Competition between electron acceptors in photosynthesis: Regulation of the malate valve during CO2 fixation and nitrite reduction

• Published in: Photosynthesis research 1994-10, Vol.42 (1), p.75-86
• Main Authors: Backhausen, J E, Kitzmann, C, Scheibe, R
• Format: Article
• Language: English
• ISSN: 0166-8595; 1573-5079
• DOI: 10.1007/bf00019060

For maximal rates of CO2 assimilation in isolated intact spinach chloroplasts the generation of the adequate NADPH/ATP ratio is achieved either by cyclic electron flow around photosystem I or by linear electron transport to oxaloacetate, nitrite or oxygen (Mehler-reaction). The interrelationships between these poising mechanisms turn out to be strictly hierarchical. In the presence of antimycin A, an inhibitor of ferredoxin-dependent cyclic electron transport, the reduction of both, oxaloacetate and nitrite, but not that of oxygen restores CO2 fixation. When oxaloacetate and nitrite are added at low concentrations simultaneously during steady-state CO2 fixation, the reduction of nitrite is clearly preferred over the reduction of oxaloacetate, but CO2 fixation is not influenced. Nitrite reduction is not decreased upon addition of oxaloacetate, but vice versa. This is due to the regulation of NADP-malate dehydrogenase activation by electron pressure via the ferredoxin/thioredoxin system on the one hand, and by the NADPH/(NADP+NADPH) ratio (anabolic reduction charge, ARC) on the other hand. Thus the closing of the 'malate valve' prevents drainage of reducing equivalents from the chloroplast (1) when a low ARC indicates a high demand for NADPH in the stroma and (2) when nitrite reduction reduces the electron pressure at ferredoxin. The 'malate valve' is opened when cyclic electron transport is inhibited by antimycin A. Under these conditions the rate of malate formation is higher than in the absence of the inhibitor even in the presence of oxaloacetate, thus indicating that the regulation of the 'malate valve' functions at various redox states of the acceptor side of Photosystem I.