Proton pumps catalyze the following reaction: Mechanisms are based on energy-induced conformational changes of the protein structure or on the Q cycle.
Thus, not only throughout nature, but also within single cells, different proton pumps that are evolutionarily unrelated can be found.
[2] The process could also be seen as analogous to cycling uphill or charging a battery for later use, as it produces potential energy.
It belongs to the H+ or Na+-translocating NADH Dehydrogenase (NDH) Family (TC# 3.D.1), a member of the Na+ transporting Mrp superfamily.
Complex III is a multi-subunit transmembrane protein encoded by both the mitochondrial (cytochrome b) and the nuclear genomes (all other subunits).
[citation needed] Complex IV (EC 1.9.3.1) (also referred to as cytochrome c oxidase), is a proton pump driven by electron transport.
This enzyme is a large transmembrane protein complex found in bacteria and inner mitochondrial membrane of eukaryotes.
In a single cell (for example those of fungi and plants), representatives from all three groups of proton ATPases may be present.
In mitochondria, reducing equivalents provided by electron transfer or photosynthesis power this translocation of protons.
This process effectively couples the translocation of protons to the mechanical motion between the Loose, Tight, and Open states of F1 necessary to phosphorylate ADP.
[citation needed] In bacteria and ATP-producing organelles other than mitochondria, reducing equivalents provided by electron transfer or photosynthesis power the translocation of protons.
This membrane of plants contains two different proton pumps for acidifying the interior of the vacuole, the V-PPase and the V-ATPase.