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Mechanism of inhibition of mitochondrial adenosine triphosphatase by dicyclohexylcarbodiimide and oligomycin: relationship to ATP synthesis.

Measurement of the rate of [gamma-32P]ATP binding (k1) and release (k-1) from catalytic sites on submitochondrial particles permitted calculation of the affinity constant in catalytic sites (k1 = K1/k1-1) of 10(12) M-1. This value is the same as that determined previously for the solubilized ATPase...

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Bibliographic Details
Published in:Proc Natl Acad Sci U S A
Main Author: Penefsky, H S
Format: Artigo
Language:Inglês
Published: National Academy of Sciences 1985
Subjects:
Online Access:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC397317/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2858849/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.82.6.1589
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