Abstract
Solvent fluctuations have been observed by electron microscopy in isolated and mitochondria in situ, in heart and liver under controlled metabolic states. Furthermore, when using mitochondrial particles, ATPase activity is demonstrated in patches on the membranous surface exposed to solvent. These observations have been extended to the molecular level using Protein Data Bank structures. The F1 model presented by Abrahams et al. (Nature 370:621–628) has less solvent content in the βe subunit when compared to the other five subunits of F1. Solvent and proton fluctuations occur in the ATP phosphorylase during ATP synthesis and the experimental ATPase states. Condensation of the mitochondrial matrix is observed during activation of the electron transport chain and ATP synthesis and may be required to obtain solvent proton fluctuations and aggregation of the protein structure. (NIH and University of Wisconsin-Madison Graduate School supported)
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