Progressive solubilization of spinach chloroplast thylakoids by Triton X‐100 was employed to investigate the domain organization of the electron transport complexes in the thylakoid membrane. Triton/chlorophyll ratios of 1:1 were sufficient to disrupt fully the continuity of the thylakoid membrane network, but not sufficient to solubilize either photosystem I (PSI), photosystem II (PSII) or the cytochrome b 6 ‐ f (Cyt b 6 ‐ f ) complex. Progressive with the Triton concentration increase (Triton/Chl >1:1), a differential solubilization of the three electron transport complexes was observed. (a) Solubilization of the Cyt b 6 ‐ f complex from the thylakoid membrane preceded that of PSI and apparently occurred early in the solubilization of stroma‐exposed segments of the chloroplast lamellae. (b) The initial removal of chlorophyll (up to 40% of the total) occurred upon solubilization of PSI from the stroma‐exposed lamella regions in which PSI is localized. (c) The tightly appressed membrane of the grana partition regions was markedly resistant to solubilization by Triton X‐100. Thus, solubilization of PSII from this membrane region was initiated only after all Cyt b 6 ‐ f and PSI complexes were removed from the chloroplast lamellae. The results support the notion of extreme lateral heterogeneity in the organization of the electron transport complexes in higher plant chloroplasts and suggest a Cyt b 6 ‐ f localization in the membrane of the narrow fret regions which serve as a continum between the grana and stroma lamellae.
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