Intact spinach chloroplasts scavenge hydrogen peroxide with a peroxidase that uses a photoreductant as the electron donor, but the activity of ruptured chloroplasts is very low [Nakano and Asada (1980) Plant & Cell Physiol. 21: 1295]. Ruptured spinach chloroplasts recovered their ability to photoreduce hydrogen peroxide with the concomitant evolution of oxygen after the addition of glutathione and dehydroascorbate (DHA). In ruptured chloroplasts, DHA was photoreduced to ascorbate and oxygen was evolved in the process in the presence of glutathione. DHA reductase (EC 1.8.5.1) and a peroxidase whose electron donor is specific to L-ascorbate are localized in chloroplast stroma. These observations confirm that the electron donor for the scavenging of hydrogen peroxide in chloroplasts is L-ascorbate and that the L-ascorbate is regenerated from DHA by the system: photosystem I-*ferredoxin-*NADP^>glutathione. A preliminary characterization of the chloroplast peroxidase is given.

Hydrogen Peroxide is Scavenged by Ascorbate-specific Peroxidase in Spinach Chloroplasts

One of the first of the specialized agencies of the United Nations to become active, the Food and Agriculture Organization has elicited interest beyond the specialized field of agricultural economists. Attempting as it does to solve one of the very basic problems of the world, that of an adequate food supply, the organization represents a significant and hopeful international attempt to create a world in which there may actually exist “freedom from want.” The objectives of FAO, as formally expressed in the preamble to the constitution, read as follows:“The nations accepting this constitution being determined to promote the common welfare by furthering separate and collective action on their part for the purpose of raising levels of nutrition and standards of living of the people under their jurisdiction, securing improvements in the efficiency of the production of all food and agricultural products, bettering the conditions of rural populations, and thus contributing toward an expanding world economy, hereby establish the Food and Agriculture Organization of the United Nations.”

The Food and Agriculture Organization of the United Nations

1. Plant Nutrients. 2. The Soil as a Plant Nutrient Medium. 3. Nutrient Uptake and Assimilation. 4. Plant Water Relationships. 5. Plant Growth and Crop Production. 6. Fertilizer Application. 7. Nitrogen. 8. Sulphur. 9. Phosphorus. 10. Potassium. 11. Calcium. 12. Magnesium. 13. Iron. 14. Manganese. 15. Zinc. 16. Copper. 17. Molybdenum. 18. Boron. 19. Further Elements of Importance. 20. Elements with More Toxic Effects. General Readings. References. Index.

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Principles of plant nutrition

Coupling of Phosphorylation to Electron and Hydrogen Transfer by a Chemi-Osmotic type of Mechanism

Publisher Summary This chapter discusses the chemistry of submerged soils. The chemical changes in the submerged materials influence: (a) the character of the sediment or soil that forms, (b) the suitability of wet soils for crops, (c) the distribution of plant species around lakes and streams and in estuaries, deltas, and marine flood plains, (d) the quality and quantity of aquatic life, and (e) the capacity of lakes and seas to serve as sinks for terrestrial wastes. The single electrochemical property that serves to distinguish a submerged soil from a well-drained soil is its redox potential. The redox potential of a soil or sediment provides a quick, useful, semiquantitative measure of its oxidation–reduction status. Two recent developments have stimulated interest in the chemistry of submerged soils: the breeding of lowland rice varieties, with a high yield potential, and the pollution of streams, lakes, and seas, by domestic, agricultural, and industrial wastes. The chemistry of submerged soils is valuable: (a) in understanding the soil problems, limiting the performance of high-yielding rice varieties, and (b) in assessing the role of lake, estuarine, and ocean sediments as reservoirs of nutrients for aquatic plants and as sinks for terrestrial wastes.

