Answers are grounded in this paper and cite their sources.
Neighbouring subunits of CF 0 (I–III) and between cf 0 and CF 1 (α‐ϵ) of the chloroplast ATP synthase have been examined by cross‐linking with Cu‐phenanthroline (CuP) and bifunctional, cleavable imidoesters. Imidoesters caused cross‐links of α‐II, β‐I, β‐II, γ‐II, δ‐I and ϵ‐III as well as of I 2 , I–III, II–III and III 2 of the CF 0 portion. subunits α‐II, β‐I, β‐II, γ‐II and I‐I are close enough to form intermolecular cystine bridges upon CuP‐catalyzed oxidation of sH groups. The results indicate that: (i) mainly interactions of the CF 1 subunits α, β and γ with the CF 0 polypeptides I and II are required for binding of CF 1 to the thylakoid membrane; (ii) subunit ϵ interacts directly with CF 0 ‐III; (iii) the CF 0 portion contains a dimer of subunit I; (iv) subunits α and β appear to be structurally non‐equivalent within the protein complex.
No takes yet. Share an insight, caveat, or question.
Karl‐Heinz Süss (1986) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: