Abstract
The electron-transport particles from Mycobacterium phlei exhibit low levels of phosphorylation unless supplemented with soluble coupling proteins. Heat treatment of the electron transport particles for 15 min at 50°C was found to result in a slight loss of oxidation and an activation of phosphorylation with NADH as substrate, while with succinate as substrate both activities increased. The heat-activated particles do not require the addition of soluble coupling factors and their level of oxidative phosphorylation is similar to that of the regular particles supplemented with the soluble coupling factors. In contrast to the lack of a requirement for the soluble coupling factors after heat activation, the heat-treated electron-transport particles require the presence of a particulate-bound coupling factor for phosphorylation. The heat-activated system, like the untreated system, was found to be sensitive to uncoupling agents.
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Selected References
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