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Application of Electrophysiology Measurement to Study the Activity of Electro-Neutral Transporters
Published on: February 3, 2018
H+-PPases: yesterday, today and tomorrow
Aurelio Serrano1, José R Pérez-Castiñeira, Margareta Baltscheffsky
1Instituto de Bioquímica Vegetal y Fotosíntesis, CSIC-Universidad de Sevilla, Seville, Spain.
IUBMB Life
|April 25, 2007
Summary
Inorganic pyrophosphatase (PPase) plays a crucial role in energy transfer, acting as an alternative to ATP in early photosynthesis and continuing to be vital in modern biological energy systems.
Area of Science:
- Biochemistry
- Molecular Biology
- Bioenergetics
Background:
- Historical suggestions proposed inorganic pyrophosphate (PPi) in early photosynthesis and as an ancestral energy donor.
- Early experiments confirmed PPi hydrolysis and formation in photosynthetic bacteria, linking it to light energy and ATP-independent reactions.
Purpose of the Study:
- To review the evolution and function of H(+)-pyrophosphatases (H(+)-PPases).
- To discuss recent advancements in understanding H(+)-PPase structure, regulation, and biochemical properties.
Main Methods:
- Review of historical experimental data on PPi and PPase.
- Analysis of gene sequences from diverse organisms (plants, protists, bacteria, archaea).
- Incorporation of recent biochemical and biophysical studies on purified H(+)-PPases.
Main Results:
- PPase identified as a proton pump, present in various organisms including plants.
- Discovery of two classes of H(+)-PPases based on potassium sensitivity.
- Over 200 H(+)-PPase sequences available, facilitating evolutionary and structural studies.
Conclusions:
- H(+)-PPases are ancient and diverse enzymes involved in biological energy transfer.
- Ongoing research utilizes new methods to elucidate H(+)-PPase structure and function.
- Further investigation into H(+)-PPases, soluble PPases, and polyphosphatases is warranted.
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