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Extended X-ray absorption fine structure of the [Fe]-hydrogenase Hmd active site

Marco Salomone-Stagni1, Sonja Vogt2, Seigo Shima2 and Wolfram Meyer-Klaucke1

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[1]
Hiromoto T, Ataka K, Pilak O, Vogt S, Stagni M S, Meyer-Klaucke W, Warkentin E, Thauer R K, Shima S and Ermler U 2009 The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl- iron ligation in the active site iron complex FEBS Lett 583 585-90
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[2]
Fontecilla-Camps J C, Volbeda A, Cavazza C and Nicolet Y 2007 Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases Chem Rev 107 4273-303
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[3]
Shima S and Thauer R K 2007 A third type of hydrogenase catalyzing H2 activation Chem Rec 7 37-46
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[4]
Korbas M, Vogt S, Meyer-Klaucke W, Bill E, Lyon E J, Thauer R K and Shima S 2006 The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motif J Biol Chem 281 30804-13
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[5]
Shima S, Pilak O, Vogt S, Schick M, Stagni M S, Meyer-Klaucke W, Warkentin E, Thauer R K and Ermler U 2008 The Crystal Structure of [Fe]-Hydrogenase reveals the geometry of the Active Site Science 321 572-5
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[6]
Lyon E J, Shima S, Boecher R, Thauer R K, Grevels F W, Bill E, Roseboom W and Albracht S P 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 J Am Chem Soc 126 14239-48
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Löscher S, Zebger I, Andersen L K, Hildebrandt P, Meyer-Klaucke W and Haumann M 2005 The structure of the Ni-Fe site in the isolated HoxC subunit of the hydrogen-sensing hydrogenase from Ralstonia eutropha Febs Lett 579 4287-91
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Buurman G, Shima S and Thauer R K 2000 The metal-free hydrogenase from methanogenic archaea: evidence for a bound cofactor FEBS Lett 485 200-4
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[9]
Korbas M, Marsa D F and Meyer-Klaucke W 2006 KEMP: A program script for automated biological x-ray absorption spectroscopy data reduction Rev Sci Instrum 77 063105
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[10]
Binsted N, Strange R W and Hasnain S S 1992 Constrained and restrained refinement in EXAFS data analysis with curved wave theory Biochemistry 31 12117-25
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Burgdorf T, Löscher S, Liebisch P, Van der Linden E, Galander M, Lendzian F, Meyer-Klaucke W, Albracht SPJ, Friedrich B, Dau H and Haumann M 2005 Structural and oxidation-state changes at its nonstandard Ni-Fe site during activation of the NAD-reducing hydrogenase from Ralstonia eutropha detected by X-ray absorption, EPR, and FTIR spectroscopy J Am Chem Soc 127 576-592
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[12]
Wellenreuther G and Meyer-Klaucke W 2007 Towards a Black-box for Biological EXAFS data analysis - I. Identification of Zinc finger proteins 2007 XAFS13 AIP Conference Proceedings 882 322-324
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