[NiFe] Group 1a-hydrogenase

This entry was last updated at: Feb. 9, 2018, 6:58 a.m.

Properties

Group	[NiFe] Group 1: Respiratory H₂-uptake [NiFe] hydrogenases
Subgroup	[NiFe] Group 1a: Periplasmic
Function	Hydrogenotrophic respiration using sulfate, metal, or organohalide compounds as terminal electron acceptors. Enzyme transfers H₂-liberated electrons through cytochrome c₃ to terminal reductase.
Activity	H₂-uptake (unidirectional)
Oxygen tolerance	O₂-sensitive (NiFe variants) or O₂-tolerant (NiFeSe variants)
Localisation	Periplasmic

Distribution

Ecosystem distribution	Anoxic soils and sediments, marine waters, animal gastrointestinal tracts
Taxonomic distribution	Widespread in sulfate-reducing Deltaproteobacteria and Firmicutes

Genetic Organisation

e.g. Desulfovibrio vulgaris (WP_010939204.1):

Architecture

Structures	4KN9 (Desulfomicrobium baculatum, 1.4 Å resolution, active) 4KO1 (Desulfomicrobium baculatum, 1.6 Å resolution, active) 4KO2 (Desulfomicrobium baculatum, 1.6 Å resolution, active) 1CC1 (Desulfomicrobium baculatum, 2.2 Å resolution, active) 4KO3 (Desulfomicrobium baculatum, 1.7 Å resolution, oxidised) 4KO4 (Desulfomicrobium baculatum, 2.0 Å resolution, oxidised) 4KL8 (Desulfomicrobium baculatum, 1.5 Å resolution, oxidised) 3ZEA (Desulfovibrio vulgaris, 1.8 Å resolution, reduced) 3ZE7 (Desulfovibrio vulgaris, 2.0 Å resolution, reduced) 3ZE8 (Desulfovibrio vulgaris, 2.0 Å resolution, reduced) 3ZE9 (Desulfovibrio vulgaris, 1.3 Å resolution, oxidised) 3ZE6 (Desulfovibrio vulgaris, 1.5 Å resolution, oxidised) 2WPN (Desulfovibrio vulgaris, 2.0 Å resolution, oxidised) 5JSK (Desulfovibrio vulgaris, 1.0 Å resolution, reduced) 5JSU (Desulfovibrio vulgaris, 1.4 Å resolution, reduced)
Subunits	3
Subunit description	HysA (hydrogenase large subunit) HysB (hydrogenase small subunit) CycA (cytochrome c₃ subunit)
Catalytic site	[NiFe]-centre or [NiFeSe]-centre
FeS clusters	Proximal: 4Cys[4Fe4S] Medial: 4Cys[4Fe4S] Distal: 3Cys1His[4Fe4S]

