(Q28255729)

1

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Sonja Vogt

2

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Wolfram Meyer-Klaucke

3

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Erica J Lyon

5

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Rudolf K Thauer

6

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Seigo Shima

Journal of Biological Chemistry

7

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language of work or name

English

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publication date

13 October 2006

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published in

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volume

281

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issue

41

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page(s)

30804-13

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cites work

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Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center

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Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans.

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Hydrogenases: hydrogen-activating enzymes

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Enzymatic mechanism of Fe-only hydrogenase: density functional study on H-H making/breaking at the diiron cluster with concerted proton and electron transfers

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Fe-only hydrogenases: structure, function and evolution.

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Hydrogenases: active site puzzles and progress

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H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum. Studies of the catalytic mechanism of H2 formation using hydrogen isotopes.

21 January 2018

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UV-A/blue-light inactivation of the 'metal-free' hydrogenase (Hmd) from methanogenic archaea

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The cofactor of the iron-sulfur cluster free hydrogenase hmd: structure of the light-inactivation product

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Tetrahydromethanopterin-specific enzymes from Methanopyrus kandleri

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Overcoming inclusion body formation in a high-level expression system.

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Activation of dihydrogen without transition metals

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N5,N10-Methylenetetrahydromethanopterin dehydrogenase fromMethanobacterium thermoautotrophicumhas hydrogenase activity

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