Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Huub Haaker"'
Publikováno v:
European Journal of Biochemistry. 127:639-646
The nitrogenase activity in whole cells of Rhodopseudomonas sphaeroides could be inhibited by lowering the electrical potential across the cytoplasmic membrane. The membrane potential was partly dissipated either by lowering the light intensity or by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::461d2e679b73e3268f847baa3ff6a548
https://doi.org/10.1111/j.1432-1033.1982.tb06920.x
https://doi.org/10.1111/j.1432-1033.1982.tb06920.x
Autor:
Huub Haaker, Wilfred R. Hagen, Baltazar de Castro, Frank T. Robb, Pedro J. Silva, Eyke C. D. van den Ban, Hans Wassink
Publikováno v:
European Journal of Biochemistry. 267:6541-6551
The genome of Pyrococcus furiosus contains the putative mbhABCDEFGHIJKLMN operon for a 14-subunit transmembrane complex associated with a Ni–Fe hydrogenase. Ten ORFs (mbhA–I and mbhM) encode hydrophobic, membrane-spanning subunits. Four ORFs (mbh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::944bc842f1e39059f3ce8cd734436109
https://doi.org/10.1046/j.1432-1327.2000.01745.x
https://doi.org/10.1046/j.1432-1327.2000.01745.x
Autor:
Hans Wassink, Wilfred R. Hagen, Huub Haaker, Pedro J. Silva, M. A. Amorim, Peter-Leon Hagedoorn, Frank T. Robb
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 5:527-534
The consecutive structural genes for the iron-sulfur flavoenzyme sulfide dehydrogenase, sudB and sudA, have been identified in the genome of Pyrococcus furiosus. The translated sequences encode a heterodimeric protein with an alpha-subunit, SudA, of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55f388defd1da0691671766a6254ac2c
https://doi.org/10.1007/pl00021452
https://doi.org/10.1007/pl00021452
Publikováno v:
Enzyme and Microbial Technology 25 (1999)
Enzyme and Microbial Technology, 25, 251-257
Enzyme and Microbial Technology, 25, 251-257
The reduction of aromatic and aliphatic (di)carboxylic acids to their corresponding aldehydes and alcohols by the hyperthermophilic organism Pyrococcus furiosus was investigated. The reduction was performed with P. furiosus cells growing in the prese
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b910354eefc7278e3482e75ed6b2323f
https://doi.org/10.1016/s0141-0229(99)00036-8
https://doi.org/10.1016/s0141-0229(99)00036-8
Publikováno v:
Biochemistry. 37:17345-17354
Nitrogenase consists of two metalloproteins (Fe protein and MoFe protein) which are assumed to associate and dissociate to transfer a single electron to the substrates. This cycle, called the Fe protein cycle, is driven by MgATP hydrolysis and is rep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f955fafa3c5a1495b2d92101d67a8032
https://doi.org/10.1021/bi981509y
https://doi.org/10.1021/bi981509y
Publikováno v:
Journal of Biological Chemistry. 271:29632-29636
The pre-steady-state electron transfer reactions of nitrogenase from Azotobacter vinelandii have been studied by stopped-flow spectrophotometry. With reduced nitrogenase proteins after the initial absorbance increase at 430 nm (which is associated wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b063561139d77c6aad8c8bd7ce3b6ee4
https://doi.org/10.1074/jbc.271.47.29632
https://doi.org/10.1074/jbc.271.47.29632
Autor:
Huub Haaker, Magdalena M. Szafran
Publikováno v:
Plant Physiology 108 (1995)
Plant Physiology, 108, 1227-1232
Plant Physiology, 108, 1227-1232
Peribacteroid membrane vesicles from pea (Pisum sativum) root nodules were isolated from membrane-enclosed bacteroids by an osmotic shock. The ATPase activity associated with this membrane preparation was characterized, and its electrogenic propertie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90cd8de9f1c7eaaaf6c0f6d1853d7a80
https://doi.org/10.1104/pp.108.3.1227
https://doi.org/10.1104/pp.108.3.1227
Publikováno v:
European Journal of Biochemistry, 225, 881-890
European Journal of Biochemistry 225 (1994)
European Journal of Biochemistry 225 (1994)
MgATP-dependent pre-steady-state proton production by nitrogenase from Azotobacter vinelandii was studied by monitoring the absorbance changes at 572 nm of the pH indicator o-cresolsulphonphtalein in a weakly buffered solution. The absorbance changes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec527df147c7df1154606bbff6961b44
https://doi.org/10.1111/j.1432-1033.1994.0881b.x
https://doi.org/10.1111/j.1432-1033.1994.0881b.x
Publikováno v:
European Journal of Biochemistry 208 (1992)
European Journal of Biochemistry, 208, 289-294
European Journal of Biochemistry, 208, 289-294
The pre-steady-state ATPase activity of nitrogenase has been reinvestigated. The exceptionally high burst in the hydrolysis of MgATP by the nitrogenase from Azotobacter vinelandii communicated by Cordewener et al. (1987) [Cordewener J., ten Asbroek A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a5599e71089420fd85d5f58a5bba11d
https://doi.org/10.1111/j.1432-1033.1992.tb17185.x
https://doi.org/10.1111/j.1432-1033.1992.tb17185.x
Autor:
Michiel A. Appels, Huub Haaker
Publikováno v:
Plant Physiology. 95:740-747
Glutamate oxaloacetate transaminase (l-glutamate: oxaloacetate aminotransferase, EC 2.6.1.1 [GOT]), a key enzyme in the flow of carbon between the organic acid and amino acid pools in pea (Pisum sativum L.) root nodules, was studied. By ion exchange
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a644ebd22e951199d9136e15d8268ea
https://doi.org/10.1104/pp.95.3.740
https://doi.org/10.1104/pp.95.3.740