Entry Database : PDB / ID : 8pow Structure visualization Downloads & linksTitle Crystal Structure of the C19G variant of the membrane-bound [NiFe]-Hydrogenase from Cupriavidus necator in the air-oxidized state at 1.61 A Resolution. Components(Uptake hydrogenase ...) x 2 Details Keywords OXIDOREDUCTASE / [NIFE]-HYDROGENASE / HYDROGENASE / OXYGEN-TOLERANCE / HYDROGEN CATALYSIS / KNALLGASBACTERIA / PROTEOBACTERIA / METALLOENZYME / BIMETALLIC / NI-FE ACTIVE SITE / [4FE-3S] / PROXIMAL CLUSTER / AEROBIC HYDROGEN BACTERIA / ELECTRON TRANSFER / METALLOPROTEIN / CATALYTIC CENTER / MEMBRANE / MEMBRANE-BOUND / OXIDOREDUCTASE-OXIDOREDUCTASE COMPLEX / ELECTRON RELAY / CUBANE CLUSTER / HIGH POTENTIAL / CLUSTER TUNING / ELECTRON TRANSPORT / AS-ISOLATED STATE / AIR-OXIDIZEDFunction / homology Function and homology informationFunction Domain/homology Component
hydrogenase (acceptor) / [Ni-Fe] hydrogenase complex / ferredoxin hydrogenase complex / hydrogenase (acceptor) activity / ferredoxin hydrogenase activity / anaerobic respiration / 3 iron, 4 sulfur cluster binding / nickel cation binding / 4 iron, 4 sulfur cluster binding / electron transfer activity ... hydrogenase (acceptor) / [Ni-Fe] hydrogenase complex / ferredoxin hydrogenase complex / hydrogenase (acceptor) activity / ferredoxin hydrogenase activity / anaerobic respiration / 3 iron, 4 sulfur cluster binding / nickel cation binding / 4 iron, 4 sulfur cluster binding / electron transfer activity / metal ion binding / plasma membrane Similarity search - Function [NiFe]-hydrogenase, small subunit / Cytochrome-c3 hydrogenase, C-terminal / [NiFe]-hydrogenase, small subunit, C-terminal domain superfamily / NiFe/NiFeSe hydrogenase small subunit C-terminal / Nickel-dependent hydrogenases large subunit signature 2. / Nickel-dependent hydrogenases large subunit signature 1. / [NiFe]-hydrogenase, small subunit, N-terminal domain superfamily / Nickel-dependent hydrogenase, large subunit, nickel binding site / Nickel-dependent hydrogenase, large subunit / Nickel-dependent hydrogenase ... [NiFe]-hydrogenase, small subunit / Cytochrome-c3 hydrogenase, C-terminal / [NiFe]-hydrogenase, small subunit, C-terminal domain superfamily / NiFe/NiFeSe hydrogenase small subunit C-terminal / Nickel-dependent hydrogenases large subunit signature 2. / Nickel-dependent hydrogenases large subunit signature 1. / [NiFe]-hydrogenase, small subunit, N-terminal domain superfamily / Nickel-dependent hydrogenase, large subunit, nickel binding site / Nickel-dependent hydrogenase, large subunit / Nickel-dependent hydrogenase / Twin-arginine translocation pathway, signal sequence, bacterial/archaeal / NADH:ubiquinone oxidoreductase-like, 20kDa subunit / NADH ubiquinone oxidoreductase, 20 Kd subunit / [NiFe]-hydrogenase, large subunit / Twin arginine translocation (Tat) signal profile. / Twin-arginine translocation pathway, signal sequence Similarity search - Domain/homology Fe4S4 / FE3-S4 CLUSTER / NI-FE OXIDIZED ACTIVE CENTER / IRON/SULFUR CLUSTER / Uptake hydrogenase large subunit / Uptake hydrogenase small subunit Similarity search - ComponentBiological species Cupriavidus necator H16 (bacteria)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.61 Å DetailsAuthors Kalms, J. / Schmidt, A. / Scheerer, P. Funding support Germany, 2items Details Hide detailsOrganization Grant number Country German Research Foundation (DFG) DFG Cluster of Excellence Unifying Concepts in Catalysis - Research Field D3/E3-1 Germany German Research Foundation (DFG) UniSysCat - Germany Excellence Strategy EXC2008/1-390540038 Germany
CitationJournal : Chem Sci / Year : 2023Title : Stepwise conversion of the Cys 6 [4Fe-3S] to a Cys 4 [4Fe-4S] cluster and its impact on the oxygen tolerance of [NiFe]-hydrogenase.Authors : Schmidt, A. / Kalms, J. / Lorent, C. / Katz, S. / Frielingsdorf, S. / Evans, R.M. / Fritsch, J. / Siebert, E. / Teutloff, C. / Armstrong, F.A. / Zebger, I. / Lenz, O. / Scheerer, P. History Deposition Jul 5, 2023 Deposition site : PDBE / Processing site : PDBERevision 1.0 Nov 15, 2023 Provider : repository / Type : Initial release