Open AccessNAD(P) + ‐dependent hydrogenase activity in extracts from the cyanobacterium Anacystis nidulans
Author(s) -
Schmitz Oliver,
Bothe Hermann
Publication year - 1996
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.1574-6968.1996.tb07972.x
Subject(s) - nad+ kinase , hydrogenase , cyanobacteria , electron acceptor , enzyme , biochemistry , oxidoreductase , chemistry , rhodospirillales , bacteria , biology , stereochemistry , genetics
Sequence data had indicated that cyanobacteria might possess a bidirectional hydrogenase with properties similar to the soluble enzymes from Alcaligenes eutrophus, Nocardia opaca and Desulfovibrio fructosovorans . The present study shows that extracts from the cyanobacterium Anacystis nidulans catalyse NAD(P)H‐dependent H 2 evolution with low but significant activity and uptake of the gas with NAD(P) + as the electron acceptor. NAD + is the preferred electron acceptor and NADH the preferred donor compared to NADP + and NADPH, respectively. Activity levels of this NAD(P) + dependent, bidirectional hydrogenase are too low to support chemoautotrophic growth in A. nidulans .