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FEBS Letters
|
December 2, 1999
Pyrococcus furiosus glyceraldehyde 3-phosphate oxidoreductase has comparable W(6+/5+) and W(5+/4+) reduction potentials and unusual [4Fe-4S] EPR properties
P L Hagedoorn, J R Freije, W R Hagen
FEBS Letters
|
November 6, 2002
Pyrococcus furiosus ferredoxin is a functional dimer
M N Hasan, P L Hagedoorn, W R Hagen
Analytical Biochemistry
|
September 25, 2001
Electroanalytical determination of tungsten and molybdenum in proteins
P L Hagedoorn, P van't Slot, H P van Leeuwen, et al.
Biochemical Society Transactions
|
January 26, 2005
On the relationship between affinity for molecular hydrogen and the physiological directionality of hydrogenases
D J van Haaster, P-L Hagedoorn, J A Jongejan, et al.
FEBS Letters
|
January 1, 1999
Hyperthermophilic redox chemistry: a re-evaluation
P L Hagedoorn, M C Driessen, M van den Bosch, et al.
The Journal of Biological Chemistry
|
April 13, 2001
The effect of substrate, dihydrobiopterin, and dopamine on the EPR spectroscopic properties and the midpoint potential of the catalytic iron in recombinant human phenylalanine hydroxylase
P L Hagedoorn, P P Schmidt, K K Andersson, et al.
Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|
September 1, 2000
Novel structure and redox chemistry of the prosthetic groups of the iron-sulfur flavoprotein sulfide dehydrogenase from Pyrococcus furiosus; evidence for a [2Fe-2S] cluster with Asp(Cys)3 ligands
W R Hagen, P J Silva, M A Amorim, et al.
Page
of 1
Search research articles
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Showing results (1-10 of 7) with videos related to
Sort By:
Page
of 1
FEBS Letters
|
December 2, 1999
Pyrococcus furiosus glyceraldehyde 3-phosphate oxidoreductase has comparable W(6+/5+) and W(5+/4+) reduction potentials and unusual [4Fe-4S] EPR properties
P L Hagedoorn, J R Freije, W R Hagen
FEBS Letters
|
November 6, 2002
Pyrococcus furiosus ferredoxin is a functional dimer
M N Hasan, P L Hagedoorn, W R Hagen
Analytical Biochemistry
|
September 25, 2001
Electroanalytical determination of tungsten and molybdenum in proteins
P L Hagedoorn, P van't Slot, H P van Leeuwen, et al.
Biochemical Society Transactions
|
January 26, 2005
On the relationship between affinity for molecular hydrogen and the physiological directionality of hydrogenases
D J van Haaster, P-L Hagedoorn, J A Jongejan, et al.
FEBS Letters
|
January 1, 1999
Hyperthermophilic redox chemistry: a re-evaluation
P L Hagedoorn, M C Driessen, M van den Bosch, et al.
The Journal of Biological Chemistry
|
April 13, 2001
The effect of substrate, dihydrobiopterin, and dopamine on the EPR spectroscopic properties and the midpoint potential of the catalytic iron in recombinant human phenylalanine hydroxylase
P L Hagedoorn, P P Schmidt, K K Andersson, et al.
Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|
September 1, 2000
Novel structure and redox chemistry of the prosthetic groups of the iron-sulfur flavoprotein sulfide dehydrogenase from Pyrococcus furiosus; evidence for a [2Fe-2S] cluster with Asp(Cys)3 ligands
W R Hagen, P J Silva, M A Amorim, et al.
Page
of 1