2011, ISBN: 9783838128009

This work elaborates on the molecular background of oxygen sensitivity in FeFe] hydrogenases. Hydrogenases are iron-sulphur proteins that catalyse hydrogen turnover in micro organisms. Fe… Mehr…

This work elaborates on the molecular background of oxygen sensitivity in FeFe] hydrogenases. Hydrogenases are iron-sulphur proteins that catalyse hydrogen turnover in micro organisms. FeFe] hydrogenases in particular are high-efficiency catalysts for hydrogen evolution but irreversibly inactivated by oxygen. Their unique 4Fe-4S]- 2Fe-2S] cofactor is referred to as "H-cluster." Three different FeFe] hydrogenases were analysed by electrochemistry. These were the bacterial hydrogenases CaHydA and DdH as well as CrHydA1 of Chlamydomonas reinhardtii, a unicellular green alga. The effects of oxygen and carbonmonoxide (CO) were probed, the latter of which reversibly inhibits hydrogenases. DdH is inactivated by oxygen ten times more rapid than CrHydA1 and three orders of magnitude faster than CaHydA. The same correlation was found for CO inhibition, although reactivation is in the same range for all three enzymes. Moreover, CO was shown to prevent the H-cluster from oxygen damage. Given that CO can not bind the 4Fe-4S] part of the cofactor, the capability of CO to protect the entire H-cluster proves that oxygen attacks the 2Fe-2S] site exclusively, too. This work elaborates on the molecular background of oxygen sensitivity in FeFe] hydrogenases. Hydrogenases are iron-sulphur proteins that catalyse hydrogen turnover in micro organisms. FeFe] hydrogenases in particular are high-efficiency catalysts for hydrogen evolution but irreversibly inactivated by oxygen. Their unique 4Fe-4S]- 2Fe-2S] cofactor is referred to as "H-cluster." Three different FeFe] hydrogenases were analysed by electrochemistry. These were the bacterial hydrogenases CaHydA and DdH as well as CrHydA1 of Chlamydomonas reinhardtii, a unicellular green alga. The effects of oxygen and carbonmonoxide (CO) were probed, the latter of which reversibly inhibits hydrogenases. DdH is inactivated by oxygen ten times more rapid than CrHydA1 and three orders of magnitude faster than CaHydA. The same correlation was found for CO inhibition, although reactivation is in the same range for all three enzymes. Moreover, CO was shown to prevent the H-cluster from oxygen damage. Given that CO can not bind the 4Fe-4S] part of the cofactor, the capability of CO to protect the entire H-cluster proves that oxygen attacks the 2Fe-2S] site exclusively, too. Inhoud: Taal: Engels; Bindwijze: Paperback; Verschijningsdatum: oktober 2011; Aantal pagina's: 104 pagina's; Illustraties: Nee; Betrokkenen: Auteur(s): Stripp Sven T; Uitgever: Sudwestdeutscher Verlag Fur Hochschulschriften AG; EAN: Overige kenmerken: Extra groot lettertype: Nee; Gewicht: 163 g; Studieboek: Ja; Verpakking breedte: 152 mm; Verpakking hoogte: 229 mm; Verpakking lengte: 229 mm; Engels | Paperback | 9783838128009 | 104 pagina's, Boeken, Wetenschap & Natuur, Biologie, Sudwestdeutscher Verlag Fur Hochschulschriften AG<

ISBN: 9783838128009

This work elaborates on the molecular background of oxygen sensitivity in [FeFe] hydrogenases. Hydrogenases are iron-sulphur proteins that catalyse hydrogen turnover in micro organisms. [… Mehr…

This work elaborates on the molecular background of oxygen sensitivity in [FeFe] hydrogenases. Hydrogenases are iron-sulphur proteins that catalyse hydrogen turnover in micro organisms. [FeFe] hydrogenases in particular are high-efficiency catalysts for hydrogen evolution but irreversibly inactivated by oxygen. Their unique [4Fe-4S]-[2Fe-2S] cofactor is referred to as H-cluster. Three different [FeFe] hydrogenases were analysed by electrochemistry. These were the bacterial hydrogenases CaHydA and DdH as well as CrHydA1 of Chlamydomonas reinhardtii, a unicellular green alga. The effects of oxygen and carbonmonoxide (CO) were probed, the latter of which reversibly inhibits hydrogenases. DdH is inactivated by oxygen ten times more rapid than CrHydA1 and three orders of magnitude faster than CaHydA. The same correlation was found for CO inhibition, although reactivation is in the same range for all three enzymes. Moreover, CO was shown to prevent the H-cluster from oxygen damage. Given that CO can not bind the [4Fe-4S] part of the cofactor, the capability of CO to protect the entire H-cluster proves that oxygen attacks the [2Fe-2S] site exclusively, too. Trade Books>Trade Paperback>Science>Biology>Biology, Südwestdeutscher Verlag für Hochschulschriften Core >1<

ISBN: 9783838128009

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*Molecular Background of Oxygen Sensitivity in [FeFe] hydrogenases* - Benefits and Challenges in Enzymatic Hydrogen Production / Taschenbuch für 53.99 € / Aus dem Bereich: Bücher, Taschen… Mehr…

*Molecular Background of Oxygen Sensitivity in [FeFe] hydrogenases* - Benefits and Challenges in Enzymatic Hydrogen Production / Taschenbuch für 53.99 € / Aus dem Bereich: Bücher, Taschenbücher, Naturwissenschaft Medien > Bücher nein Taschenbuch Hardcover;Naturwissenschaften, Medizin, Informatik, Technik;Biochemie, Biophysik, Südwestdeutscher Verlag für Hochschulschriften<

2011, ISBN: 3838128001

Kartoniert / Broschiert, mit Schutzumschlag 11, [PU:Südwestdeutscher Verlag für Hochschulschriften]