Open AccessTransition metal requirement to express high level NAD + ‐dependent formate dehydrogenase from a serine‐type methylotrophic bacterium
Author(s) -
Gírio Francisco M.,
Marcos João C.,
AmaralCollaço M.T.
Publication year - 1992
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.1574-6968.1992.tb05456.x
Subject(s) - formate dehydrogenase , methylobacterium , formate , dehydrogenase , chemistry , nad+ kinase , biochemistry , bacteria , nuclear chemistry , cofactor , molybdenum , inorganic chemistry , enzyme , biology , catalysis , genetics , 16s ribosomal rna , gene
Formate dehydrogenase (EC 1.2.1.2) from an aerobic organism was found to be metal‐dependent. This NAD + ‐dependent enxyme required the presence of tungsten or molybdenum to express high enzyme levels in the facultative methylotrophic Methylobacterium sp. RXM. The apparent V max of the reaction increased 22‐fold in a tungstate‐containing medium when compared with a non‐metal‐supplemented growth medium. The absence of those metals in the culture medium resulted in the partial loss of an energy‐yielding step and approx. 50% decrease in the cell yield was observed. Moreover, formate accumulated in the extracellular medium and culture pH dropped. Tungsten produced a higher stimulation of formate dehydrogenase activity than that obtained with molybdenum for batch cultivation of Methylobacterium sp. RXM.