Sulfate reduction in Catharanthus roseus (L.) |
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Authors: | H Urlaub G Jankowski |
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Institution: | (1) Abteilung für Biologie der Ruhr-Universität, Postfach 102148, D-4630 Bochum 1, Federal Republic of Germany |
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Abstract: | Cell homogenates from Catharanthus roseus (L.) G. Don. grown S-autotrophically on sulfate in the dark are capable of reducing adenylysulfate (APS) to cysteine. This reduction required a particulate protein fraction from the cell extract and reduced ferredoxin as the electron donor. The protein fraction (MW 700,000±50,000) was found to contain Fd:NADP+ reductase, glutathione reductase and an unspecific dithiol reductase, and APS-sulfotransferase and thiosulfonate reductase activity. Resolution into these individual enzyme activities led to a non-restorable loss of the APS reducing activity. It was observed that a slow gradual decay of the APS reducing activity was accompanied by a likewise slow generation of a ferredoxin-dependent sulfite reductase.Enzymes and abbreviations APS
Adenosine 5-phosphosulfate
- APS-kinase
E.C.2.7.1.25
- ATP-sulfurylase
E.C.2.7.7.4
- Fd
ferredoxin
- Fd-NADP+-reductase
E.C.1.6.7.1.
- Glutathione reductase
E.C.1.6.4.2.
- G6P
Glucose 6-phosphate
- G6PDH
glucose 6-phosphate dehydrogenase, E.C.1.1.49
- GSSG
oxidized glutathione
- GSSO3H
S-sulfoglutathione
- MVH
reduced methylviologen
- OASS
O-acetylserine sulfhydrylase-E.C. 4.2.99.8
- Sulfite reductase
E.C.1.8.1.2 |
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Keywords: | Adenosine 5-phosphosulfate" target="_blank">gif" alt="prime" align="BASELINE" BORDER="0">-phosphosulfate Catharanthus Sulfate reduction |
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