- W.R. Dunham (2)
- M. Filipiak (1)
- H.J. Grande (3)
- H. Haaker (1)
- W.R. Hagen (6)
- R. Hilhorst (2)
- M. Kruse-Wolters (5)
- K.M. Kruse-Wolters (2)
- C. Laane (2)
- C. Veeger (7)
- G. Voordouw (2)
- H. Wassink (1)
|The role of Mg ATP hydrolysis in nitrogenase catalysis.
Cordewener, J. ; Kruse-Wolters, M. ; Wassink, H. ; Haaker, H. ; Veeger, C. - \ 1988
European Journal of Biochemistry 172 (1988). - ISSN 0014-2956 - p. 739 - 745.
|Structural and magnetic properties of Fe-hydrogenases reinvestigated.
Filipiak, M. ; Hagen, W.R. ; Grande, H.J. ; Dunham, W.R. ; Berkel-Arts, A. van; Kruse-Wolters, M. ; Veeger, C. - \ 1987
Recueil des travaux chimiques des Pays-Bas = Journal of the Royal Netherlands Chemical Society 106 (1987). - ISSN 0165-0513 - p. 230 - 230.
Purification and characterization of Desulfovibrio vulgaris (Hildenborough) hydrogenase expressed in Escherichia coli.
Voordouw, G. ; Hagen, W.R. ; Kruse-Wolters, M. ; Berkel-Arts, A. van; Veeger, C. - \ 1987
European Journal of Biochemistry 162 (1987)1. - ISSN 0014-2956 - p. 31 - 36.
Hydrogenase from Desulfovibrio vulgaris (Hildenborough) is a heterologous dimer of molecular mass 46 + 13.5 kDa. Its two structural genes have been cloned on a 4664-base-pair fragment of known sequence in the vector pUC9. Expression of hydrogenase polypeptides in Escherichia coli transformed with this plasmid is poor (∼0.1% w/w of total protein). Deletion of up to 1.9 kb of insert DNA brings the gene encoding for the large subunit in close proximity to the lac promotor of pUC9 and results in a 50-fold increased expression of hydrogenase polypeptides in E. coli. The protein formed is inactive and was purified in order to delineate its defect. Complete purification was achieved with a procedure similar to that used for the isolation of active hydrogenase from D. vulgaris H. The derived protein is also an αβ dimer and electron-paramagnetic resonance studies indicate the presence of the electron-transferring ferredoxin-type iron-sulfur clusters. In contrast to the native protein from D. vulgaris H, these can only be reduced with dithionite, not with hydrogen, indicating that the hydrogen-binding active centre which also contains an iron-sulfur cluster is missing.
|The iron-sulfur composition of the active site of hydrogenase from Desulfovibrio vulgaris deduced from its subunit structure and total iron-sulfur content.
Hagen, W.R. ; Berkel-Arts, A. van; Kruse-Wolters, K.M. ; Voordouw, G. ; Veeger, C. - \ 1986
FEBS Letters 203 (1986). - ISSN 0014-5793 - p. 59 - 59.
|EPR of a novel high-spin component in activated hydrogenase from Desulfovibrio vulgaris (Hildenborough).
Hagen, W.R. ; Berkel-Arts, A. van; Kruse-Wolters, K.M. ; Dunham, W.R. ; Veeger, C. - \ 1986
FEBS Letters 201 (1986). - ISSN 0014-5793 - p. 158 - 158.
Application of hydrogenase in biotechnological conversions.
Berkel-Arts, A. van; Dekker, M. ; Dijk, C. van; Grande, H.J. ; Hagen, W.R. ; Hilhorst, R. ; Kruse-Wolters, M. ; Laane, C. ; Veeger, C. - \ 1986
Biochimie 68 (1986)1. - ISSN 0300-9084 - p. 201 - 209.
|Application of hydrogenase in biotechnological conversions
Berkel-Arts, A. van; Dekker, A. ; Dijk, C. van; Grande, H.J. ; Hagen, W.R. ; Hilhorst, R. ; Kruse-Wolters, M. ; Laane, C. ; Veeger, C. - \ 1985
In: Abstr. Proc. Int. Symp. Molecular Biology of Hydrogenases, Szeged, Hungary (1985)