8DQV
The 1.52 angstrom CryoEM structure of the [NiFe]-hydrogenase Huc from Mycobacterium smegmatis - catalytic dimer (Huc2S2L)
Summary for 8DQV
Entry DOI | 10.2210/pdb8dqv/pdb |
Related | 7UTD 7UUR 7UUS |
EMDB information | 26767 26801 26802 27661 |
Descriptor | Hydrogenase-2, large subunit, Hydrogenase-2, small subunit, OXYGEN ATOM, ... (9 entities in total) |
Functional Keywords | [nife] hydrogenase, membrane-associated, complex, quinone transport, electron transport |
Biological source | Mycolicibacterium smegmatis More |
Total number of polymer chains | 4 |
Total formula weight | 187167.04 |
Authors | Grinter, R.,Venugopal, H.,Kropp, A.,Greening, C. (deposition date: 2022-07-20, release date: 2023-01-04, Last modification date: 2023-03-29) |
Primary citation | Grinter, R.,Kropp, A.,Venugopal, H.,Senger, M.,Badley, J.,Cabotaje, P.R.,Jia, R.,Duan, Z.,Huang, P.,Stripp, S.T.,Barlow, C.K.,Belousoff, M.,Shafaat, H.S.,Cook, G.M.,Schittenhelm, R.B.,Vincent, K.A.,Khalid, S.,Berggren, G.,Greening, C. Structural basis for bacterial energy extraction from atmospheric hydrogen. Nature, 615:541-547, 2023 Cited by PubMed Abstract: Diverse aerobic bacteria use atmospheric H as an energy source for growth and survival. This globally significant process regulates the composition of the atmosphere, enhances soil biodiversity and drives primary production in extreme environments. Atmospheric H oxidation is attributed to uncharacterized members of the [NiFe] hydrogenase superfamily. However, it remains unresolved how these enzymes overcome the extraordinary catalytic challenge of oxidizing picomolar levels of H amid ambient levels of the catalytic poison O and how the derived electrons are transferred to the respiratory chain. Here we determined the cryo-electron microscopy structure of the Mycobacterium smegmatis hydrogenase Huc and investigated its mechanism. Huc is a highly efficient oxygen-insensitive enzyme that couples oxidation of atmospheric H to the hydrogenation of the respiratory electron carrier menaquinone. Huc uses narrow hydrophobic gas channels to selectively bind atmospheric H at the expense of O, and 3 [3Fe-4S] clusters modulate the properties of the enzyme so that atmospheric H oxidation is energetically feasible. The Huc catalytic subunits form an octameric 833 kDa complex around a membrane-associated stalk, which transports and reduces menaquinone 94 Å from the membrane. These findings provide a mechanistic basis for the biogeochemically and ecologically important process of atmospheric H oxidation, uncover a mode of energy coupling dependent on long-range quinone transport, and pave the way for the development of catalysts that oxidize H in ambient air. PubMed: 36890228DOI: 10.1038/s41586-023-05781-7 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (1.52 Å) |
Structure validation
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