• molecules
  • Two phospholipid molecules, one cardiolipin and one phosphatidylethanolamine, are also found in the SdhC and SdhD subunits (not shown in the image). (wikipedia.org)
  • It receives an electron from each of four cytochrome c molecules, and transfers them to one oxygen molecule, converting molecular oxygen to two molecules of water. (wikipedia.org)
  • It is the final common pathway for oxidation - in other words harvesting high energy electrons--fuel molecules such as carbohydrate fatty acids, and amino acids by entering the cycle as Acetyl Coenzyme A (CoA). (wikibooks.org)
  • any of the group of highly complex organic compounds found in all living cells and comprising the most abundant class of all biological molecules. (thefreedictionary.com)
  • Crucially, single ROS initiation events can generate multiple reactions and radical molecules by complex chain reactions (mostly catalysed by metal cations in Fenton reactions) that affect all cell components [ 20 ]. (royalsocietypublishing.org)
  • cytochrome
  • The enzyme cytochrome c oxidase or Complex IV, EC 1.9.3.1 is a large transmembrane protein complex found in bacteria and the mitochondrion of eukaryotes. (wikipedia.org)
  • The complex contains two hemes, a cytochrome a and cytochrome a3, and two copper centers, the CuA and CuB centers. (wikipedia.org)
  • In fact, the cytochrome a3 and CuB form a binuclear center that is the site of oxygen reduction. (wikipedia.org)
  • The reduced CuA binuclear center now passes an electron on to cytochrome a, which in turn passes an electron on to the cytochrome a3-CuB binuclear center. (wikipedia.org)
  • It plays a vital role in enabling the cytochrome a3- CuB binuclear center to accept four electrons in reducing molecular oxygen to water. (wikipedia.org)
  • Summary reaction: 4 Fe2+-cytochrome c + 8 H+in + O2 → 4 Fe3+-cytochrome c + 2 H2O + 4 H+out Two electrons are passed from two cytochrome c's, through the CuA and cytochrome a sites to the cytochrome a3- CuB binuclear center, reducing the metals to the Fe2+ form and Cu+. (wikipedia.org)
  • substrate
  • Although this finding suggests a mechanism for proton-dependent substrate transport through mutually exclusive binding to glutamate-14 (Figure 1a), the structural basis for the mechanism remains poorly defined. (vanderbilt.edu)
  • To address this question, Vanderbilt Institute of Chemical Biology members Hassane Mchaourab and Jens Meiler used double electron-electron resonance spectroscopy (DEER) in combination with molecular modeling to probe the conformational changes that occur in EmrE during proton and substrate binding [R. Dastvan et al. (vanderbilt.edu)
  • In the only available low resolution crystal structure of EmrE, the protein is complexed with a cationic substrate, tetraphenylphosphonium (TPP). (vanderbilt.edu)
  • Disulfide bond formation involves electron transfer from the substrate to a disulfide carrier protein (e.g. (hindawi.com)
  • molecule
  • Both dimers are connected by a cardiolipin molecule, which has been found to play a key role in stabilization of the holoenzyme complex. (wikipedia.org)
  • Absorption of visible light by a chromophore molecule is known to induce transfer of an electron from the main orbital (S0) to one of the singlet (S1 * , S2 * …) or triplet (T) excited orbitals (Fig. 2.2). (slideshare.net)
  • What part of the molecule would be found in this hydrophobic area? (sporcle.com)
  • reduction
  • However, the currently accepted mechanism involves a rapid four-electron reduction involving immediate oxygen-oxygen bond cleavage, avoiding any intermediate likely to form superoxide. (wikipedia.org)
  • This causes a reduction in Complex I activity and disturbs its assembly. (wikipedia.org)
  • soluble
  • Based on all these data, we developed a three-dimensional structural model of the Nup82 complex that depicts how this module might be anchored to the NPC scaffold and concomitantly can interact with the soluble nucleocytoplasmic transport machinery. (rupress.org)
  • oxidation
  • After the electrons are derived from succinate oxidation via FAD, they tunnel along the [Fe-S] relay until they reach the [3Fe-4S] cluster. (wikipedia.org)
  • 2. Oxidation: In order to form an acetyl group, the hydroxyethyl group which is attached to TTP is oxidized. (wikibooks.org)
  • adopt
  • The predicted secondary structure is primarily alpha helix, but the carboxy-terminal half of the protein has high potential to adopt a coiled-coil form. (wikipedia.org)
  • structure
  • However, the crystal structure shows that FAD, Glu255, Arg286, and His242 of subunit A (not shown) are good candidates for the initial deprotonation step. (wikipedia.org)
  • This structure has led to the hypothesis that transport of protons and substrates by EmrE occurs through interconversion of the subunits between the two conformations (Figure 1b). (vanderbilt.edu)
  • ribosomes
  • These complexes are very large, even bigger than ribosomes, with its molecular mass to be in between 4 million to 10 million daltons. (wikibooks.org)
  • found
  • Human mitochondria contain two distinct isoforms of SdhA (Fp subunits type I and type II), these isoforms are also found in Ascaris suum and Caenorhabditis elegans. (wikipedia.org)
  • The products of these steps have been found, though specific subunit compositions have not been determined. (wikipedia.org)