Publications of Seigo Shima
All genres
Journal Article (137)
Journal Article
321 (5888), pp. 572 - 575 (2008)
The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site. Science
Journal Article
47 (10), pp. 3969 - 3977 (2008)
Characterization of the Fe site in iron-sulfur cluster-free hydrogenase (Hmd) and of a model compound via nuclear resonance vibrational spectroscopy (NRVS). Inorganic Chemistry
Journal Article
10 (11), pp. 3164 - 3173 (2008)
Denitrifying bacteria anaerobically oxidize methane in the absence of Archaea. Environmental Microbiology
Journal Article
80 (9), pp. 846 - 849 (2008)
[Structure of [Fe]-hydrogenase and the convergent evolution of the active site of hydrogenases]. Seikagaku
Journal Article
13 (1), pp. 97 - 106 (2008)
The exchange activities of [Fe] hydrogenase (iron-sulfur-cluster-free hydrogenase) from methanogenic archaea in comparison with the exchange activities of [FeFe] and [NiFe] hydrogenases. Journal of Biological Inorganic Chemistry
Journal Article
274, pp. 4913 - 4921 (2007)
Post-translational modifications in the active site region of methyl-coenzyme M reductase from methanogenic and methanotrophic archaea. The FEBS Journal
Journal Article
274, pp. 1588 - 1599 (2007)
Structure of coenzyme F420 H2 oxidase (FprA), a di-iron flavoprotein from methanogenic Archaea catalyzing the reduction of O2 to H2 O. The FEBS Journal
Journal Article
281 (41), pp. 30804 - 30813 (2006)
The Iron-Sulfur Cluster-free Hydrogenase (Hmd) Is a Metalloenzyme with a Novel Iron Binding Motif. Journal of Biological Chemistry
Journal Article
358 (3), pp. 798 - 809 (2006)
The crystal structure of the apoenzyme of the iron-sulphur cluster-free hydrogenase. Journal of Molecular Biology
Journal Article
357, pp. 870 - 879 (2006)
The Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with its Coenzymes. Journal of Molecular Biology
Journal Article
8 (6), pp. 643 - 648 (2005)
Methyl-coenzyme M reductase and the anaerobic oxidation of methane in methanotrophic Archaea. Current Opinion in Microbiology
Journal Article
127 (29), pp. 10430 - 10435 (2005)
Mössbauer studies of the iron-sulfur cluster-free hydrogenase: The electronic state of the mononuclear Fe active site. Journal of the American Chemical Society
Journal Article
14 (7), pp. 1840 - 1849 (2005)
Crystal structure of methylenetetrahydromethanopterin reductase (Mer) in complex with coenzyme F420: Architecture of the F420/FMN binding site of enzymes within the nonprolyl cis-peptide containing bacterial luciferase family. Protein Science
Journal Article
61, pp. 198 - 202 (2005)
The structure of F420-dependent methylenetetrahydromethanopterin dehydrogenase: a crystallographic 'superstructure' of the selenomethionine-labelled protein crystal structure. Acta Crystallographica Section D - Structural Biology
Journal Article
13 (12), pp. 3161 - 3171 (2004)
Structural and functional analysis of the gpsA gene product of Archaeoglobus fulgidus: A glycerol-3-phosphate dehydrogenase with an unusual NADP(+) preference. Protein Science
Journal Article
126 (43), pp. 14239 - 14248 (2004)
Carbon monoxide as an intrinsic ligand to iron in the active site of the iron-sulfur-cluster-free hydrogenase H2-Forming methylenetetrahydromethanopterin dehydrogenase as revealed by infrared spectroscopy. The Journal of Organic Chemistry
Journal Article
182 (2-3), pp. 126 - 137 (2004)
F420H2 oxidase (FprA) from Methanobrevibacter arboriphilus, a coenzyme F420-dependent enzyme involved in O2 detoxification. Archives of Microbiology
Journal Article
12 (3), pp. 361 - 370 (2004)
Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family. Structure
Journal Article
271 (1), pp. 195 - 204 (2004)
UV-A/blue-light inactivation of the 'metal-free' hydrogenase (Hmd) from methanogenic archaea - The enzyme contains functional iron after all. European Journal of Biochemistry
Journal Article
43 (19), pp. 2547 - 2551 (2004)
The cofactor of the iron-sulfur cluster free hydrogenase Hmd: Structure of the light-inactivation product. Angewandte Chemie International Edition