Zobrazeno 1 - 10
of 13
pro vyhledávání: '"MESH: Hydrogenase"'
Autor:
Carole Baffert, Ugo Cosentino, Christophe Léger, Toshiko Miyake, Vincent Fourmond, Giorgio Moro, Maurizio Bruschi, Luca De Gioia, Claudio Greco
Publikováno v:
European Journal of Biochemistry
European Journal of Biochemistry, 2013, 18 (6), pp.693-700. ⟨10.1007/s00775-013-1014-4⟩
European Journal of Biochemistry, Wiley, 2013, 18 (6), pp.693-700. ⟨10.1007/s00775-013-1014-4⟩
European Journal of Biochemistry, 2013, 18 (6), pp.693-700. ⟨10.1007/s00775-013-1014-4⟩
European Journal of Biochemistry, Wiley, 2013, 18 (6), pp.693-700. ⟨10.1007/s00775-013-1014-4⟩
International audience; [FeFe] hydrogenases are H2-evolving enzymes that feature a diiron cluster in their active site (the [2Fe]H cluster). One of the iron atoms has a vacant coordination site that directly interacts with H2, thus favoring its split
Autor:
Matthew C. Taylor, Michael Berney, Ralf Conrad, Chris Greening, Robyn J. Russell, Gregory M. Cook, Kiel Hards, Philippe Constant, John G. Oakeshott, Sergio E. Morales
Publikováno v:
Applied and Environmental Microbiology
Applied and Environmental Microbiology, American Society for Microbiology, 2015, 81 (4), pp.1190-9. ⟨10.1128/AEM.03364-14⟩
Applied and Environmental Microbiology, American Society for Microbiology, 2015, 81 (4), pp.1190-9. ⟨10.1128/AEM.03364-14⟩
We have known for 40 years that soils can consume the trace amounts of molecular hydrogen (H 2 ) found in the Earth's atmosphere. This process is predicted to be the most significant term in the global hydrogen cycle. However, the organisms and enzym
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7eb6985c1c7aa9fda08a46a3bdcd973
https://hal-riip.archives-ouvertes.fr/pasteur-01352155
https://hal-riip.archives-ouvertes.fr/pasteur-01352155
Autor:
Yatendra S. Chaudhary, Vincent Wang, Thomas W. Woolerton, Sophie Bell, Stephen W. Ragsdale, Juan C. Fontecilla-Camps, Mehmet Can, Andreas Bachmeier, Fraser A. Armstrong
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, 2013, 135 (40), pp.15026-15032. ⟨10.1021/ja4042675⟩
Journal of the American Chemical Society, American Chemical Society, 2013, 135 (40), pp.15026-15032. ⟨10.1021/ja4042675⟩
Journal of the American Chemical Society, 2013, 135 (40), pp.15026-15032. ⟨10.1021/ja4042675⟩
Journal of the American Chemical Society, American Chemical Society, 2013, 135 (40), pp.15026-15032. ⟨10.1021/ja4042675⟩
International audience; The most efficient catalysts for solar fuel production should operate close to reversible potentials, yet possess a bias for the fuel-forming direction. Protein film electrochemical studies of Ni-containing carbon monoxide deh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7664302acac5ec523caa31078768809d
https://hal.science/hal-01664648
https://hal.science/hal-01664648
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, 2013, 110 (28), pp.E2538-E2538. ⟨10.1073/pnas.1302304110⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2013, 110 (28), pp.E2538-E2538. ⟨10.1073/pnas.1302304110⟩
Proceedings of the National Academy of Sciences of the United States of America, 2013, 110 (28), pp.E2538-E2538. ⟨10.1073/pnas.1302304110⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2013, 110 (28), pp.E2538-E2538. ⟨10.1073/pnas.1302304110⟩
Recently, Pandelia et al. (1) used density functional theory (DFT) calculations to interpret their Mossbauer experiments on the superoxidized state of the O2-tolerant hydrogenase [4Fe3S] proximal cluster. Experimentally (table 2 in ref. 1), the subsp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70b5bdbdb2f9366b741895314491f807
https://hal.science/hal-01664837
https://hal.science/hal-01664837
Publikováno v:
Angewandte Chemie International Edition
Angewandte Chemie International Edition, 2013, 52 (7), pp.2002-2006. ⟨10.1002/anie.201209063⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2013, 52 (7), pp.2002-2006. ⟨10.1002/anie.201209063⟩
Angewandte Chemie International Edition, 2013, 52 (7), pp.2002-2006. ⟨10.1002/anie.201209063⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2013, 52 (7), pp.2002-2006. ⟨10.1002/anie.201209063⟩
International audience
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7830ceb49d7a5fd426b45fa8865906d1
https://hal.science/hal-01664841
https://hal.science/hal-01664841
Autor:
Bonnie J. Murphy, Fraser A. Armstrong, Maxie M. Roessler, Juan C. Fontecilla-Camps, Alison Parkin, Rhiannon M. Evans, Anne Volbeda, Hope Adamson, Frank Sargent, Michael J. Lukey
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, 2013, 135 (7), pp.2694-2707. ⟨10.1021/ja311055d⟩
Journal of the American Chemical Society, American Chemical Society, 2013, 135 (7), pp.2694-2707. ⟨10.1021/ja311055d⟩
Journal of the American Chemical Society, 2013, 135 (7), pp.2694-2707. ⟨10.1021/ja311055d⟩
