Structure of an ancient respiratory system

• Hongjun Yu ^[2] ; Chang-Hao Wu ^[1] ; Gerrit J. Schut ^[1]
  1. [1] University of Georgia

     University of Georgia

     Estados Unidos

     
  2. [2] Van Andel Research Institute
• Localización: Cell, ISSN 0092-8674, Vol. 173, Nº. 7, 2018, págs. 1636-1649
• Idioma: inglés
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• Resumen

  • Hydrogen gas-evolving membrane-bound hydrogenase (MBH) and quinone-reducing complex I are homologous respiratory complexes with a common ancestor, but a structural basis for their evolutionary relationship is lacking. Here, we report the cryo-EM structure of a 14-subunit MBH from the hyperthermophile Pyrococcus furiosus. MBH contains a membrane-anchored hydrogenase module that is highly similar structurally to the quinone-binding Q-module of complex I while its membrane-embedded ion-translocation module can be divided into a H +- and a Na +-translocating unit. The H +-translocating unit is rotated 180° in-membrane with respect to its counterpart in complex I, leading to distinctive architectures for the two respiratory systems despite their largely conserved proton-pumping mechanisms. The Na +-translocating unit, absent in complex I, resembles that found in the Mrp H +/Na + antiporter and enables hydrogen gas evolution by MBH to establish a Na + gradient for ATP synthesis near 100°C. MBH also provides insights into Mrp structure and evolution of MBH-based respiratory enzymes.