The γ-subunits of chloroplast ATP synthases are about 30 amino acids longer than the bacterial or mitochondrial homologous proteins. This additional sequence is located in the mean part of the polypeptide chain and includes in green algae and higher plants two cysteines (Cys198 and Cys204 in Chlamydomonas reinhardtii) responsible for thiol regulation. In order to investigate its functional significance, a segment ranging from Asp-D210 to Arg-226 in the γ-subunit of chloroplast ATP synthase from C. reinhardtii was deleted. This deletion mutant called T2 grows photoautotrophically, but slowly than the parental strain. The chloroplast ATP synthase complex with the mutated γ is assembled, membrane bound, and as CF0CF1 displays normal ATPase activity, but photophosphorylation is inhibited by about 20 %. This inhibition is referred to lower light-induced transmembrane proton gradient. Reduction of the proton gradient is apparently caused by a disturbed functional connection between CF1 and CF0 effecting a partially leaky ATP synthase complex.