2022
DOI: 10.3390/ijms23169504
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The Mechanism of Energy Coupling in H+/Na+-Pumping Membrane Pyrophosphatase—Possibilities and Probabilities

Abstract: Membrane pyrophosphatases (mPPases) found in plant vacuoles and some prokaryotes and protists are ancient cation pumps that couple pyrophosphate hydrolysis with the H+ and/or Na+ transport out of the cytoplasm. Because this function is reversible, mPPases play a role in maintaining the level of cytoplasmic pyrophosphate, a known regulator of numerous metabolic reactions. mPPases arouse interest because they are among the simplest membrane transporters and have no homologs among known ion pumps. Detailed phylog… Show more

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Cited by 3 publications
(4 citation statements)
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“…Conversely, two recently published papers from Baykov and co-workers (Baykov et al, 2022 ; Malinen et al, 2022 ) continue to posit their billiard-type mechanism, where hydrolysis precedes pumping. By using quenched-flow measurements on Tm PPase at 40 °C, they demonstrate that hydrolysis is the most likely rate-determining step, which is consistent with our electrometric measurements on Tm PPase at 20 °C.…”
Section: Discussionmentioning
confidence: 99%
“…Conversely, two recently published papers from Baykov and co-workers (Baykov et al, 2022 ; Malinen et al, 2022 ) continue to posit their billiard-type mechanism, where hydrolysis precedes pumping. By using quenched-flow measurements on Tm PPase at 40 °C, they demonstrate that hydrolysis is the most likely rate-determining step, which is consistent with our electrometric measurements on Tm PPase at 20 °C.…”
Section: Discussionmentioning
confidence: 99%
“…Conversely, two recently-published papers from Baykov and co-workers (Baykov et al, 2022; Malinen et al, 2022) continue to posit their “billiard-type” mechanism, where hydrolysis precedes pumping. By using stopped-flow measurements on Tm PPase at 40 °C, they demonstrate that hydrolysis is the most likely rate-determining step, which is consistent with our SURFE 2 R N1 data on Tm PPase at 20 °C.…”
Section: Discussionmentioning
confidence: 99%
“…M-PPases belong to an evolutionarily ancient protein family [ 4 , 5 , 6 ] and act as primary ion pumps in plants, algae and some protozoans, bacteria, and archaea that producing proton and/or sodium gradients [ 7 , 8 ]. M-PPases are among the simplest membrane transporters and have no homologs among known ion pumps [ 9 ]. These unique enzymes couple the reversible reaction of phosphorolysis/synthesis of PP i to H + and/or Na + pumping across cytoplasm.…”
Section: Introductionmentioning
confidence: 99%
“…Significant progress has been made in recent years in understanding the structural and functional properties of M-PPases and the mechanism through which these PPases couple PP i hydrolysis with cation transport [ 9 , 16 , 17 , 18 , 19 ].…”
Section: Introductionmentioning
confidence: 99%