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Oxidative phosphorylation (UK / ɒ k ˈ s ɪ d. ə. t ɪ v /, US / ˈ ɑː k. s ɪ ˌ d eɪ. t ɪ v / [1]) or electron transport-linked phosphorylation or terminal oxidation is the metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing chemical energy in order to produce adenosine triphosphate (ATP).
An uncoupler or uncoupling agent is a molecule that disrupts oxidative phosphorylation in prokaryotes and mitochondria or photophosphorylation in chloroplasts and cyanobacteria by dissociating the reactions of ATP synthesis from the electron transport chain.
In 1950, first experimental evidence for the existence of photophosphorylation in vivo was presented by Otto Kandler using intact Chlorella cells and interpreting his findings as light-dependent ATP formation. [1] In 1954, Daniel I. Arnon et.al. discovered photophosphorylation in vitro in isolated chloroplasts with the help of P 32. [2]
The free energy is used to drive ATP synthesis, catalyzed by the F 1 component of the complex. [13] Coupling with oxidative phosphorylation is a key step for ATP production. However, in specific cases, uncoupling the two processes may be biologically useful.
In cyclic photophosphorylation, cytochrome b 6 f uses electrons and energy from PSI to create more ATP and to stop the production of NADPH. Cyclic phosphorylation is important to create ATP and maintain NADPH in the right proportion for the light-independent reactions. The net-reaction of all light-dependent reactions in oxygenic photosynthesis ...
Phosphorylation of glucose and fructose 6-phosphate uses two ATP from the cytoplasm. Glycolysis pay-off phase 4 Substrate-level phosphorylation 2 NADH 3 or 5 Oxidative phosphorylation: Each NADH produces net 1.5 ATP (instead of usual 2.5) due to NADH transport over the mitochondrial membrane Oxidative decarboxylation of pyruvate 2 NADH 5
Serine in an amino acid chain, before and after phosphorylation. In biochemistry, phosphorylation is the attachment of a phosphate group to a molecule or an ion. [1] This process and its inverse, dephosphorylation, are common in biology. [2] Protein phosphorylation often activates (or deactivates) many enzymes. [3] [4]
The proton gradient can be generated through either noncyclic or cyclic photophosphorylation. Of the proteins that participate in noncyclic photophosphorylation, photosystem II (PSII), plastiquinone, and cytochrome b 6 f complex directly contribute to generating the proton gradient. For each four photons absorbed by PSII, eight protons are ...