Irradiation with ultraviolet light (360 nm) of cell-free extracts, electron-transport particles, and soluble components from Mycobacterium phlei resulted in the loss of malate oxidation by the flavine adenine dinucleotide pathway both in cell-free extracts and reconstituted systems. Addition of vitamin K1 restored the loss to the extent of 14% and 11% in cell-free extracts and reconstituted systems respectively. Electron-transport particles from M. phlei upon reduction with malate exhibited electron-paramagnetic resonance signals at g = 2.002 and 1.94, characteristic of napthosemiquinone and nonheme iron protein, respectively. Upon irradiating the particles with ultraviolet light (360 nm) these signals were not observed. Particulate flavine-adenine-dinucleotide-dependent malate dehydrogenase (EC 1.1.1.37) of M. phlei assayed by the 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyl tetrazolium bromide and phenazine methosulfate–2,6-dichlorophenolindophenol systems, which trap electrons at cytochrome c and at the flavine level respectively, was inhibited by o-phenanthroline. These observations suggest that nonheme iron protein is sensitive to ultraviolet light (360 nm) and participates before or in combination with flavine in the malate (flavine adenine dinucleotide) pathway of M. phlei.
Purification and Properties of a Membrane-bound Phospholipase A1 from Mycobacterium phlei
