D. Scheide

发表

A Novel, Enzymatically Active Conformation of theEscherichia coli NADH:Ubiquinone Oxidoreductase (Complex I)*

B. Böttcher, T. Friedrich, L. Nagel-Steger, 2002, The Journal of Biological Chemistry.

Identification of two tetranuclear FeS clusters on the ferredoxin-type subunit of NADH:ubiquinone oxidoreductase (complex I).

B. Brors, T. Rasmussen, T. Friedrich, 2001, Biochemistry.

Zika virus diagnostik

M. Kintrup, D. Scheide, Lilly Kronsteiner, 2017 .

The Ubiquinone-binding Site in NADH:Ubiquinone Oxidoreductase from Escherichia coli*

X. Gong, T. Friedrich, Chang-an Yu, 2003, Journal of Biological Chemistry.

The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane‐bound multisubunit hydrogenases

T. Friedrich, D. Scheide, 2000, FEBS letters.

Characterization of two novel redox groups in the respiratory NADH:ubiquinone oxidoreductase (complex I).

B. Brors, W. Mäntele, U. Schulte, 2000, Biochimica et biophysica acta.

The proton‐pumping NADH:ubiquinone oxidoreductase (complex I) of Aquifex aeolicus

R. Huber, T. Friedrich, D. Scheide, 2002, FEBS letters.

Redox components and structure of the respiratory NADH:ubiquinone oxidoreductase (complex I).

B. Brors, U. Schulte, K. Leonard, 1998, Biochimica et biophysica acta.

FT-IR spectroscopic characterization of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli: oxidation of FeS cluster N2 is coupled with the protonation of an aspartate or glutamate side chain.

W. Mäntele, T. Friedrich, P. Hellwig, 2000, Biochemistry.