Regulation of the NADH and NADPH-ferredoxin oxidoreductases in clostridia of the butyric group. Export

@article{citeulike:4893668, abstract = {NADH and NADPH-ferredoxin oxidoreductases have been studied in Clostridium acetobutylicum, Cl. tyrobutyricum and Cl. pasteurianum. The study of the distribution and regulation of these enzymatic activities in well-defined culture conditions, reveals that the essential function of NADPH-ferredoxin oxidoreductase is to produce NADPH, while NADH-ferredoxin oxidoreductase can, depending on cellular conditions, produce or oxidize NADH. When these Clostridia use glycolysis, regulation of the NADH-ferredoxin oxidoreductase by acetyl-CoA (obligatory activator of NADH-ferroxin reductase activity) and by NADH (competitive inhibitor of ferredoxin-NAD+ reductase activity) allow the enzymes to function correlatively with glyceraldehyde-3-phosphate dehydrogenase and thus control the levels of NAD+ and NADH in the cell. In Cl. tyrobutyricum and Cl. pasteurianum, the ferredoxin-NADP+ reductase activities are regulated by NAD+ and NADH in accordance with the intracellular concentrations of these coenzymes. In Cl. tyrobutyricum growing on pyruvate/acetate, NADH and NADPH-ferredoxin reductase activities cannot be detected; only the ferredoxin-NAD+ and ferredoxin-NADP+ reductase activities are found. In this Clostridium, regulation of the ferredoxin-NADP+ reductase activity is the same whether it is grown on glucose or pyruvate. Contrary to this, the ferredoxin-NAD+ reductase activity undergoes a drastic change, since NADH no longer controls the enzymatic activity. In this case regulation is no longer necessary, since glyceraldehyde-3-phosphate dehydrogenase does not function.}, author = {Petitdemange, H. and Cherrier, C. and Raval, R. and Gay, R.}, citeulike-article-id = {4893668}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/3218}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=3218}, day = {24}, issn = {0006-3002}, journal = {Biochimica et biophysica acta}, keywords = {acetobutylicum, butyric, clostridia, ferredoxin, group, nadh, nadph, oxidoreductases}, month = {February}, number = {2}, pages = {334--337}, posted-at = {2009-06-18 15:57:50}, priority = {2}, title = {Regulation of the NADH and NADPH-ferredoxin oxidoreductases in clostridia of the butyric group.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/3218}, volume = {421}, year = {1976} }

TY - JOUR ID - citeulike:4893668 L3 - citeulike-article-id:4893668 N2 - NADH and NADPH-ferredoxin oxidoreductases have been studied in Clostridium acetobutylicum, Cl. tyrobutyricum and Cl. pasteurianum. The study of the distribution and regulation of these enzymatic activities in well-defined culture conditions, reveals that the essential function of NADPH-ferredoxin oxidoreductase is to produce NADPH, while NADH-ferredoxin oxidoreductase can, depending on cellular conditions, produce or oxidize NADH. When these Clostridia use glycolysis, regulation of the NADH-ferredoxin oxidoreductase by acetyl-CoA (obligatory activator of NADH-ferroxin reductase activity) and by NADH (competitive inhibitor of ferredoxin-NAD+ reductase activity) allow the enzymes to function correlatively with glyceraldehyde-3-phosphate dehydrogenase and thus control the levels of NAD+ and NADH in the cell. In Cl. tyrobutyricum and Cl. pasteurianum, the ferredoxin-NADP+ reductase activities are regulated by NAD+ and NADH in accordance with the intracellular concentrations of these coenzymes. In Cl. tyrobutyricum growing on pyruvate/acetate, NADH and NADPH-ferredoxin reductase activities cannot be detected; only the ferredoxin-NAD+ and ferredoxin-NADP+ reductase activities are found. In this Clostridium, regulation of the ferredoxin-NADP+ reductase activity is the same whether it is grown on glucose or pyruvate. Contrary to this, the ferredoxin-NAD+ reductase activity undergoes a drastic change, since NADH no longer controls the enzymatic activity. In this case regulation is no longer necessary, since glyceraldehyde-3-phosphate dehydrogenase does not function. IS - 2 JF - Biochimica et biophysica acta SN - 0006-3002 EP - 337 TI - Regulation of the NADH and NADPH-ferredoxin oxidoreductases in clostridia of the butyric group. VL - 421 SP - 334 KW - acetobutylicum KW - butyric KW - clostridia KW - ferredoxin KW - group KW - nadh KW - nadph KW - oxidoreductases AU - Petitdemange, H AU - Cherrier, C AU - Raval, R AU - Gay, R PY - 1976/02/24/ UR - http://view.ncbi.nlm.nih.gov/pubmed/3218 ER -