Tanja Burgdorf

The open conformation of a Pseudomonas lipase

Joseph D. Schrag, Yunge Li, Mirosław Cygler et al. · Structure · 1997 · 275 citations · Full text

Biochemistry, Structure-function Enzyme Kinetics, Open Conformation +4

The Soluble NAD⁺-Reducing [NiFe]-Hydrogenase from<i>Ralstonia eutropha</i>H16 Consists of Six Subunits and Can Be Specifically Activated by NADPH

Tanja Burgdorf, Eddy van der Linden, Michael Bernhard et al. · Journal of Bacteriology · 2005 · 118 citations · Full text

Structural and Oxidation-State Changes at Its Nonstandard Ni−Fe Site during Activation of the NAD-Reducing Hydrogenase from <i>Ralstonia</i> <i>eutropha</i> Detected by X-ray Absorption, EPR, and FTIR Spectroscopy

Tanja Burgdorf, Simone Löscher, Peter Liebisch et al. · Journal of the American Chemical Society · 2004 · 74 citations

Engineering, Molecular Biology, Chemistry +16

The soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygen

Eddy van der Linden, Tanja Burgdorf, Michael Bernhard et al. · JBIC Journal of Biological Inorganic Chemistry · 2004 · 67 citations

Ralstonia Eutropha, Biochemistry, Reactive Nitrogen Specie +11

Selective release and function of one of the two FMN groups in the cytoplasmic NAD⁺‐reducing [NiFe]‐hydrogenase from <i>Ralstonia eutropha</i>

Eddy van der Linden, Bart W. Faber, Boris Bleijlevens et al. · European Journal of Biochemistry · 2004 · 47 citations · Full text

Molecular Biology, Hoxfu Dimer, Chemical Biology +16