Sequences in this class

NCBI Accession	Organism	Hydrogenase Class	Phylum	Order	Activity (Predicted)	Oxygen Tolerance (Predicted)	Subunits (Predicted)	Metal Centres (Predicted)	Accessory Subunits (Predicted)
WP_015262308.1	Desulfitobacterium dichloroeliminans	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_015262676.1	Desulfitobacterium dichloroeliminans	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_015336980.1	Desulfovibrio hydrothermalis	[NiFe] Group 1a	Deltaproteobacteria	Desulfovibrionales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_015394142.1	Clostridium saccharoperbutylacetonicum	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_015407385.1	Dehalococcoides mccartyi	[NiFe] Group 1a	Chloroflexi	Dehalogenimonas	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_015614971.1	Clostridium pasteurianum	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_015739219.1	Ammonifex degensii	[NiFe] Group 1a	Firmicutes	Thermoanaerobacterales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_015739752.1	Ammonifex degensii	[NiFe] Group 1a	Firmicutes	Thermoanaerobacterales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_015774148.1	Desulfomicrobium baculatum	[NiFe] Group 1a	Deltaproteobacteria	Desulfovibrionales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_015851925.1	Desulfovibrio salexigens	[NiFe] Group 1a	Deltaproteobacteria	Desulfovibrionales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_015924586.1	Clostridium cellulolyticum	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_015958012.1	Clostridium botulinum	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_016206881.1	Clostridium sartagoforme	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_017209204.1	Clostridium beijerinckii	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_017379378.1	Paenisporosarcina sp. TG-14	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_017413313.1	Clostridium tunisiense	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_019123746.1	Brevibacillus massiliensis	[NiFe] Group 1a	Firmicutes	Bacillales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_019225238.1	Dehalobacter sp. E1	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_019850824.1	Desulfitobacterium sp. PCE1	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_020001710.1	Desulfovibrio desulfuricans	[NiFe] Group 1a	Deltaproteobacteria	Desulfovibrionales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_020491267.1	Dehalobacter sp. FTH1	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_020589054.1	Desulfobacter curvatus	[NiFe] Group 1a	Deltaproteobacteria	Desulfobacterales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_021169773.1	Sporomusa ovata	[NiFe] Group 1a	Firmicutes	Selenomonadales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_022664892.1	Desulfospira joergensenii	[NiFe] Group 1a	Deltaproteobacteria	Desulfobacterales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_024335307.1	Desulfotignum balticum	[NiFe] Group 1a	Deltaproteobacteria	Desulfobacterales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_024346501.1	Clostridium methoxybenzovorans	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_024363302.1	Lysinibacillus sphaericus	[NiFe] Group 1a	Firmicutes	Bacillales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_025205213.1	Dehalobacter restrictus	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_025219113.1	Lysinibacillus sp. GY32	[NiFe] Group 1a	Firmicutes	Bacillales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_025324287.1	Deferrisoma camini	[NiFe] Group 1a	Deltaproteobacteria	Unclassified	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_025334897.1	Paenibacillus sabinae	[NiFe] Group 1a	Firmicutes	Bacillales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_025690867.1	Paenibacillus zanthoxyli	[NiFe] Group 1a	Firmicutes	Bacillales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_025694942.1	Paenibacillus durus	[NiFe] Group 1a	Firmicutes	Bacillales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_025697751.1	Paenibacillus forsythiae	[NiFe] Group 1a	Firmicutes	Bacillales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_026688533.1	Bacillus aurantiacus	[NiFe] Group 1a	Firmicutes	Bacillales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_027178658.1	Desulfovibrio bastinii	[NiFe] Group 1a	Deltaproteobacteria	Desulfovibrionales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_027185047.1	Desulfovibrio inopinatus	[NiFe] Group 1a	Deltaproteobacteria	Desulfovibrionales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_027360998.1	Desulfovibrio acrylicus	[NiFe] Group 1a	Deltaproteobacteria	Desulfovibrionales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_027365812.1	Desulfotomaculum alcoholivorax	[NiFe] Group 1a	Deltaproteobacteria	Desulfobacterales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_027623849.1	Clostridium lundense	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_027639785.1	Clostridium cadaveris	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_027722757.1	Desulfovibrio zosterae	[NiFe] Group 1a	Deltaproteobacteria	Desulfovibrionales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_028052542.1	Carboxydothermus ferrireducens	[NiFe] Group 1a	Firmicutes	Thermoanaerobacterales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_028573845.1	Desulfonatronovibrio hydrogenovorans	[NiFe] Group 1a	Deltaproteobacteria	Desulfovibrionales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_028575942.1	Desulfomicrobium escambiense	[NiFe] Group 1a	Deltaproteobacteria	Desulfovibrionales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_028784867.1	Thalassobacillus devorans	[NiFe] Group 1a	Firmicutes	Bacillales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_029159252.1	Clostridium scatologenes	[NiFe] Group 1a	Firmicutes	Clostridiales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_029915207.1	Pelobacter seleniigenes	[NiFe] Group 1a	Deltaproteobacteria	Desulfobacterales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome
WP_029968792.1	Desulfonauticus sp. A7A	[NiFe] Group 1a	Deltaproteobacteria	Desulfovibrionales	Anaerobic Uptake	Sensitive	3	[NiFe]-centre, 3 x [4Fe4S] clusters	Cytochrome

Literature

Genetics:

Calusinska, M., Happe, T., Joris, B., and Wilmotte, A. (2010) The surprising diversity of clostridial hydrogenases: a comparative genomic perspective. Microbiol. 156: 1575-1588.
Greening, C., Biswas, A., Carere, C.R., Jackson, C.J., Taylor, M.C., Stott, M.B., Cook, G.M., and Morales, S.E. (2016) Genomic and metagenomic surveys of hydrogenase distribution indicate H₂ is a widely utilised energy source for microbial growth and survival. ISME J. 10: 761-777.
Menon, N.K., Peck, H.D., Gall, J.L., and Przybyla, A.E. (1987) Cloning and sequencing of the genes encoding the large and small subunits of the periplasmic (NiFeSe) hydrogenase of Desulfovibrio baculatus. J. Bacteriol. 169: 5401-5407.
Valente, F.M., Almeida, C.C., Pacheco, I., Carita, J., Saraiva, L.M., and Pereira, I.A., (2006) Selenium is involved in regulation of periplasmic hydrogenase gene expression in Desulfovibrio vulgaris Hildenborough. J. Bacteriol. 188: 3228-3235.
Voordouw, G., Menon, N.K., LeGall, J., Choi, E.S., Peck, H.D., and Przybyla, A.E. (1989) Analysis and comparison of nucleotide sequences encoding the genes for [NiFe] and [NiFeSe] hydrogenases from Desulfovibrio gigas and Desulfovibrio baculatus. J. Bacteriol. 171: 2894-2899.

