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Goris T, Wait AF, Saggu M, Fritsch J, Heidary N, Stein M, et al. (May 2011). "A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase". Nature Chemical Biology. 7 (5): 310–318. doi:10.1038/nchembio.555. PMID21390036.
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Burgdorf T, Lenz O, Buhrke T, van der Linden E, Jones AK, Albracht SP, et al. (2005). "[NiFe]-hydrogenases of Ralstonia eutropha H16: modular enzymes for oxygen-tolerant biological hydrogen oxidation". Journal of Molecular Microbiology and Biotechnology. 10 (2–4): 181–196. doi:10.1159/000091564. PMID16645314. S2CID8030367.
Madden C, Vaughn MD, Díez-Pérez I, Brown KA, King PW, Gust D, et al. (January 2012). "Catalytic turnover of [FeFe]-hydrogenase based on single-molecule imaging". Journal of the American Chemical Society. 134 (3): 1577–1582. doi:10.1021/ja207461t. PMID21916466.
Glick BR, Martin WG, Martin SM (October 1980). "Purification and properties of the periplasmic hydrogenase from Desulfovibrio desulfuricans". Canadian Journal of Microbiology. 26 (10): 1214–1223. doi:10.1139/m80-203. PMID7006765.
Nakos G, Mortenson L (March 1971). "Purification and properties of hydrogenase, an iron sulfur protein, from Clostridium pasteurianum W5". Biochimica et Biophysica Acta (BBA) - Enzymology. 227 (3): 576–583. doi:10.1016/0005-2744(71)90008-8. PMID5569125.
Chongdar N, Birrell JA, Pawlak K, Sommer C, Reijerse EJ, Rüdiger O, et al. (January 2018). "Unique Spectroscopic Properties of the H-Cluster in a Putative Sensory [FeFe] Hydrogenase". Journal of the American Chemical Society. 140 (3): 1057–1068. doi:10.1021/jacs.7b11287. PMID29251926.
Shima S, Vogt S, Göbels A, Bill E (December 2010). "Iron-chromophore circular dichroism of [Fe]-hydrogenase: the conformational change required for H2 activation". Angewandte Chemie. 49 (51): 9917–9921. doi:10.1002/anie.201006255. PMID21105038.
Lill SO, Siegbahn PE (February 2009). "An autocatalytic mechanism for NiFe-hydrogenase: reduction to Ni(I) followed by oxidative addition". Biochemistry. 48 (5): 1056–1066. doi:10.1021/bi801218n. PMID19138102.
Cao Z, Hall MB (April 2001). "Modeling the active sites in metalloenzymes. 3. Density functional calculations on models for [Fe]-hydrogenase: structures and vibrational frequencies of the observed redox forms and the reaction mechanism at the Diiron Active Center". Journal of the American Chemical Society. 123 (16): 3734–3742. doi:10.1021/ja000116v. PMID11457105.
Vignais PM, Billoud B (October 2007). "Occurrence, classification, and biological function of hydrogenases: an overview". Chemical Reviews. 107 (10): 4206–4272. doi:10.1021/cr050196r. PMID17927159.
Hinnemann B, Moses PG, Bonde J, Jørgensen KP, Nielsen JH, Horch S, et al. (April 2005). "Biomimetic hydrogen evolution: MoS2 nanoparticles as catalyst for hydrogen evolution". Journal of the American Chemical Society. 127 (15): 5308–5309. doi:10.1021/ja0504690. PMID15826154.
Goris T, Wait AF, Saggu M, Fritsch J, Heidary N, Stein M, et al. (May 2011). "A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase". Nature Chemical Biology. 7 (5): 310–318. doi:10.1038/nchembio.555. PMID21390036.
Burgdorf T, Lenz O, Buhrke T, van der Linden E, Jones AK, Albracht SP, et al. (2005). "[NiFe]-hydrogenases of Ralstonia eutropha H16: modular enzymes for oxygen-tolerant biological hydrogen oxidation". Journal of Molecular Microbiology and Biotechnology. 10 (2–4): 181–196. doi:10.1159/000091564. PMID16645314. S2CID8030367.
Land H, Senger M, Berggren G, Stripp ST (2020-05-28). "Current State of [FeFe]-Hydrogenase Research: Biodiversity and Spectroscopic Investigations". ACS Catalysis. 10 (13): 7069–7086. doi:10.1021/acscatal.0c01614. ISSN2155-5435. S2CID219749715.
Land H, Senger M, Berggren G, Stripp ST (2020-05-28). "Current State of [FeFe]-Hydrogenase Research: Biodiversity and Spectroscopic Investigations". ACS Catalysis. 10 (13): 7069–7086. doi:10.1021/acscatal.0c01614. ISSN2155-5435. S2CID219749715.