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Title: Subunit interaction during catalysis: alternating site cooperativity in photophosphorylation shown by substrate modulation of (/sup 18/O)ATP species formation

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)

Pronounced substrate modulation of incorporation of water oxygen into ATP formed by photophosphorylation is observed, as measured by /sup 31/P NMR analysis of products formed from ADP and highly /sup 18/O-labeled P/sub i/. A marked increase occurs in oxygen exchange per ATP formed as ADP or P/sub i/ concentration is decreased. This is explainable by the binding-change mechanism for ATP synthesis, in which the energy linked release of ATP from one site requires the binding of ADP and P/sub i/ at an alternate site. Analysis of the distribution of /sup 18/O-labeled species arising from the ATP formed eliminates explanations for substrate modulation based on preexisting or induced enzyme heterogeneity. Furthermore, the results, together with other related findings, make participation of control sites unlikely. The occurrence of alternating site catalysis cooperativity in ATP synthesis by chloroplasts thus appears to be reasonably well established.

Research Organization:
Univ. of California, Los Angeles, CA (United States)
DOE Contract Number:
EY-76-S-03-0034
OSTI ID:
5374478
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 76:8
Country of Publication:
United States
Language:
English