Biochemistry:

Badziong, W., Thauer, R.K., and Zeikus, J.G. (1978) Isolation and characterization of Desulfovibrio growing on hydrogen plus sulfate as the sole energy source. Arch. Microbiol. 116: 41-49.
Brandis, A. and Thauer, R.K. (1981) Growth of Desulfovibrio species on hydrogen and sulphate as sole energy source. Microbiol. 126: 249-252.
Caffrey, S.M., Park, H.S., Voordouw, J.K., He, Z., Zhou, J., and Voordouw, G. (2007) Function of periplasmic hydrogenases in the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough. J. Bacteriol. 189: 6159-6167.
Chardin, B., Giudici-Orticoni, M.T., De Luca, G., Guigliarelli, B. and Bruschi, M. (2003) Hydrogenases in sulfate-reducing bacteria function as chromium reductase. Appl. Microbiol. Biotechnol. 63: 315-321.
Da Silva, S.M., Venceslau, S.S., Fernandes, C.L., Valente, F.M., and Pereira, I.A,. (2008) Hydrogen as an energy source for the human pathogen Bilophila wadsworthia. Antonie Van Leeuwenhoek 93: 381-390.
Li, X., McInerney, M.J., Stahl, D.A. and Krumholz, L.R. (2011) Metabolism of H₂ by Desulfovibrio alaskensis G20 during syntrophic growth on lactate. Microbiol. 157: 2912-2921.
Holliger, C., Hahn, D., Harmsen, H., Ludwig, W., Schumacher, W., Tindall, B., Vazquez, F., Weiss, N., and Zehnder, A.J. (1998) Dehalobacter restrictus gen. nov. and sp. nov., a strictly anaerobic bacterium that reductively dechlorinates tetra- and trichloroethene in an anaerobic respiration. Arch. Microbiol. 169: 313-321.
Malki, S., De Luca, G., Fardeau, M.L., Rousset, M., Belaich, J.P., and Dermoun, Z. (1997) Physiological characteristics and growth behavior of single and double hydrogenase mutants of Desulfovibrio fructosovorans. Arch. Microbiol. 167: 38-45.
Meyer, B., Kuehl, J.V., Deutschbauer, A.M., Arkin, A.P., and Stahl, D.A. (2013) Flexibility of syntrophic enzyme systems in Desulfovibrio species ensures their adaptation capability to environmental changes. J. Bacteriol. 195: 4900-4914.
Nijenhuis, I. and Zinder, S.H. (2005) Characterization of hydrogenase and reductive dehalogenase activities of Dehalococcoides ethenogenes strain 195. Appl. Environ. Microbiol. 71: 1664-1667.
Rohde, M., Fürstenau, U., Mayer, F., Przybyla, A.E., Peck, H.D., Gall, J., Choi, E.S., and Menon, N.K. (1990) Localization of membrane-associated (NiFe) and (NiFeSe) hydrogenases of Desulfovibrio vulgaris using immunoelectron microscopic procedures. Eur. J. Biochem. 191: 389-396.
Valente, F.M., Pereira, P.M., Venceslau, S.S., Regalla, M., Coelho, A.V., and Pereira, I.A. (2007) The [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough is a bacterial lipoprotein lacking a typical lipoprotein signal peptide. FEBS Lett. 581: 3341-3344.

Biochemistry:

