ISSN:
1573-6881
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Physics
Notes:
Abstract Changes in the ferricyanide-reducing activity in isolated spinach chloroplasts by adenine nucleotides were measured in the presence or absence of phosphate, arsenate or pyrophosphate at 15°C. The activity changes were analyzed and ascribed to the interaction between the nucleotides and the chloroplast coupling factor (CF1). ADP and ATP (but not AMP) partially inhibited ferricyanide reduction through a 1∶1 binding to the inhibition site on CF1. When the ferricyanide reduction was coupled to either phosphorylation or arsenylation, the inhibition by ADP was released through a 1∶1 binding of the second ADP molecule to the coupling site on the CF1 with which the first ADP had been associated. The association constants of ADP for the inhibition and the coupling site were found to be approximately 5×105 and 6×104 M−1, respectively. TheKm value of ADP for arsenylation (pH 8.3) was around 17 μM. The ADP-regulated electron transport was defined based on these results. The ADP-regulated ferricyanide reduction, when coupled with phosphorylation, revealed a stoichiometry of P/Δe=1 between the amounts of esterified phosphate and reduced ferricyanide.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01516403
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