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Evolution of Life on Earth
Published in Michael Hehenberger, Zhi Xia, Huanming Yang, Our Animal Connection, 2020
Michael Hehenberger, Zhi Xia, Huanming Yang
ATP synthase is present in abundance in intracellular membranes of mitochondria, plant chloroplasts, bacteria, and other organisms. The ATP is then transported out of the mitochondria and used for various body functions, including muscle, brain, nerve, kidney, liver, and other tissues. The ADP and phosphate formed when ATP is “used,” return to the mitochondria where ATP is remade using the energy from oxidations. This process, also referred to as oxidative phosphorylation, is the most prevalent chemical reaction that occurs in all living organisms. It is estimated that organisms typically consume their body weights of ATP over the course of a day, i.e., each ATP molecule is recycled over 500 times in each body cell. ATP cannot be stored; hence its consumption closely follows its synthesis. At any time, ATP used by cell processes in the human body will add up to about 5 g.
Evolution of Life on Earth
Published in Michael Hehenberger, Zhi Xia, Our Animal Connection, 2019
ATP synthase is present in abundance in intracellular membranes of mitochondria, plant chloroplasts, bacteria, and other organisms. The ATP is then transported out of the mitochondria and used for various body functions, including muscle, brain, nerve, kidney, liver, and other tissues. The ADP and phosphate formed when ATP is “used,” return to the mitochondria where ATP is remade using the energy from oxidations. This process, also referred to as oxidative phosphorylation, is the most prevalent chemical reaction that occurs in all living organisms. It is estimated that organisms typically consume their body weights of ATP over the course of a day, i.e., each ATP molecule is recycled over 500 times in each body cell. ATP cannot be stored; hence its consumption closely follows its synthesis. At any time, ATP used by cell processes in the human body will add up to about 5 g.
Molecular Motors
Published in Yubing Xie, The Nanobiotechnology Handbook, 2012
Timothy D. Riehlman, Zachary T. Olmsted, Janet L. Paluh
A review of cellular molecular motors would not be complete without some discussion of motors that perform absolutely vital functions to cells but which are not motile along tracks. While space limitations here prevent detailed discussion, we briefly mention three interesting and well-studied motor complexes. ATP synthase is responsible for the synthesis of energy-rich ATP that is needed in a multitude of cellular processes (for review, see Boyer, 1997; García-Trejo and Morales-Ríos, 2008). The 600 kDa multiprotein complex is docked within the phospholipid membrane of cells and acts as a drive shaft (Davies et al., 2011). To drive the rotating, axial motion, a chemical gradient of hydrogen atoms across the complex is used (for review, see Yoshida et al., 2001).
Adverse Outcome Pathway for Antimicrobial Quaternary Ammonium Compounds
Published in Journal of Toxicology and Environmental Health, Part A, 2022
Supporting Data. ATP synthase requires the electrochemical proton gradient to function. Inhibition of complex I might result in collapse of mitochondrial membrane potential observed by Datta et al. (2017), Inácio et al. (2013), and Bragadin and Dell’Antone (1996). Bragadin and Dell’Antone (1996) proposed that the loss in mitochondrial membrane potential was mediated by increased membrane permeability as evidenced by calcium and potassium ion leakage. However, arrested complex I loss of membrane potential, due to loss of proton translocation, might also lead to ion release from losing the electrochemical gradient. Data suggest that complex I inhibition is likely the culprit for reducedATP production, but mitochondrial membrane disruption is a plausible alternative or complimentary mechanism that might induce similar effects on energy production. Changes in mitochondrial morphology observed by Inácio et al. (2013) might result from membrane disruption, but observed fragmentation was also associated with apoptosis. Finally, Datta et al. (2017) screened several compounds and demonstrated similar dose responses between cetylpyridinium chloride and ADBAC in reducing ATP production and oxygen consumption. Evidence indicates that the approach here to generalize cetylpyridinium chloride (Datta et al. 2017) and cetrimonium bromide (Bragadin and Dell’Antone 1996; Inácio et al. 2013) behavior to that of the ADBAC and DDAC is appropriate when discussing mitochondrial effects.
Microbial fuel cells: a sustainable solution for bioelectricity generation and wastewater treatment
Published in Biofuels, 2019
Har Mohan Singh, Atin K. Pathak, Kapil Chopra, V.V. Tyagi, Sanjeev Anand, Richa Kothari
Microorganisms can use a wide spectrum of organic compounds (carbohydrates, proteins, lipids) as carbon and energy sources. These compounds can perform as electron donors in citric acid chain reactions and form energy carrier adenosine triphosphate (ATP) molecules before cyclic chain reactions. The conglomerated carbohydrates, proteins and lipids break into their constituting monomers and form acetyl coenzyme A (CoA) by glycolysis. The CoA molecule initiates the citric acid cycle and oxidation reactions occur jointly with reduction of nicotinamide adenine dinucleotide (NAD+) and flavin adenine dinucleotide (FAD) and form nicotinamide adenine dinucleotide (NADH) and flavin adenine dinucleotide (FADH2) as electron carriers. The citric acid cycle is completed in the cytoplasm and cell membrane with the assistance of electron carriers NADH and FADH2 (Figure 2). The cell membrane passes to terminal electron acceptor through various complex membrane intermediates and ATP synthase transmembrane protein is used to convert adenosine diphosphate (ADP) to ATP. These ATP molecules act as the chemical currency of living organisms and the production process represents respiration. In the anodic compartment, a bacterial cell replaces an electrode as the terminal electron acceptor. The mechanism of the cell membrane is shown in Figure 3 [11].
Imidacloprid affects rat liver mitochondrial bioenergetics by inhibiting FoF1-ATP synthase activity
Published in Journal of Toxicology and Environmental Health, Part A, 2018
Paulo F. V. Bizerra, Anilda R. J. S. Guimarães, Marcos A. Maioli, Fábio E. Mingatto
The effects of IMD on the bioenergetics of mitochondria isolated from rat liver were determined to assess the potential involvement of mitochondria in hepatic injury induced by this insecticide. Mitochondria are responsible for most of the energy generated and used by cells through oxidative phosphorylation (Nicholls and Ferguson 2013). The energy released by oxidation of substrates in the respiratory chain is utilized to transport protons across the inner membrane, supporting the proton motive force that drives ATP synthesis by FoF1-ATP synthase or complex V, which consists of two functional proteins: F1, situated in the mitochondrial matrix, and Fo, located in the inner mitochondrial membrane. Several investigators reported that various compounds are capable of producing alterations in oxidative phosphorylation (Bridges et al. 2014; Maioli et al. 2012; Wallace and Starkov 2000). Among these are inhibitors that interfere with ATP synthesis often operating in respiratory chain complexes or in FoF1-ATP synthase (Nicholls and Ferguson 2013; Zheng and Ramirez 2000).