The kinetics of the flash-induced P515 response in relation to the H+-permeability of the membrane bound ATPase in spinach chloroplasts |
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Authors: | Robert L A Peters Olaf van Kooten Wim J Vredenberg |
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Institution: | (1) Laboratory of Plant Physiological Research, Agricultural University, Gen. Foulkesweg 72, 6703 BW Wageningen, The Netherlands |
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Abstract: | The effect of dicyclohexylcarbodiimide (DCCD) on the kinetics of the flashinduced P515 response and on the activity of the ATPase was investigated in isolated spinach chloroplasts. It was found that after the addition of 5×10–8 mol DCCD the rate of ATP hydrolysis induced by a period of 60 sec illumination was decreased to less than 5% of its original value. At this concentration, hardly any effect, if at all, could be detected on the kinetics of the flash-induced P515 response, neither in dark-adapted nor in light-activated chloroplasts. It was concluded that the presence of concentrations of DCCD, sufficiently high to affect the ATPase activity, does not affect the kinetics of the flash-induced P515 response. Since DCCD decreases the H+ permeability of the membrane-bound ATPase, it was concluded that this permeability coefficient for protons is not an important factor in the regulation of the flash-induced membrane potential and, therefore, does not affect the kinetics of the flash-induced P515 response. |
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Keywords: | P515 electrochromic band shift ATPase DCCD proton flux spinach chloroplast |
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