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Hydrogenases oxygen-tolerant

Burgdorf T, Lenz O, Buhrke T, van der Linden E, Jones AK, Albracht SPJ, Friedrich B. 2005. [NiFe]-hydrogenases of Rahtonia eutropha H16 Modular enzymes for oxygen-tolerant biological hydrogen oxidation. J Mol Microbiol Biotechnol 10 181-196. [Pg.630]

Bleijlevens B, Buhrke T, van der Linden E, Friedrich B, Albracht SPJ (2004) The auxiliary protein HypX provides oxygen tolerance to the soluble [NiFe]-hydrogenase of Ralstonia eutropha H16 by way of a cyanide ligand to nickel. J Biol Chem 279 46686-46691... [Pg.154]

Several crystal structures of [NiFe] hydrogenases have been determined from sulfate-reducing and photosynthetic bacteria [8, 84, 85], and recently also from oxygen-tolerant species [9, 10]. Two structures from the subclass [NiFeSe] hydrogenase are known [86-88] and from two [FeFe] hydrogenases [8, 89, 90],... [Pg.200]

Fritsch F, Scheerer P, Frielingsdorf S, et al. The crystal structure of an oxygen-tolerant hydrogenase unvocers a novel iron-sulphur centre. Nature. 2011 479(7372) 249-52. [Pg.215]

Shomura Y, Yoon KS, Nishihara H, Higuchi Y. Structural basis for [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe] hydrogenase. Nature. 2011 479(7372) 253-7. [Pg.215]

Pandelia ME, Nitschke W, Infossi P, Giudici-Orticoni MT, Bill E, Lubitz W. Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus. Proc Nat Acad Sci USA. 2011 108(15) 6097—102. [Pg.220]

Goris T, Wait AF, Saggu M, et al. A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase. Nat Chem Biol. 2011 7(5) 310—8. [Pg.220]

Lukey MJ, Roessler MM, Parkin A, et al. Oxygen-tolerant [NiFe]-hydrogenases the individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster. J Am Chem Soc. 2011 133(42) 16881-92. [Pg.220]

Buhrke T, Lenz O, Krauss N, Friedrich B. Oxygen tolerance of the H2-sensing [NiFe] hydrogenase from Ralstonia eutropha HI6 is based on limited access of oxygen to the active site. J Biol Chem. 2005 280(25) 23791-6. [Pg.222]

Pandelia ME, Fourmond V, Tron-Infossi P, et al. Membrane-bound hydrogenase I from the hyperthermophilic bacterium Aquifex aeolicus enzyme activation, redox intermediates and oxygen tolerance. J Am Chem Soc. 2010 132(20) 6991-7004. [Pg.222]

Maness, P. C., Smolinski, S., Dillon, A. C., Heben, M. J., and Weaver, P. F. 2002. Characterization of the oxygen tolerance of a hydrogenase linked to a carbon monoxide oxidation pathway in Rubrivivax gelatinosus. Appl. Environ. Microbiol. 68, 2633-2636. [Pg.263]

J.R., Ludwig, M., Lenz, O., Friedrich, B., and Armstrong, F.A. (2006) Electricity from low-level H2 in still air-an ultimate test for an oxygen tolerant hydrogenase. Chemical Communications, 48, 5033-5035. [Pg.68]

M.J., and Weaver, P.F. "Characterization of the Oxygen Tolerance of a Hydrogenase Linked to a Carbon-Monoxide Oxidation Pathway in Rubrivivax gelatinosusApplied and Environmental Microbiology, 68 2633-2636 (2002). [Pg.26]

Fig. 4 Structures of the (a) [4Fe3S] proximal cluster found in oxygen-tolerant [NiFe]-hydrogenases and (b) [4Fe4S] proximal cluster found in oxygen-sensitive [NiFe]-hydrogenases. Reprinted with permission from Macmillan Publishers Ltd Nature 479(7372) 249-252, copyright 2011... Fig. 4 Structures of the (a) [4Fe3S] proximal cluster found in oxygen-tolerant [NiFe]-hydrogenases and (b) [4Fe4S] proximal cluster found in oxygen-sensitive [NiFe]-hydrogenases. Reprinted with permission from Macmillan Publishers Ltd Nature 479(7372) 249-252, copyright 2011...
Wait, A.F., Parkin, A., Morley, G.M., dos Santos, L., Armstrong, F.A. Characteristics of enzyme-based hydrogen fuel cells using an oxygen-tolerant hydrogenase as the anodic catalyst. J. Phys. Chem. C 114(27), 12003-12009 (2010). doi 10.1021/jpl02616m... [Pg.64]


See other pages where Hydrogenases oxygen-tolerant is mentioned: [Pg.96]    [Pg.114]    [Pg.172]    [Pg.239]    [Pg.202]    [Pg.202]    [Pg.209]    [Pg.209]    [Pg.210]    [Pg.211]    [Pg.66]    [Pg.123]    [Pg.126]    [Pg.54]    [Pg.96]    [Pg.97]    [Pg.97]    [Pg.239]    [Pg.287]    [Pg.1164]    [Pg.280]    [Pg.232]    [Pg.233]   
See also in sourсe #XX -- [ Pg.84 , Pg.89 ]




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