Abstract
Publisher Summary This chapter discusses the bacterial activity of light-influenced adenosine triphosphatase (ATPase). Chromatophores prepared from Rhodospirillum rubrum are able to synthesize ATP from adenosine diphosphate (ADP) and P i coupled with photosynthetic electron flow in a cyclic fashion. Besides photosynthetic ATP formation, chromatophores can catalyze the oxidation of nicotinamide adenine dinucleotide (NADH) by molecular oxygen coupled with ATP formation. The chromatophores have activities for ATP-P i exchange and ATPase either in the light or in darkness, which are in part brought about because of the reversibility of the ATP-forming reaction. ATPase activity by chromatophores is firmly associated with particle structure and influenced by illumination, redox dyes, and extraction of the quinones from chromatophores. The ATPase activity is catalyzed by an enzyme system containing redox components associated with chromatophores. The inhibition of ATPase activity in the light is neutralized by adding antimycin A, whereas the inhibitor hardly influences the activity in the dark.
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