Electronic Resource
Oxford, UK
:
Blackwell Publishing Ltd
FEMS microbiology letters
135 (1996), S. 0
ISSN:
1574-6968
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
Notes:
Abstract 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 H2 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1574-6968.1996.tb07972.x
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