Open AccessHydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon, Pyrococcus furiosus : A key role for NADPH
Author(s) -
Ma Kesen,
Hao Zhi,
Adams Michael W.W.
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb07175.x
Subject(s) - pyrococcus furiosus , ferredoxin , hydrogenase , oxidoreductase , biochemistry , chemistry , enzyme , fermentation , sulfur , archaea , organic chemistry , gene
The archaeon Pyrococcus furiosus grows optimally at 100°C during the fermentation of peptides and carbohydrates to yield organic acids, CO 2 and H 2 . It also reduces elemental sulfur (S°) to H 2 S. The production of H 2 is catalyzed by a Ni‐containing hydrogenase which also functions as a sulfur reductase [Ma et al. (1993) Proc. Natl. Acad. Sci. 90, 5341–5344]. It is shown here that this bifunctional enzyme, termed sulhydrogenase, uses NADPH rather than ferredoxin (or NADH) as an electron donor. The disposal of excess reductant during fermentation is proposed to occur via ferredoxin‐linked oxidoreductases, a NADP: ferredoxin oxidoreductase and sulfhydrogenase.