Abstract. Cyanobacteria and plastids harbor a putative NAD(P)H-or ferredoxin-plastoquinone oxidoreductase that is homologous to the NADH-ubiquinone oxidoreductase (complex I) of mitochondria and eubacteria. The enzyme is a multimeric protein complex that consists of at least 11 subunits (NDH-A-K) and is localized in the stroma lamellae of the thylakoid membrane system. We investigated the expression of the different subunits of the enzyme in mesophyll and bundle-sheath chloroplasts of Sorghum bicolor [L.] Moench, a C4 plant of the NADPmalic enzyme type. The relative amounts of the subunits NDH-H, -J and -K were strongly increased in bundlesheath plastids as compared to mesophyll plastids. This increase was accompanied by enhanced transcript levels for all subunits except NDH-I. Because the main function of the protein complexes in the thylakoid membranes of bundle-sheath chloroplasts (photosystem I, cytochrome b6/J:complex and ATPase) is the generation of ATP for C02 fixation via cyclic electron transport, we conclude that the NAD(P)H/ferredoxin-plastoquinone oxidoreductase is an essential component of the cyclic electrontransport pathway in chloroplasts.

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Plastids contain a NAD(P)H-plastoquinone-oxidoreductase which is homologous to the eubacterial and mitochondrial NADH-ubiquinone-oxidoreductase (complex I), but the meta­bolic function of the enzyme is still not yet understood. The enzyme consists of at least eleven subunits (NDH-A-K), which are all encoded in the plastid chromosome. In this study we have investigated the tissue-specific and light-dependent expression of the subunits NDH-H and NDH-K in maize, rice and mustard by western blot analysis. No NDH-proteins were found in root tissue, indicating that the presence of the enzyme is confined to leaf plastids. Analysis of the expression during the light-dependent development from etioplasts to chloro­plasts showed that high amounts of NDH-H and -K are present in etioplasts. The same result was found for subunits of the ATPase. In contrast, components of the photosynthetic electron transport chain (PSII-B, cytochrome f and PSI-D) accumulated only after illumination. In an second investigation, the expression of NDH-proteins along the natural chloroplast develop­ mental gradient from proplastids to chloroplasts in light-grown maize leaves was analysed. NDH-H and NDH-K as well as the ATPase were present at the youngest stages of chloro­plast development, while the massive accumulation of subunits of the photosystems and the cytochrome b6/f-complex took place in older leaf sections. We conclude from these studies that a functional NAD(P)H-plastoquinone-oxidoreductase is present in etioplasts and devel­oping plastids. We suggest that the enzyme serves the generation of a proton gradient across the prothylakoid membrane that is necessary for protein integration into the membrane at developmental stages where a functional photosynthetic electron transport chain is not yet operating.

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