Hydrogen evolution by a chloroplast-ferredoxin-hydrogenase system.
TL;DR: Findings indicate that hydrogen evolution from water and sunlight by photosynthetic processes could be a method for solar energy conversion.
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Abstract: Spinach chloroplast preparations were mixed with Clostridium kluyveri hydrogenase and ferredoxin. Hydrogen evolution could be measured in the light in the absence of any added electron donors. Inhibition of the water-splitting reaction or of photosystem II reduced the amount of H2 evolved more than 95%, indicating that H2O was the electron donor in this reaction. The rates of H2 evolution observed were up to 20% of those measured in the presence of an oxygen-consuming reaction or of photosystem I electron donors. These findings indicate that hydrogen evolution from water and sunlight by photosynthetic processes could be a method for solar energy conversion.
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Citations
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Hara P. Misra,Irwin Fridovich +1 more
TL;DR: Clostridial and spinach ferredoxins, reduced enzymatically by the action of ferredoxin-TPN+ oxidoreductase, have been shown to carry out the univalent reduction of oxygen.
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TL;DR: The evolution of oxygen by illuminated chloroplasts does not involve the intermediate production of H 2 O 2 in a form available to the enzyme catalase, and there is no evidence of a generalized reducing power in plants as part of the photosynthetic mechanism.
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Potentiometric titration of the fluorescence yield of spinach chloroplasts.
W.A. Cramer,Warren L. Butler +1 more
TL;DR: The potentiometric-titration curve showed two fluorescence quenching processes, both quenched in the oxidized state, and the hypothetical quencher, Q, assumed to be responsible for light-induced fluorescence-yield changes in green photosynthetic systems could be ascribed to the more positive quench component.
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On the formation of the superoxide anion radical during the reaction of reduced iron-sulfur proteins with oxygen.
TL;DR: The formation of a free radical species, having the characteristics of the superoxide anion radical, (O2−), during aerobic catalysis involving milk xanthine oxidase is confirmed, and on reoxidation of a number of flavin-free iron-sulfur proteins of the plant ferredoxin type no O2− radicals were detected.
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Purification and properties of hydrogenase, an iron sulfur protein, from Clostridium pasteurianum W5
TL;DR: Hydrogenase (H2:ferredoxin oxidoreductase, EC 1.12.1) from Clostridium pasteurianum W5 has been purified to a state that shows one protein band with one coincident activity peak on disc electrophoresis on polyacrylamide gel and a single peak in the analytical ultracentrifuge.
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