Journal of the American Chemical Society, American Chemical Society, 2013, 135 (7), pp.2694-2707. ⟨10.1021/ja311055d⟩
International audience; "Hyd-1", produced by Escherichia coli , exemplifies a special class of [NiFe]-hydrogenase that can sustain high catalytic H(2) oxidation activity in the presence of O(2)-an intruder that normally incapacitates the sulfur- and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a9369d18a2de02194fdca56665cbdd6
https://hal.science/hal-01664819
https://hal.science/hal-01664819
Autor:
Anne Volbeda, Juan C. Fontecilla-Camps, Marina Iannello, Antonio L. De Lacey, Patricia Amara, Christine Cavazza
Publikováno v:
Chemical Communications
Chemical Communications, Royal Society of Chemistry, 2013, 49 (63), pp.7061-3. ⟨10.1039/c3cc43619e⟩
Digital.CSIC. Repositorio Institucional del CSIC
instname
Chemical Communications, 2013, 49 (63), pp.7061-3. ⟨10.1039/c3cc43619e⟩
Chemical Communications, Royal Society of Chemistry, 2013, 49 (63), pp.7061-3. ⟨10.1039/c3cc43619e⟩
Digital.CSIC. Repositorio Institucional del CSIC
instname
Chemical Communications, 2013, 49 (63), pp.7061-3. ⟨10.1039/c3cc43619e⟩
This study shows how the NiFeSe site of an anaerobically purified O2-resistant hydrogenase reacts with air to give a seleninate as the first product. Less oxidized states of the active site are readily reduced in the presence of X-rays. Reductive enz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b20f9b5faba40efda4b74c676bb74187
http://hdl.handle.net/10261/183008
http://hdl.handle.net/10261/183008
Autor:
Sébastien Dementin, Abbas Abou Hamdan, Patrick Bertrand, Laurent Cournac, Pierre Richaud, Christophe Léger, Marc Rousset, Pierre-Pol Liebgott, Antonio L. De Lacey, Óscar Gutiérrez-Sanz
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, 2012, 134 (20), pp.8368-8371. ⟨10.1021/ja301802r⟩
Journal of the American Chemical Society, American Chemical Society, 2012, 134 (20), pp.8368-71. ⟨10.1021/ja301802r⟩
Journal of the American Chemical Society, American Chemical Society, 2012, 134 (20), pp.8368-8371. ⟨10.1021/ja301802r⟩
Journal of the American Chemical Society, 2012, 134 (20), pp.8368-71. ⟨10.1021/ja301802r⟩
Journal of the American Chemical Society, 2012, 134 (20), pp.8368-8371. ⟨10.1021/ja301802r⟩
Journal of the American Chemical Society, American Chemical Society, 2012, 134 (20), pp.8368-71. ⟨10.1021/ja301802r⟩
Journal of the American Chemical Society, American Chemical Society, 2012, 134 (20), pp.8368-8371. ⟨10.1021/ja301802r⟩
Journal of the American Chemical Society, 2012, 134 (20), pp.8368-71. ⟨10.1021/ja301802r⟩
International audience; When enzymes are optimized for biotechnological purposes, the goal often is to increase stability or catalytic efficiency. However, many enzymes reversibly convert their substrate and product, and if one is interested in catal
Autor:
Catherine Texier, Patrick Wincker, Christian P. Vivarès, Kevin S. W. Tan, Frédéric Delbac, Marie Diogon, Michaël Roussel, Ivan Wawrzyniak, Arnaud Couloux, Hicham El Alaoui
Publikováno v:
International Journal for Parasitology
International Journal for Parasitology, 2008, 38 (12), pp.1377-1382. ⟨10.1016/j.ijpara.2008.06.001⟩
International Journal for Parasitology, Elsevier, 2008, 38 (12), pp.1377-1382. ⟨10.1016/j.ijpara.2008.06.001⟩
International Journal for Parasitology, 2008, 38 (12), pp.1377-1382. ⟨10.1016/j.ijpara.2008.06.001⟩
International Journal for Parasitology, Elsevier, 2008, 38 (12), pp.1377-1382. ⟨10.1016/j.ijpara.2008.06.001⟩
International audience; Blastocystis hominis is an anaerobic parasite of the human intestinal tract belonging to the Stramenopile group. Using genome sequencing project data, we describe here the complete sequence of a 29,270-bp circular DNA molecule
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fb4b21bee9a0bfe821af4e2216a4a3e
https://hal.science/hal-00527813
https://hal.science/hal-00527813
Publikováno v:
International Journal for Parasitology
International Journal for Parasitology, Elsevier, 2008, 38 (2), pp.177-90. ⟨10.1016/j.ijpara.2007.06.006⟩
International Journal for Parasitology, 2008, 38 (2), pp.177-90. ⟨10.1016/j.ijpara.2007.06.006⟩
International Journal for Parasitology, Elsevier, 2008, 38 (2), pp.177-90. ⟨10.1016/j.ijpara.2007.06.006⟩
International Journal for Parasitology, 2008, 38 (2), pp.177-90. ⟨10.1016/j.ijpara.2007.06.006⟩
International audience; Histomonas meleagridis is a trichomonad species that undergoes a flagellate-to-amoeba transformation during tissue invasion and causes a serious disease in gallinaceous birds (blackhead disease or histomoniasis). Living in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d83346da49aecc738b98bee05fc10a85
https://hal.archives-ouvertes.fr/hal-00527816
https://hal.archives-ouvertes.fr/hal-00527816