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H + ‐proton‐pumping inorganic pyrophosphatase: a tightly membrane‐bound family
Author(s) -
Baltscheffsky Margareta,
Schultz Anders,
Baltscheffsky Herrick
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00617-1
Subject(s) - inorganic pyrophosphatase , pyrophosphatases , rhodospirillum rubrum , pyrophosphate , pyrophosphatase , atp synthase , proton , proton transport , atpase , biochemistry , chemistry , chemiosmosis , enzyme , membrane , physics , quantum mechanics
The earliest known H + ‐proton‐pumping inorganic pyrophosphatase, the integrally membrane‐bound H + ‐proton‐pumping inorganic pyrophosphate synthase from Rhodospirillum rubrum , is still the only alternative to H + ‐ATP synthase in biological electron transport phosphorylation. Cloning of several higher plant vacuolar H + ‐proton‐pumping inorganic pyrophosphatase genes has led to the recognition that the corresponding proteins form a family of extremely similar proton‐pumping enzymes. The bacterial H + ‐proton‐pumping inorganic pyrophosphate synthase and two algal vacuolar H + ‐proton‐pumping inorganic pyrophosphatases are homologous with this family, as deduced from their cloned genes. The prokaryotic and algal homologues differ more than the H + ‐proton‐pumping inorganic pyrophosphatases from higher plants, facilitating recognition of functionally significant entities. Primary structures of H + ‐proton‐pumping inorganic pyrophosphatases are reviewed and compared with H + ‐ATPases and soluble proton‐pumping inorganic pyrophosphatases.