The Chemistry of Submerged Soils

Acetylene reduction by nitrogenase from Rhodospirillum rubrum, unlike that by other nitrogenases, was recently found by other investigators to require an activation of the iron protein of nitrogenase by an activating system comprising a chromatophore membrane component, adenosine 5′-triphosphate (ATP), and divalent metal ions. In an extension of this work, we observed that the same activating system was also required for nitrogenase-linked H2 evolution. However, we found that, depending on their nitrogen nutrition regime, R. rubrum cells produced two forms of nitrogenase that differed in their Fe protein components. Cells whose nitrogen supply was totally exhausted before harvest yielded predominantly a form of nitrogenase (A) whose enzymatic activity was not governed by the activating system, whereas cells supplied up to harvest time with N2 or glutamate yielded predominantly a form of nitrogenase (R) whose enzymatic activity was regulated by the activating system. An unexpected finding was the rapid (less than 10 min in some cases) intracellular conversion of nitrogenase A to nitrogenase R brought about by the addition to nitrogen-starved cells of glutamine, asparagine, or, particularly, ammonia. This finding suggests that mechanisms other than de novo protein synthesis were involved in the conversion of nitrogenase A to the R form. The molecular weights of the Fe protein and Mo-Fe protein components from nitrogenases A and R were the same. However, nitrogenase A appeared to be larger in size, because it had more Fe protein units per Mo-Fe protein than did nitrogenase R. A distinguishing property of the Fe protein from nitrogenase R was its ATP requirement. When combined with the Mo-Fe protein (from either nitrogenase A or nitrogenase R), the R form of Fe protein required a lower ATP concentration but bound or utilized more ATP molecules during acetylene reduction than did the A form of Fe protein. No differences between the Fe proteins from the two forms of nitrogenase were found in the electron paramagnetic resonance spectrum, midpoint oxidation-reduction potential, or sensitivity to iron chelators.

Two Forms of Nitrogenase from the Photosynthetic Bacterium Rhodospirillum rubrum

Although cytochrome b-559 has long been known as a membrane-bound redox component closely linked to the reaction center of the oxygen-generating photosystem (PSII), its role in photosynthesis has remained obscure. This paper reports evidence and outlines a hypothesis in support of a “b-559 cycle”—i.e., a light-induced, cytochrome b-559-dependent, cyclic electron transport pathway around PSII that promotes translocation of protons from plastoquinol into the aqueous domain (lumen) of photosynthetic membranes (thylakoids). Light-induced proton transport coupled to light-induced electron transport is an essential aspect of energy transduction in photosynthesis because it generates an electrochemical proton gradient that drives ATP synthesis by the process of photosynthetic phosphorylation. The principal carrier of electrons and protons in thylakoids is the plastoquinone/plastoquinol couple. We propose that the b-559 cycle functions as a redox-linked proton pump that may operate jointly with the Rieske iron-sulfur pathway in oxidizing plastoquinol. The overall effect of such concerted oxidation of plastoquinol would be the translocation into the thylakoid lumen of two protons for each electron transferred from water to plastocyanin via plastoquinone.

http://www.pnas.org/content/85/24/9524.full.pdf

Cytochrome b-559 and proton conductance in oxygenic photosynthesis

Photosynthesis by Isolated Chloroplasts XI. CO2 ASSIMILATION IN A RECONSTITUTED CHLOROPLAST SYSTEM

Photosynthesis by isolated chloroplasts. VIII. Photosynthetic phosphorylation and the generation of assimilatory power.

http://www.pnas.org/content/52/3/839.full.pdf

Daniel I. Arnon

Papers

Two Forms of Nitrogenase from the Photosynthetic Bacterium Rhodospirillum rubrum

Cytochrome b-559 and proton conductance in oxygenic photosynthesis

Photosynthesis by Isolated Chloroplasts XI. CO2 ASSIMILATION IN A RECONSTITUTED CHLOROPLAST SYSTEM

Photosynthesis by isolated chloroplasts. VIII. Photosynthetic phosphorylation and the generation of assimilatory power.

Role of ferredoxin in the reductive assimilation of co2 and acetate by extracts of the photosynthetic bacterium, chromatium.