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New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II
A project to systematically investigate respiratory supercomplexes in plant mitochondria was initiated. Mitochondrial fractions from Arabidopsis, potato (Solanum tuberosum), bean (Phaseolus vulgaris), and barley (Hordeum vulgare) were carefully treated with various concentrations of the nonionic detergents dodecylmaltoside, Triton X-100, or digitonin, and proteins were subsequently separated by (a) Blue-native polyacrylamide gel electrophoresis (PAGE), (b) two-dimensional Blue-native/sodium dodecyl sulfate-PAGE, and (c) two-dimensional Blue-native/Blue-native PAGE. Three high molecular mass complexes of 1,100, 1,500, and 3,000 kD are visible on one-dimensional Blue native gels, which were identified by separations on second gel dimensions and protein analyses by mass spectrometry. The 1,100-kD complex represents dimeric ATP synthase and is only stable under very low concentrations of detergents. In contrast, the 1,500-kD complex is stable at medium and even high concentrations of detergents and includes the complexes I and $\\text{III}_{2}$. Depending on the investigated organism, 50% to 90% of complex I forms part of this supercomplex if solubilized with digitonin. The 3,000-kD complex, which also includes the complexes I and III, is of low abundance and most likely has a $\\text{III}_{4}\\text{I}_{2}$ structure. The complexes IV, II, and the alternative oxidase were not part of supercomplexes under all conditions applied. Digitonin proved to be the ideal detergent for supercomplex stabilization and also allows optimal visualization of the complexes II and IV on Blue-native gels. Complex II unexpectedly was found to be composed of seven subunits, and complex IV is present in two different forms on the Blue-native gels, the larger of which comprises additional subunits including a 32-kD protein resembling COX VIb from other organisms. We speculate that supercomplex formation between the complexes I and III limits access of alternative oxidase to its substrate ubiquinol and possibly regulates alternative respiration. The data of this investigation are available at http://www.gartenbau.uni-hannover.de/genetik/braun/AMPP.
Journal Article
Nanoelectronics : a molecular view
\"This is a reference book for graduate students and researchers in the areas of nanomaterials, nanoelectronics, solid state physics and solid state devices. Segments of this book are also useful as textbook for a course in nanoelectronics\"-- Provided by publisher.
Book
Structural basis of mitochondrial membrane bending by the I-II-III 2 -IV 2 supercomplex
Mitochondrial energy conversion requires an intricate architecture of the inner mitochondrial membrane
. Here we show that a supercomplex containing all four respiratory chain components contributes to membrane curvature induction in ciliates. We report cryo-electron microscopy and cryo-tomography structures of the supercomplex that comprises 150 different proteins and 311 bound lipids, forming a stable 5.8-MDa assembly. Owing to subunit acquisition and extension, complex I associates with a complex IV dimer, generating a wedge-shaped gap that serves as a binding site for complex II. Together with a tilted complex III dimer association, it results in a curved membrane region. Using molecular dynamics simulations, we demonstrate that the divergent supercomplex actively contributes to the membrane curvature induction and tubulation of cristae. Our findings highlight how the evolution of protein subunits of respiratory complexes has led to the I-II-III
-IV
supercomplex that contributes to the shaping of the bioenergetic membrane, thereby enabling its functional specialization.
Journal Article
Supercomplex Assembly Determines Electron Flux in the Mitochondrial Electron Transport Chain
The textbook description of mitochondrial respiratory complexes (RCs) views them as free-moving entities linked by the mobile carriers coenzyme Q (CoQ) and cytochrome c (cyt c). This model (known as the fluid model) is challenged by the proposal that all RCs except complex II can associate in supercomplexes (SCs). The proposed SCs are the respirasome (complexes I, III, and IV), complexes I and III, and complexes III and IV. The role of SCs is unclear, and their existence is debated. By genetic modulation of interactions between complexes I and III and III and IV, we show that these associations define dedicated CoQ and cyt c pools and that SC assembly is dynamic and organizes electron flux to optimize the use of available substrates.
Journal Article
Electron in action
Wouldn't it be great to build desktop applications using just your web dev skills? Electron is a framework designed for exactly that! Fully cross-platform, Electron lets you use JavaScript and Node to create simple, snappy desktop apps. Spinning up tools, games, and utilities with Electron is fast, practical, and fun! \"Electron in action\" teaches you to build cross-platform applications using JavaScript, Node, and the Electron framework. You'll learn how to think like a desktop deveoper as you build a text tool that reads and renders Markdown. You'll add OS-specific features like the file systems, menus, and clipboards, and use Chromium's tools to distribute the finished product. You'll even round off your learning with data storage, performance optimization, and testing.
Book
Precise test of lepton flavour universality in Formula omitted-boson decays into muons and electrons in Formula omitted collisions at Formula omitted with the ATLAS detector
The ratio of branching ratios of the W boson to muons and electrons, [Formula omitted]/ [Formula omitted], has been measured using [Formula omitted] of pp collision data at [Formula omitted] [Formula omitted] collected with the ATLAS detector at the LHC, probing the universality of lepton couplings. The ratio is obtained from measurements of the [Formula omitted] production cross-section in the ee, [Formula omitted] and [Formula omitted] dilepton final states. To reduce systematic uncertainties, it is normalised by the square root of the corresponding ratio [Formula omitted] for the Z boson measured in inclusive [Formula omitted] and [Formula omitted] events. By using the precise value of [Formula omitted] determined from [Formula omitted] colliders, the ratio [Formula omitted] is determined to be RW/e=0.9995±0.0022(stat)±0.0036(syst)±0.0014(ext).The three uncertainties correspond to data statistics, experimental systematics and the external measurement of [Formula omitted], giving a total uncertainty of 0.0045, and confirming the Standard Model assumption of lepton flavour universality in W-boson decays at the 0.5% level.
Journal Article
Atomistic simulation of quantum transport in nanoelectronic devices
\"Computational nanoelectronics is an emerging multi-disciplinary field covering condensed matter physics, applied mathematics, computer science, and electronic engineering. In recent decades, a few state-of-the-art software packages have been developed to carry out first-principle atomistic device simulations. Nevertheless those packages are either black boxes (commercial codes) or accessible only to very limited users (private research codes). The purpose of this book is to open one of the commercial black boxes, and to demonstrate the complete procedure from theoretical derivation, to numerical implementation, all the way to device simulation. Meanwhile the affiliated source code constitutes an open platform for new researchers. This is the first book of its kind. We hope the book will make a modest contribution to the field of computational nanoelectronics\"-- Provided by publisher.
Book
Interaction of complexes I, III, and IV within the bovine respirasome by single particle cryoelectron tomography
The respirasome is a multisubunit supercomplex of the respiratory chain in mitochondria. Here we report the 3D reconstruction of the bovine heart respirasome, composed of dimeric complex III and single copies of complex I and IV, at about 2.2-nm resolution, determined by cryoelectron tomography and subvolume averaging. Fitting of X-ray structures of single complexes I, III2, and IV with high fidelity allows interpretation of the model at the level of secondary structures and shows how the individual complexes interact within the respirasome. Surprisingly, the distance between cytochrome c binding sites of complexes III2 and IV is about 10 nm. Modeling indicates a loose interaction between the three complexes and provides evidence that lipids are gluing them at the interfaces.
Journal Article