Localization of NADPH‐protochlorophyllide oxidoreductase in dark‐grown wheat (Triticum aestivum) by immuno‐electron microscopy before and after transformation of the prolamellar bodies

Abstract

The localization of NADPH‐protochlorophyllide oxidoreductase (PChlide reductase, EC 1.6.99.–) in dark‐grown and in irradiated dark‐grown leaves of wheat (Triticum aestivum L. cv. Walde) was investigated by subjecting thin sections of Lowicryl K4M‐embedded leaf pieces to a monospecific antiserum raised against PChlide reductase followed by protein A‐gold. A well‐preserved antigenicity of the tissue was achieved by polymerizing the resin under UV‐light at low temperature. In dark‐grown leaves PChlide reductase was found in prolamellar bodies only. In leaves irradiated for 30 min with white light PChlide reductase was found not only in the transformed prolamellar bodies but also to a large extent in connection with the prothylakoids. The localization of PChlide reductase is discussed in relation to fluorescence emission spectra of the dark‐grown and greening leaves. We conclude that the light‐dependent transformation of protochlorophyllide to chlorophyllide initiates a translocation of PChlide reductase from the prolamellar bodies to the prothylakoids.