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- W100402615 abstract "The ability of vanadate to act as a photosensitizing agent and also as an inhibitor of the function of beef heart mitochondria1 F1-ATPase was investigated. Vanadate-sensitized photoinactivation of F l was biphasic with a fast rate of inactivation followed by a less sensitive phase. Monovanadate was found to be the species interacting with F1 during the photoinactivation process with a Ki of 12.3 + 0.9 pM. ADP and PPi both diminished Pi binding and Vi binding to the enzyme. ADP protected F1 from photoinactivation whereas PPi at concentration below 120 pM enhanced the process, but reduced the extent of photoinactivation when present in higher concentration. Pi at high concentration did not prevent vanadate-sensitized photoinactivation. Vanadate inhibited 3 2 ~ [ ~ i ] binding to F1 but not completely. These results suggest that Pi and Vi can bind simultaneously to the protein, and that the protein is sensitized to photoinactivation when both ligands are bound. Electrophoresis of photoinactivated F1 on an SDS gel showed the appearance of two new bands, PI and P2, located slightly above the y and 6 bands respectively. These two bands appeared to be the products of photocleavage of the heavy subunits of F1, but they could also be the modified y and 6 subunits with altered mobility on the SDS gel. Direct amino acid sequencing of the heavier peptide P I could not identify its origin because its N-terminal was ragged. Modification of P subunits also resulted from exposure of the enzyme to UV irradiation in presence of vanadate. The modified peptide had a lowered p1 compared with the native j3 subunits. This alteration of the protein as well as the loss in activity was not reversible by the reducing agents, NaBH4 o r dithiothreitol. F 1 was inhibited by vanadate in the micromolar concentration range. NMR studies of vanadium(V) species in the assay mixture at pH 7.5 established three major forms of the vanadate in solution: mono-, di-, and tetravanadate. Analysis of results from direct kinetic inhibition studies could not identify which of the three vanadate species was the inhibitor of F1. However, addition of Pi enhanced the inhibition of F1-catalyzed ATP hydrolysis, and this is consistent with divanadate being one of the i n h i b i t o r s ." @default.
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- W100402615 date "1990-01-01" @default.
- W100402615 modified "2023-09-27" @default.
- W100402615 title "Study of vanadate as a photosensitizer and kinetic inhibitor of beef heart mitochondrial F1-ATPase" @default.
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