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Evron, Yoav; Johnson, Eric A.; McCarty, Richard E.

doi:10.1023/a:1005669008974

Cited by 26 publications

(10 citation statements)

References 34 publications

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“…This could occur due to: (i) vW H þ -dependent activation of ATP synthase [23], and (ii) thioredoxin-mediated activation of the Calvin cycle enzymes [24]. Actually, in the presence of MV the EPR signal of P þ 700 rapidly reached a steady-state level, which was higher than that in the control sample ( Fig.…”

Section: Uncouplersmentioning

confidence: 86%

EPR study of light‐induced regulation of photosynthetic electron transport in Synechocystis sp. strain PCC 6803

et al. 2003

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The kinetics of the light-induced redox changes of the photosystem 1 (PS 1) primary donor P 700 in whole cells of the cyanobacteria Synechocystis sp. PCC 6803 were studied by the electron paramagnetic resonance method. It was shown that the linear photosynthetic electron transport in cyanobacteria was controlled by two main mechanisms: (i) oxygen-dependent acceleration of electron transfer from PS 1 to NADP + due to activation of the Calvin cycle reactions and (ii) retardation of electron £ow between two photosystems governed by a transmembrane proton gradient. In addition to the linear photosynthetic electron transport, cyanobacteria were capable of maintaining alternative pathways involving cyclic electron transfer around PS 1 and respiratory chains.

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Section: Uncouplersmentioning

confidence: 86%

EPR study of light‐induced regulation of photosynthetic electron transport in Synechocystis sp. strain PCC 6803

et al. 2003

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“…More thorough investigations of the behavior of the " subunit are required to evaluate this scenario. Since the " subunit of chloroplast ATP synthase plays pivotal roles in the energy coupling of the trans-membrane electrochemical gradient to ATP synthesis 20) as well as stabilization of the ATPase complex, 21) it is plausible that quantitative regulation of it influences the efficiency of photosynthetic energy conversion in chloroplasts. 14,18) To address the biological relevance of N-terminal acetylation of the " subunit, more comprehensive investigation of the biochemical, genetic, and physiological aspects of the " subunit and the whole complex of chloroplast ATP synthase under stress conditions is required.…”

Section: Discussionmentioning

confidence: 99%

“…In the present study, we set out to examine the detailed structure and molecular responses of the ATP synthase " subunit, which serves as an essential factor in multiple functions, including coupling of the proton efflux to ATP synthesis, 20) inhibition of the ATP hydrolase activity of CF 1 , and stabilization of the whole ATP synthase complex.…”

Section: Potential Involvement Of N-terminal Acetylation In the Quantmentioning

confidence: 99%

Potential Involvement of N-Terminal Acetylation in the Quantitative Regulation of the ε Subunit of Chloroplast ATP Synthase under Drought Stress

Hoshiyasu

Kohzuma

Yoshida

et al. 2013

Bioscience, Biotechnology, and Biochemistry

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“…The regulation of catalytic activity and H + efflux by chloroplast subunit γ due to interaction with subunit ϵ, reduction of the disulfide bridge or other means, interpreted to reflect a displacement of γ, is discussed elsewhere [28,37–39], as is the function of subunit F 1 ϵ in Escherichia coli [40]. Recently an additional regulation of the chloroplast ATPase by a 14‐3‐3 protein has been described [41].…”

Section: Artificial and Functional Stops In γ Rotationmentioning

confidence: 99%

Does F₁‐ATPase subunit γ turn in the wrong direction?

Berzborn

Schlitter

2002

FEBS Letters

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Analyzing the direction of F 1 -ATPase subunit Q Q rotation, its shape and non-random distribution of surface residues, a mechanism is proposed for how Q Q induces the closing/ opening of the catalytic sites at L L/K K interfaces: by keeping contact with the mobile domain of subunits L L at the 'jaw' (D386, the seven consecutive hydrophobic residues and D394/ E395), rotating Q Q works as a screw conveyer within the barrel of (K K,L L) 3 3 . This rotation, in turn, is energized by a rotation of the connected membrane integral rotor of F o c subunits driven by H þ e¥ux. A topological problem arises, however, when the information on (1) the direction of the rotation of subunits Q/O in the bacterial enzyme(s) during ATP hydrolysis [14,15] and (2) the X-ray structure of the bovine enzyme [16^18] is correlated with (3) the sequence of kinetic conformational states [2^9].In the X-ray structure of bovine F 1 , di¡erent sectors of the asymmetric subunit Q are in contact with the three subunits L in di¡erent conformations [16]. The relative position of the occupancies E (empty), TP (triphosphate binding) and DP (diphosphate binding) of the three L subunits is counter-clockwise, when viewed from above. Therefore, if the interactions with subunit Q determine the conformation and occupancy of the three di¡erent subunits L, the direction of rotation of subunit Q driven by ATP hydrolysis could have been deduced to be clockwise relative to the ¢xed catalytic sites, viewed from above. Accordingly, in videograms of ATP hydrolysisdriven movements of devices ¢xed to subunit Q the direction of rotation is clockwise, viewed from above, because it is counter-clockwise, when viewed from the membrane side [14,15,19].Mainly from exchange rates in pulse/chase experiments, on the other hand, three conformational states have been de¢ned, Open with low, Loose with medium and Tight with high a⁄nity to nucleotides, and the 'energy-linked binding change mechanism' has been formulated [2^7]. In the assignment [16] of the occupancies to these conformational states, E corresponds to O, TP to L and DP to T. This assignment suggests that the sequence of conformational changes during ATP hydrolysis is O-L-T-O. From kinetic analyses this O-L-T-O sequence has been deduced for ATP synthesis [2^10,20], however.The assumption that in the videograms Q turns arti¢cially in the wrong way would lead in reality to the sequence O-T-L-O in ATP hydrolysis, in agreement with the deduced sequence of the three kinetic conformational states; but this consideration would also require the interchange of the occupancies L DP and L TP in the X-ray structures. Interchanging the assignment [21] or introducing the additional conformation 'closed' into the static three-sector cartoons [10] does not solve the problem either. The 'direction of rotation discrepancy ' [22] is represented in this article as two three-step cartoons (Fig. 1a,b), showing the course of events in one catalytic site correlated to the three conformational a⁄nities. The data and conclusions rep...

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Untitled

Cited by 26 publications

References 34 publications

EPR study of light‐induced regulation of photosynthetic electron transport in Synechocystis sp. strain PCC 6803

EPR study of light‐induced regulation of photosynthetic electron transport in Synechocystis sp. strain PCC 6803

Potential Involvement of N-Terminal Acetylation in the Quantitative Regulation of the ε Subunit of Chloroplast ATP Synthase under Drought Stress

Does F₁‐ATPase subunit γ turn in the wrong direction?

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Untitled

Cited by 26 publications

References 34 publications

EPR study of light‐induced regulation of photosynthetic electron transport in Synechocystis sp. strain PCC 6803

EPR study of light‐induced regulation of photosynthetic electron transport in Synechocystis sp. strain PCC 6803

Potential Involvement of N-Terminal Acetylation in the Quantitative Regulation of the ε Subunit of Chloroplast ATP Synthase under Drought Stress

Does F1‐ATPase subunit γ turn in the wrong direction?

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Does F₁‐ATPase subunit γ turn in the wrong direction?