Baltazar, C.S., Marques, M.C., Soares, C.M., DeLacey, A.M., Pereira, I.A., and Matias, P.M. (2011) Nickel-iron-selenium hydrogenases—an overview. Eur. J. Inorg. Chem. 7: 948-962.
Berlier, Y., Fauque, G.D., LeGall, J., Choi, E.S., Peck, H.D. and Lespinat, P.A. (1987) Inhibition studies of three classes of Desulfovibrio hydrogenase: application to the further characterization of the multiple hydrogenases found in Desulfovibrio vulgaris Hildenborough. Biochem. Biophys. Res. Commun. 2011: 147-153.
Eidsness, M.K., Scott, R.A., Prickril, B.C., DerVartanian, D.V., Legall, J., Moura, I., Moura, J.J., and Peck, H.D. (1989) Evidence for selenocysteine coordination to the active site nickel in the [NiFeSe] hydrogenases from Desulfovibrio baculatus. Proc. Natl. Acad. Sci. USA 86: 147-151.
Garcin, E., Vernede, X., Hatchikian, E.C., Volbeda, A., Frey, M., and Fontecilla-Camps, J.C. (1999) The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center. Structure 7: 557-566.
Gutiérrez-Sanz, O., Marques, M.C., Baltazar, C.S., Fernández, V.M., Soares, C.M., Pereira, I.A., and De Lacey, A.L. (2013) Influence of the protein structure surrounding the active site on the catalytic activity of [NiFeSe] hydrogenases. J. Biol. Inorg. Chem. 18: 419-427.
Hartwig, S., Dragomirova, N., Kublik, A., Türkowsky, D., von Bergen, M., Lechner, U., Adrian, L. and Sawers, R.G. (2017) A H₂‐oxidizing, 1, 2, 3‐trichlorobenzene‐reducing multienzyme complex isolated from the obligately organohalide‐respiring bacterium Dehalococcoides mccartyi strain Cbdb1. Environ. Microbiol. Rep. 9: 618-625.
Marques, M.C., Coelho, R., De Lacey, A.L., Pereira, I.A., and Matias, P.M. (2010. The three-dimensional structure of [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough: a hydrogenase without a bridging ligand in the active site in its oxidised, "as-isolated" state. J. Mol. Biol. 396: 893-907.
Marques, M.C., Coelho, R., Pereira, I.A., and Matias, P.M. (2013) Redox state-dependent changes in the crystal structure of [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough. Int. J. Hydrogen Energy 38: 8664-8682.
Marques, M.C., Tapia, C., Gutierrez-Sanz, O., Ramos, A.R., Keller, K.L., Wall, J.D., De Lacey, A.L., Matias, P.M., and Pereira, I.A.C. (2017) The direct role of selenocysteine in [NiFeSe] hydrogenase maturation and catalysis. Nature Chem. Biol. 13: 544-550.
Parkin, A., Goldet, G., Cavazza, C., Fontecilla-Camps, J.C., and Armstrong, F.A. (2008) The difference a Se makes? Oxygen-tolerant hydrogen production by the [NiFeSe]-hydrogenase from Desulfomicrobium baculatum. J. Am. Chem. Soc. 130: 13410-13416.
Teixeira, M., Fauque, G., Moura, I., Lespinat, P.A., Berlier, Y., Prickril, B., Peck, H.D., Xavier, A.V., Gall, J., and Moura, J.J. (1987) Nickel-[iron-sulfur]-selenium-containing hydrogenases from Desulfovibrio baculatus (DSM 1743). Eur. J. Biochem. 167: 47-58.
Valente, F.M., Oliveira, A.S.F., Gnadt, N., Pacheco, I., Coelho, A.V., Xavier, A.V., Teixeira, M., Soares, C.M., and Pereira, I.A. (2005) Hydrogenases in Desulfovibrio vulgaris Hildenborough: structural and physiologic characterisation of the membrane-bound [NiFeSe] hydrogenase. J. Biol. Inorg. Chem. 10: 667-682.
Volbeda, A., Amara, P., Iannello, M., De Lacey, A.L., Cavazza, C. and Fontecilla-Camps, J.C. (2013) Structural foundations for the O₂ resistance of Desulfomicrobium baculatum [NiFeSe]-hydrogenase. Chem. Commun. 49: 7061-7063.

Chemistry:

He, S.H., Teixeira, M., LeGall, J., Patil, D.S., Moura, I., Moura, J.J., DerVartanian, D.V., Huynh, B.H., and Peck, H.D. (1989) EPR studies with ⁷⁷Se-enriched (NiFeSe) hydrogenase of Desulfovibrio baculatus. Evidence for a selenium ligand to the active site nickel. J. Biol. Chem. 264: 2678-2682.
Reisner, E., Fontecilla-Camps, J.C., and Armstrong, F.A. (2009) Catalytic electrochemistry of a [NiFeSe]-hydrogenase on TiO₂ and demonstration of its suitability for visible-light driven H₂ production. Chem. Commun. 5: 550-552.
Riethausen, J., Rödiger, O., Gärtner, W., Lubitz, W., and Shafaat, H.S. (2013) Spectroscopic and electrochemical characterization of the [NiFeSe] hydrogenase from Desulfovibrio vulgaris Miyazaki F: Reversible redox behavior and interactions between electron transfer centers. ChemBioChem 14: 1714-1719.
Stein, M. and Lubitz, W. (2001) The electronic structure of the catalytic intermediate Ni-C in [NiFe] and [NiFeSe] hydrogenases. Phys. Chem. Chem. Phys. 3: 5115-5120.
Wang, C.P., Franco, R., Moura, J.J., Moura, I., and Day, E.P. (1992) The nickel site in active Desulfovibrio baculatus [NiFeSe] hydrogenase is diamagnetic. Multifield saturation magnetization measurement of the spin state of Ni(II). J. Biol. Chem. 267: 7378-7380.