Electron transport systems of Candida utilis: purification and properties of the respiratory chain-linked external NADH dehydrogenase.
The respiratory chain-linked external NADH dehydrogenase has been isolated from Candida utilis in highly purified form. The enzyme is soluble and has a molecular weight of approx. 1.5 x 10(6). The enzyme contains two moles of FMN per mole of enzyme and is composed of two large subunits of mol. wt. 270 000 and eight smaller subunits of mol. wt. 135 000. Iron and copper are present in the preparations, but appear to be contaminants. The enzyme catalyzes the oxidation of NADH and NADPH at nearly equal rates and reacts readily with 2,6-dichlorophenolindophenol, CoQ6 and CoQ1 derivatives as acceptors. Rotenone (10(-5) M) and seconal (10(-3) M) do not inhibit enzymatic activity.
D002175:Candida / Q000201:enzymology* / Q000378:metabolism; D003579:Cytochrome Reductases / Q000302:isolation & purification*; D004579:Electron Transport; D004591:Electrophoresis, Polyacrylamide Gel; D004792:Enzyme Precursors / Q000302:isolation & purification; D008970:Molecular Weight; D009245:NADH Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism
D004792:Enzyme Precursors; D003579:Cytochrome Reductases; D009245:NADH Dehydrogenase