae as compare
d to the PS I centers in the stroma lamellae and are more like the PS
I, centers located in the grana domain. The ability to reduce ferredox
in and NADP(+) was also tested and it was found that the grana margin
membrane fraction was unable to reduce ferredoxin, even in the presenc
e of added artificial electron donors. The stroma lamellae and whole t
hylakoid fractions both reduced ferredoxin at high rates. However, the
grana margins could catalyze the reduction of NADP(+) when supplied w
ith the necessary components (ferredoxin, ferredoxin:NADP(+) oxidoredu
ctase, and an electron source). The results suggest that the PS I popu
lations located in the margins of the grana domain are functionally di
fferent from the PS I centers located in the stroma lamellae. The data
support a model whereby the PS I centers in the grana are primarily i
nvolved in non-cyclic electron transport, while the PS I centers locat
ed in the stroma lamellae are capable of participating in both cyclic
and non-cyclic electron transport.