D. Kastrau

发表

Sequence-specific assignment of the 1H and 15N nuclear magnetic resonance spectra of the reduced recombinant high-potential iron-sulfur protein I from Ectothiorhodospira halophila.

I. Bertini, C. Luchinat, I. Felli, 1994, European journal of biochemistry.

A comparative EPR investigation of the multicopper proteins nitrous-oxide reductase and cytochrome c oxidase.

D. Kastrau, P. Kroneck, W. Zumft, 1992, European journal of biochemistry.

Multifrequency EPR evidence for a bimetallic center at the CuA site in cytochrome c oxidase

D. Kastrau, P. Kroneck, W. Zumft, 1990, FEBS letters.

Nitrite oxidoreductase from Nitrobacter hamburgensis: redox centers and their catalytic role

D. Kastrau, P. Kroneck, E. Bock, 1992, Archives of Microbiology.

The EPR-Detectable Copper of Nitrous Oxide Reductase as a Model for CuA in Cytochrome c Oxidase: A Multifrequency Electron Paramagnetic Resonance Investigation

F. Neese, D. Kastrau, P. Kroneck, 1993 .

Three-dimensional solution structure of the oxidized high potential iron-sulfur protein from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced species.

I. Bertini, C. Luchinat, D. Kastrau, 1995, Biochemistry.

Nitric oxide reductase from Pseudomonas stutzeri, a novel cytochrome bc complex. Phospholipid requirement, electron paramagnetic resonance and redox properties.

D. Kastrau, P. Kroneck, W. Zumft, 1994, European journal of biochemistry.

THE THREE DIMENSIONAL STRUCTURE OF THE PARAMAGNETIC PROTEIN HIPIP I FROM E.HALOPHILA THROUGH NUCLEAR MAGNETIC RESONANCE

I. Bertini, C. Luchinat, I. Felli, 1994 .

The three-dimensional structure in solution of the paramagnetic high-potential iron-sulfur protein I from Ectothiorhodospira halophila through nuclear magnetic resonance.

I. Bertini, C. Luchinat, I. Felli, 1994, European journal of biochemistry.

The Solution Structure of Oxidized HiPIP I from Ectothiorhodospira halophila; Can NMR Spectroscopy Be Used to Probe Rearrangements Associated with Electron Transfer Processes?

I. Bertini, C. Luchinat, I. Felli, 1995 .

Solution structure of Desulfovibrio vulgaris (Hildenborough) ferrocytochrome c3: structural basis for functional cooperativity.

H. Santos, D. Kastrau, D. Turner, 1998, Journal of molecular biology.

The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR.

I. Bertini, C. Luchinat, L. Banci, 1995, Biochemistry.

The solution structure of oxidized HiPIP I from Echtothiorhodospira halophila. Can NMR probe rearrangements associated to electron transfer processes

I. Bertini, C. Luchinat, I. Felli, 1995 .

The copper site in nitrous oxide reductase

D. Kastrau, P. Kroneck, W. Zumft, 1991 .