Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.3.14 (ATP synthase)
 7,042 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The kinetics of thiol modulation of the chloroplast H+-ATPase (CF0CF1) in membrana were analyzed by employing thioredoxins that were kept reduced by 0.1 mM dithiothreitol. The kinetics of thiol modulation depend on the extent of the proton gradient. The process is an exponential function of the thioredoxin concentration and reaction time and can be described by an irreversible second order reaction. The results indicate that the formation of the complex between thioredoxin and CF0CF1 is slow compared with the subsequent reduction step. Furthermore we have compared the efficiencies of the Escherichia coli thioredoxin Trx and the two chloroplast thioredoxins Tr-m and Tr-f. The second order rate constants are 0.057 (Tr-f), 0.024 (Trx), and 0.010 s-1 microM-1 (Tr-m) suggesting that Tr-f rather than Tr-m is the physiological reductant for the chloroplast ATPase. The often employed artificial reductant dithiothreitol exhibits a second order rate constant in thiol modulation of 1.02.10(-6) s-1 microM-1.
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PMID:Kinetics and thioredoxin specificity of thiol modulation of the chloroplast H+-ATPase. 920 2

The mechanism of thiol modulation of the chloroplast ATP synthase by Escherichia coli thioredoxin was investigated in the isolated ATPase subcomplex and in the ATP synthase complex reconstituted in bacteriorhodopsin proteoliposomes. Thiol modulation was resolved kinetically by continuously monitoring ATP hydrolysis by the isolated subcomplex and ATP synthesis by proteoliposomes. The binding rate constant of reduced thioredoxin to the oxidized ATPase subcomplex devoid of its epsilon subunit could be determined. It did not depend on the catalytic turnover. Reciprocically, the catalytic turnover did not seem to depend on thioredoxin binding. Thiol modulation by Trx of the epsilon-bearing ATPase subcomplex was slow and favored the release of epsilon. The rate constant of thioredoxin binding to the membrane-bound ATP synthase increased with the protonmotive force. It was lower in the presence of ADP than in its absence, revealing a specific effect of the ATP synthase turnover on thioredoxin-gamma subunit interaction. These findings, and more especially the comparisons between the isolated ATPase subcomplex and the ATP synthase complex, can be interpreted in the frame of the rotational catalysis hypothesis. Finally, thiol modulation changed the catalytic properties of the ATP synthase, the kinetics of which became non-Michaelian. This questions the common view about the nature of changes induced by ATP synthase thiol modulation.
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PMID:Mechanism of activation of the chloroplast ATP synthase. A kinetic study of the thiol modulation of isolated ATPase and membrane-bound ATP synthase from spinach by Eschericia coli thioredoxin. 1078 30

Gravity perception and gravitropic response are essential for plant development. In herbaceous species it is widely accepted that one of the primary events in gravity perception involves the displacement of amyloplasts within specialized cells. However the signaling cascade leading to stem reorientation is not fully known especially in woody species in which primary and secondary growth occur. Several different second messengers and proteins have been suggested to be involved in signal transduction of gravitropism. Reactive oxygen species (ROS) have been implicated as second messengers in several plant hormone responses. It has been shown that ROS are asymmetrically generated in roots by gravistimulation to regions of reduced growth. Proteins involved in detoxification of ROS and defense were identified by mass spectrometry: i.e., Thioredoxin h (Trx h), CuZn superoxide dismutase (CuZn SOD), ascorbate peroxidase (APX2), oxygen evolving enhancer 1 (OEE1), oxygen evolving enhancer 2 (OEE2), and ATP synthase. These differentially accumulated proteins that correspond to detoxification of ROS were analyzed at the mRNA level. The mRNA levels showed different expression patterns than those of the corresponding proteins, and revealed that transcription levels were not completely concomitant with translation. Our data showed that these proteins may play a role in the early response to gravitropic stimulation.
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PMID:Putative role of proteins involved in detoxification of reactive oxygen species in the early response to gravitropic stimulation of poplar stems. 2310 8

Cadmium stress causes a decrease in chlorophyll content and inhibits photosynthesis in tobacco leaves. The role of thioredoxin-like protein CDSP32 expressed in plant chloroplasts is to alleviates the reduced enzymes expression involved in chlorophyll synthesis of tobacco leaves due to Cd exposure, effectively preventing chlorophyll degradation and promoting increased tobacco biomass. Overexpression of Trx CDSP32 can protect the oxygen-evolving complex on the PSII donor side and promote electron transfer on the PSII acceptor side of tobacco leaves under Cd stress. Trx CDSP32 not only significantly increase the PSI activity of tobacco leaves, but also alleviate cadmium-induced PSI photoinhibition. Although Trx CDSP32 has no significant effect on the expression of PC and FNR proteins in tobacco leaves under Cd stress, it can alleviate the decreased expression of protein subunits involved in photosynthetic electron transfer such as Cyt b6/f complex subunits, Fd, and ATP synthase subunits. Trx CDSP32 can promote the synthesis of chlorophyll, stabilize the electron transfer chain, and promote ATP synthase activity to alleviate cadmium-induced photoinhibition of PSII and PSI in tobacco leaves.
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PMID:Overexpression of Trx CDSP32 gene promotes chlorophyll synthesis and photosynthetic electron transfer and alleviates cadmium-induced photoinhibition of PSII and PSI in tobacco leaves. 3245 Apr 65