Mapping of the immunodominant regions of the NAD‐dependent formate dehydrogenase

Bogdanova, A.; Cherednikova, T.V.; Egorov, Tsezi A.; Harutyunyan, E. G.; Kurochkina, Nataleya A.; Lamzin, Victor S.; Savitskiy, Alexsander P.; Shumilin, I.A.; Popov, Vladimir O.

doi:10.1016/0014-5793(90)80128-6

Cited by 1 publication

(1 citation statement)

References 15 publications

(3 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Similarly, there is lack of immunological relationship between the yeasttype, homodimeric NAD-FDH and the complex N-FDH from Pseudomonas sp. 101, but resemblance with the dimeric FDH from Candida methylica (Bogdanova et al, 1990). The immunological data suggest that the FDH from various facultatively autotrophic bacteria and from the methanotroph M. trichosporium are immunologically related and might belong to the same structural FDH group.…”

Section: Discussionmentioning

confidence: 86%

Structural and Immunological Studies on the Soluble Formate Dehydrogenase fromAlcaligenes eutrophus

Friedebold¹,

Mayer²,

Bill³

et al. 1995

Biological Chemistry Hoppe-Seyler

View full text Add to dashboard Cite

During growth with formate as the sole energy source the autotrophic bacterium Alcaligenes eutrophus synthesizes a cytoplasmic formate dehydrogenase. The enzyme is a molybdo-iron-sulfur-flavo protein and the major NADH-producing system under these growth conditions, although it was estimated to constitute only 0.65% of the soluble cell protein. An electron microscopic analysis of the purified enzyme revealed that the particle is made up of four nonidentical submasses, corroborating previous structural data. The NH2-terminal amino acid sequences of the enzyme subunits exhibited significant similarities to those of only one other heteromeric formate dehydrogenase, the enzyme from the methane-utilizing bacterium Methylosinus trichosporium. Metal analyses yielded 21.5 g-atom iron, 2.18 g-atom nickel, 0.76 g-atom molybdenum, and 0.59 g-atom zinc per mol of enzyme. Initial electron paramagnetic resonance spectroscopic studies showed at least three distinct signals which appeared upon reduction of the enzyme with NADH or formate. The corresponding spin systems could be attributed to iron-sulfur centers of the enzyme. Comparative immunostaining and activity-staining experiments using cell extracts from various bacteria established immunological similarities between the soluble formate dehydrogenase of A. eutrophus and the soluble enzymes from all tested facultative autotrophs as well as from M. trichosporium.

show abstract

Section: Discussionmentioning

confidence: 86%