S P Albracht - JoVE Visualize

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European Journal of Biochemistry|December 1, 1987

On the anomalous temperature behaviour of the EPR signal of monovalent nickel in hydrogenaseJ W Van der Zwaan, S P Albracht, R D Fontijn, et al.

Biochimica Et Biophysica Acta|June 1, 1990

New evidence for the dimeric nature of NADH:Q oxidoreductase in bovine-heart submitochondrial particlesR van Belzen, M C van Gaalen, P A Cuypers, et al.

European Journal of Biochemistry|August 15, 1994

A second terminal oxidase in Sulfolobus acidocaldariusM Lübben, S Arnaud, J Castresana, et al.

Biochimica Et Biophysica Acta|January 15, 1981

Purification and some properties of the soluble hydrogenase from Chromatium vinosumH van Heerikhuizen, S P Albracht, E C Slater, et al.

Journal of Bacteriology|March 1, 1993

Abundance, subunit composition, redox properties, and catalytic activity of the cytochrome bc1 complex from alkaliphilic and halophilic, photosynthetic members of the family EctothiorhodospiraceaeT Leguijt, P W Engels, W Crielaard, et al.

Biochimica Et Biophysica Acta|November 15, 1990

Effect of 17O2 and 13CO on EPR spectra of nickel in hydrogenase from Chromatium vinosumJ W van der Zwaan, J M Coremans, E C Bouwens, et al.

FEBS Letters|January 7, 1985

Monovalent nickel in hydrogenase from Chromatium vinosum. Light sensitivity and evidence for direct interaction with hydrogenJ W van der Zwaan, S P Albracht, R D Fontijn, et al.

Biochemistry|January 28, 1997

The iron-sulfur clusters 2 and ubisemiquinone radicals of NADH:ubiquinone oxidoreductase are involved in energy coupling in submitochondrial particlesR van Belzen, A B Kotlyar, N Moon, et al.

Biochemistry|April 25, 1995

Infrared-detectable groups sense changes in charge density on the nickel center in hydrogenase from Chromatium vinosumK A Bagley, E C Duin, W Roseboom, et al.

Biochemistry|November 24, 1992

Resolution of NADH:ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzymeM Finel, J M Skehel, S P Albracht, et al.

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Showing results (51-60 of 78) with videos related to

Sort By:

Pageof 8

European Journal of Biochemistry|December 1, 1987

On the anomalous temperature behaviour of the EPR signal of monovalent nickel in hydrogenaseJ W Van der Zwaan, S P Albracht, R D Fontijn, et al.

Biochimica Et Biophysica Acta|June 1, 1990

New evidence for the dimeric nature of NADH:Q oxidoreductase in bovine-heart submitochondrial particlesR van Belzen, M C van Gaalen, P A Cuypers, et al.

European Journal of Biochemistry|August 15, 1994

A second terminal oxidase in Sulfolobus acidocaldariusM Lübben, S Arnaud, J Castresana, et al.

Biochimica Et Biophysica Acta|January 15, 1981

Purification and some properties of the soluble hydrogenase from Chromatium vinosumH van Heerikhuizen, S P Albracht, E C Slater, et al.

Journal of Bacteriology|March 1, 1993

Abundance, subunit composition, redox properties, and catalytic activity of the cytochrome bc1 complex from alkaliphilic and halophilic, photosynthetic members of the family EctothiorhodospiraceaeT Leguijt, P W Engels, W Crielaard, et al.

Biochimica Et Biophysica Acta|November 15, 1990

Effect of 17O2 and 13CO on EPR spectra of nickel in hydrogenase from Chromatium vinosumJ W van der Zwaan, J M Coremans, E C Bouwens, et al.

FEBS Letters|January 7, 1985

Monovalent nickel in hydrogenase from Chromatium vinosum. Light sensitivity and evidence for direct interaction with hydrogenJ W van der Zwaan, S P Albracht, R D Fontijn, et al.

Biochemistry|January 28, 1997

The iron-sulfur clusters 2 and ubisemiquinone radicals of NADH:ubiquinone oxidoreductase are involved in energy coupling in submitochondrial particlesR van Belzen, A B Kotlyar, N Moon, et al.

Biochemistry|April 25, 1995

Infrared-detectable groups sense changes in charge density on the nickel center in hydrogenase from Chromatium vinosumK A Bagley, E C Duin, W Roseboom, et al.

Biochemistry|November 24, 1992

Resolution of NADH:ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzymeM Finel, J M Skehel, S P Albracht, et al.

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