Energy-linked pyridine nucleotide transhydrogenase activity in photosynthetically grown Rhodopseudomonas palustris
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Updated: Oct 24, 2026
![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
Abstract:
Rhodopseudomonas palustris (ATCC 17001) develops energy-dependent NADP+ transhydrogenase activity while growing photosynthetically on thiosulfate, formate, or acetate as the electron donors. The enzymatic activity is present in the supernatant fraction S-144 000. -- As reported, this fraction contains small membrane fragments but no closed vesicles and was shown to drive energy-dependent reversed electron flow as well as an aerobic respiratory electron transport. The energy-dependent transhydrogenase reaction in this fraction can be driven either by ATP, ADP, or inorganic pyrophosphate, but also by acetyl phosphate or acetyl-coenzyme A in the presence of orthophosphate. -- Arsenate acts as an inhibitor and decreases preferentially the acetyl-coenzyme A-dependent and the acetyl phosphate-driven reaction; whereas, oligomycin inhibits preferentially the ATP- and the acetyl phosphate-dependent reactions. -- Acetate kinase and a phosphotransacetylase are operative in S-144 000.
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