How [Fe]-Hydrogenase from Methanothermobacter is Protected Against Light and Oxidative Stress.

Wagner, Tristan; Huang, Gangfeng; Ermler, Ulrich; Shima, Seigo

Wagner, Tristan; Huang, Gangfeng; Ermler, Ulrich; Shima, Seigo.

Affiliation

Wagner T; Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Straße 10, 35043, Marburg, Germany.
Huang G; Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Straße 10, 35043, Marburg, Germany.
Ermler U; Max-Planck-Institut für Biophysik, Max-von-Laue-Straße 3, 60438, Frankfurt/Main, Germany.
Shima S; Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Straße 10, 35043, Marburg, Germany.

Angew Chem Int Ed Engl ; 57(46): 15056-15059, 2018 11 12.

Article in En | MEDLINE | ID: mdl-30207625

Subject(s)

Hydrogenase/metabolism; Iron-Sulfur Proteins/metabolism; Methanobacteriaceae/enzymology; Oxidative Stress; Binding Sites; Crystallography, X-Ray; Hydrogenase/chemistry; Hydrogenation; Iron-Sulfur Proteins/chemistry; Light; Methanobacteriaceae/chemistry; Methanobacteriaceae/metabolism; Models, Molecular; Protein Conformation; Protein Multimerization; Pterins/metabolism

Key words

FeGP cofactor; [Fe]-hydrogenase; environmental stresses; enzymes; protein structures

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Methanobacteriaceae / Oxidative Stress / Hydrogenase / Iron-Sulfur Proteins Language: En Journal: Angew Chem Int Ed Engl Year: 2018 Document type: Article Affiliation country: Germany Country of publication: Germany

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