English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Soluble NADH dehydrogenase was purified to homogeneity from chemotrophically grown cells of Rhodopseudomonas capsulata by ammonium sulfate fractionation, AH -Sepharose 4B chromatography and FMN-Sepharose 6B affinity chromatography. The enzyme contains a single polypeptide chain of an apparent M, of 37000, suggesting that the subunit structure is different from that of the membrane-bound enzyme. The purified soluble NADH dehydrogenase requires flavin compounds, e.g., FMN, FAD and riboflavin, for activity. Addition of FMN and FAD. but not riboflavin, to the enzyme solution stabilized the enzyme. The pH optimum for activity was at 7.5. The enzyme was specific for NADH as an electron donor while NADPH was inert. Menadione, ferricyanide, cytochrome c and DCIP served as an electron acceptor. The M ichaelis constants for NADH. DCIP, FM N. and cytochrome c were 45, 2.9. 7.9 and 15 μM, respectively. Many properties of soluble NADH dehydrogenase were substantially different from those of the membrane-bound enzyme, suggesting different functions.

Purification and Partial Characterization of the Soluble NADH Dehydrogenase from the Phototrophic Bacterium Rhodopseudomonas capsulata