Purification and crystallization of NADPH-adrenodoxin reductase from bovine adrenocortical mitochondria.

Flavoprotein and iron sulfur protein as components of an electron transport system have been shown to form a complex under certain conditions [ 1,2]. Chu and Kimura [3] demonstrated that the complex formation between adrenodoxin reductase and adrenodoxin depends on the ionic strength of the environment. We have succeeded in showing the complex formation of adrenodoxin reductase with immobilized adrenodoxin on Sepharose gel and achieving a high purification in one step. By the novel purification procedure including the affinity chromatography, the enzyme was crystallized as rhombic plates with a yield of 24% and 200-fold purification from the crude extract.