Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.3.14 (ATP synthase)
 7,042 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Photophosphorylation was discovered in chloroplasts by D. Arnon and coworkers, and in bacterial 'chromatophores' (intercytoplasmic membranes) by A. Frenkel. Initial low rates were amplified by adding electron-carrying compounds such as FMN, later shown to support the 'pseudocyclic' electron flow. ATP synthesis, and coupling to electron flow, was detected accompanying linear electron flow from H(2)O to either NADP(+) or ferricyanide. Another pattern of electron flow supporting photophosphorylation was that of a cycle around Photosystem I (PS I). Isolation and analysis of the ATP synthase showed, as with mitochondrial and bacterial analogues, an intrinsic membrane complex (CF(0)) and an extrinsic complex (CF(1)). CF(1) is a latent ATPase, activated additively by the high-energy state of the thylakoids, and by reduction of a disulfide bond on the gamma subunit. Once reduced, ATP synthesis occurs at lower energy levels. The search for an 'intermediate' linking electron flow and ATP synthesis led to the discovery of post-illumination ATP synthesis by thylakoids, where turnover occurs in the dark. Once interpreted by P.Mitchell's chemiosmotic hypothesis, this led to the discovery of light-driven proton uptake into the thylakoid lumen, with accompanying Cl(-) intake and Mg(2+) and K(+) output. Chemiosmosis was confirmed in several ways, including ATP synthesis in the dark due to an acid-to-base transition of thylakoids, and photophosphorylation accomplished in artificial lipid vesicles containing both the proton-pumping bacterial rhodopsin and a mitochondrial ATPase complex. The now generally accepted chemiosmotic interpretation is able to clarify some other aspects of photosynthesis as well.
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PMID:Photophosphorylation and the chemiosmotic perspective. 1624 26

We prepared ATP photosynthetic vesicles from inside-out membranes of Escherichia coli cells that express delta-rhodopsin (a novel light-driven H(+) transporter) and TF(0)F(1)-ATP synthase (a thermo-stable ATP synthase). These vesicles showed light-dependent ATP synthesis. Furthermore, coupling the ATP photosynthetic vesicles with an ATP-hydrolyzing hexokinase enabled light-dependent glucose consumption. The ATP photosynthetic vesicles indicate their potential to applied to light-driven ATP-regenerating bioprocess for various ATP-hydrolyzing bioproductions.
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PMID:ATP photosynthetic vesicles for light-driven bioprocesses. 2128 30

Vertebrate retinal rod Outer Segments (OS) are the site of visual transduction, an energy demanding process for which mechanisms of ATP supply are still poorly known. Glycolysis or diffusion of either ATP or phosphocreatine from the Inner Segment (IS) does not seem to display adequate timing to supply ATP for phototransduction. We have previously reported data suggesting an aerobic metabolism in OS, which would largely account for the light-stimulated ATP need of the photoreceptor. Here, by oxymetry and biochemical analyses we show that: (i) disks isolated by Ficoll flotation consume O(2) in the presence of physiological respiring substrates either in coupled or uncoupled conditions; (ii) OS homogenates contain the whole biochemical machinery for the degradation of glucose, i.e. glycolysis and the tricarboxylic acid cycle (TCA cycle), consistently with the results of our previous proteomic study. Activities of the 8 TCA cycle enzymes in OS were comparable to those in retinal mitochondria-enriched fractions. Disk and OS preparations were subjected to TEM analysis, and while they can be considered free of inner segment contaminants, immunogold with specific antibodies demonstrate the expression therein of both the visual pigment rhodopsin and F(o)F(1)-ATP synthase. Finally, double immunofluorescence on mouse retina sections demonstrated a colocalization of some respiratory complex mitochondrial proteins with rhodopsin in rod OS. Data, suggestive of the exportability of the mitochondrial machinery for aerobic metabolism, may shed light on those retinal pathologies related to energy supply impairment in OS and to mutations in TCA enzymes.
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PMID:Extramitochondrial tricarboxylic acid cycle in retinal rod outer segments. 2168 17

Great efforts in using non-photosynthetic bacteria as light-utilizing bacteria for producing biomaterials have been developed recently as increasing interest in renewable resources such as light energy. With respect to producing bio-materials industrially such as food ingredients and amino acids, huge amount of adenosine-5'-triphosphate (ATP) is required. In this work, we developed a bio-ATP-synthesis system using ATP synthase of Escherichia coil as a biocatalyst and a microbial rhodopsin which is from primitive cyanobacteria, Gloeobacter violaceus. Gloeobacter rhodopsin (GR) is a light-driven proton pump. Besides electro-chemical gradient produced by cellular respiration system, GR produces a proton gradient using light illumination which is used in additional driving force of synthesizing ATP by ATP synthase. Inverted membrane vesicle was prepared so that it could be incorporated with both of GR and ATP synthase and produced ATP in the exterior side of the vesicle in the presence of light. Since inverted membrane vesicle does not contain precursors for ATP, we added ADP and inorganic phosphate (P(i)). Then, we measured the amounts of ATP produced by ATP synthase in the presence of light. As the average value of 6 samples, 4.79 x 10(-2) micromole of ATP produced for 1 microg of GR per minute. Also, we measured again after 7 days and 65 days, respectively, in order to check the stability of the bio-ATP-synthesis system. Amount of ATP produced decayed double-exponentially and an expected value of half-life of the system was 1.5 days and 39.7 days. Our results demonstrate that ATP was regenerated successfully by using GR and ATP synthase. However, the stability of ATP synthase should be increased to use this system industrially in the near future.
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PMID:ATP regeneration system using E. coli ATP synthase and Gloeobacter rhodopsin and its stability. 2178 Apr 38