Detail of "73077-67-5"
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- Characterization of an 8-hydroxy-5-deazaflavin:NADPH oxidoreductase from Streptomyces griseus
- Characterization of an 8-hydroxy-5-deazaflavin:NADPH oxidoreductase from Streptomyces griseus. Eker, A. P. M.; Hessels, J. K. C.; Meerwaldt, R. (Biochem. Biophys. 73077-67-5 is the cas registry number of certain chemical which is used as reagents here. Lab., Delft Univ. Technol., Delft, Neth.). Biochim. Biophys. Acta, 990(1), 80-6 (English) 1989. CODEN: BBACAQ. ISSN: 0006-3002. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) An 8-hydroxy-5-deazaflavin dependent oxidoreductase [coenzyme F420-NADP reductase (I)] was isolated from S. griseus and purified 590-fold with 72% overall yield. I catalyzed electron transfer between 8-hydroxy-5-deazaflavins and NADPH. It appeared to be more specific than methanogenic I as it had an abs. requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate. A mol. wt. of 42,000 was found with gel permeation chromatog, whereas SDS-PAGE indicated the presence of 2 identical subunits. Maximal enzymic activity was at 0.32M NaCl and pH 5.9 for the redn. of 8-hydroxy-5-deazaflavin and pH 7.9 for the reverse reaction. From the kinetic consts. it was estd. that the main function of I is probably to provide cells with reduced 8-hydroxy-5-deazaflavin to be used in specific redn. reactions. These results indicate the occurrence of 8-hydroxy-5-deazaflavin-dependent electron transfer in microorganisms not belonging to the archaebacteria. .


