Succinate dehydrogenase and other respiratory pathways in thylakoid membranes of Synechocystis sp strain PCC 6803:: Capacity comparisons and physiological function

被引:169
作者
Cooley, JW
Vermaas, WFJ
机构
[1] Arizona State Univ, Dept Plant Biol, Tempe, AZ 85287 USA
[2] Arizona State Univ, Ctr Study Early Events Photosynth, Tempe, AZ 85287 USA
关键词
D O I
10.1128/JB.183.14.4251-4258.2001
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Respiration in cyanobacterial thylakoid membranes is interwoven with photosynthetic processes. We have constructed a range of mutants that are impaired in several combinations of respiratory and photosynthetic electron transport complexes and have examined the relative effects on the redox state of the plastoquinone (PQ) pool by using a quinone electrode. Succinate dehydrogenase has a major effect on the PQ redox poise, as mutants lacking this enzyme showed a much more oxidized PQ pool. Mutants lacking type I and II NAD(P)H dehydrogenases also had more oxidized PQ pools. However, in the mutant lacking type I NADPH dehydrogenase, succinate was essentially absent and effective respiratory electron donation to the PQ pool could be established after addition of 1 mM succinate. Therefore, lack of the type I NADPH dehydrogenase had an indirect effect on the PQ pool redox state. The electron donation capacity of succinate dehydrogenase was found to be an order of magnitude larger than that of type I and II NAD(P)H dehydrogenases. The reason for the oxidized PQ pool upon inactivation of type II NADH dehydrogenase may be related to the facts that the NAD pool in the cell is much smaller than that of NADP and that the NAD pool is fully reduced in the mutant without type II NADH dehydrogenase, thus causing regulatory inhibition. The results indicate that succinate dehydrogenase is the main respiratory electron transfer pathway into the PQ pool and that type I and II NAD(P)H dehydrogenases regulate the reduction level of NADP and NAD, which, in turn, affects respiratory electron flow through succinate dehydrogenase.
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页码:4251 / 4258
页数:8
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