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Oxidative Phosphorylation in Fractionated Bacterial Systems

XXII. THE EFFECT OF NEAR ULTRAVIOLET IRRADIATION ON THE SUCCINATE OXIDASE PATHWAY OF MYCOBACTERIUM PHLEI

C. K. Ramakrishna Kurup 1 and Arnold F. Brodie 1

From the 1 From the Department of Microbiology, University of Southern California School of Medicine, and the Los Angeles County General Hospital, Los Angeles, California 90033

The succinate oxidase activity of Mycobacterium phlei was sensitive to irradiation with light at 360 mµ. The loss of activity was due to a lesion occurring in the electron transport chain between the flavoprotein and cytochrome b regions. The activity lost was not restored by addition of vitamin K1 or other cofactors but could be restored by the addition of the supernatant fraction. The factor responsible for the restoration of the succinate chain has been purified. It was sensitive to heat and irradiation and appeared to be protein in nature. It activated both oxidation and phosphorylation in irradiated particulate systems. The proteins which restored the two activities could not be separated.

Submitted on March 10, 1966


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This article has been cited by other articles:


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ScienceHome page
E. Bogin, T. Higashi, and A. F. Brodie
Extraparticulate Chain Interaction between Different Electron Transport Particles
Science, September 26, 1969; 165(3900): 1364 - 1367.
[Abstract] [PDF]


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C. R. K. Murti and A. F. Brodie
New Light-Sensitive Cofactor Required for Oxidation of Succinate by Mycobacterium phlei
Science, April 18, 1969; 164(3877): 302 - 304.
[Abstract] [PDF]




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