Induction by different thioredoxins of ATPase activity in coupling factor 1 from spinach chloroplasts

Chloroplast thioredoxin mutants without active-site cysteines facilitate the reduction of the regulatory disulphide bridge on the γ-subunit of chloroplast ATP synthase

“…six times that with Trx-m [16]. This difference was not observed for soluble CF " (Figure 3) and is in agreement with an earlier report that E. coli Trx and Trx-m have the same efficiency [28]. The difference in second-order rate constants observed for Trx-m and Trx-f activation of CF o CF " is probably due to the fact that Schwarz et al [16] were comparing Trx effects on the membrane-embedded enzyme in the presence of a proton gradient.…”

“…However, no differences were found in this experiment [27]. Furthermore, little is known of the difference between Trx-f and Trxm for the activation of CF " [19,28]. Comparing the effects of recombinant chloroplast Trx-f and Trx-m on the acceleration kinetics of membrane-bound Cf o CF " , Schwarz et al [16] found that Trx-f was a better reductant for this complex.…”

Chloroplast thioredoxin mutants without active-site cysteines facilitate the reduction of the regulatory disulphide bridge on the γ-subunit of chloroplast ATP synthase

“…six times that with Trx-m [16]. This difference was not observed for soluble CF " (Figure 3) and is in agreement with an earlier report that E. coli Trx and Trx-m have the same efficiency [28]. The difference in second-order rate constants observed for Trx-m and Trx-f activation of CF o CF " is probably due to the fact that Schwarz et al [16] were comparing Trx effects on the membrane-embedded enzyme in the presence of a proton gradient.…”

“…However, no differences were found in this experiment [27]. Furthermore, little is known of the difference between Trx-f and Trxm for the activation of CF " [19,28]. Comparing the effects of recombinant chloroplast Trx-f and Trx-m on the acceleration kinetics of membrane-bound Cf o CF " , Schwarz et al [16] found that Trx-f was a better reductant for this complex.…”

Differential Effects of Chilling-Induced Photooxidation on the Redox Regulation of Photosynthetic Enzymes

“…This cystine disulfide is the target of thioredoxin in the physiological reduction pathway (65)(66)(67)(68). Although there was an initial suggestion of no differential selectivity between thioredoxin f and thioredoxin m in γ subunit reduction (69), later work showed clear specificity for thioredoxin f (70). The redox titration depicted in Figure 5 is the first reported for γ subunit reduction.…”

Mechanism of Activation of the Chloroplast ATP Synthase

“…Surprisingly, it reports for the first time kinetic data about the interaction between Trx and the isolated CF 1 (with or without its ⑀ subunit). Previous data included qualitative studies of the interaction between CF 1 and different Trxs (22,23), quantitative studies of this interaction at equilibrium using fluorescent probes (23), and kinetic studies of this interaction in thylakoids (21). These different approaches are complementary.…”

Chloroplast thioredoxin mutants without active-site cysteines facilitate the reduction of the regulatory disulphide bridge on the γ-subunit of chloroplast ATP synthase

“…six times that with Trx-m [16]. This difference was not observed for soluble CF " (Figure 3) and is in agreement with an earlier report that E. coli Trx and Trx-m have the same efficiency [28]. The difference in second-order rate constants observed for Trx-m and Trx-f activation of CF o CF " is probably due to the fact that Schwarz et al [16] were comparing Trx effects on the membrane-embedded enzyme in the presence of a proton gradient.…”

“…However, no differences were found in this experiment [27]. Furthermore, little is known of the difference between Trx-f and Trxm for the activation of CF " [19,28]. Comparing the effects of recombinant chloroplast Trx-f and Trx-m on the acceleration kinetics of membrane-bound Cf o CF " , Schwarz et al [16] found that Trx-f was a better reductant for this complex.…”

Differential Effects of Chilling-Induced Photooxidation on the Redox Regulation of Photosynthetic Enzymes

“…This cystine disulfide is the target of thioredoxin in the physiological reduction pathway (65)(66)(67)(68). Although there was an initial suggestion of no differential selectivity between thioredoxin f and thioredoxin m in γ subunit reduction (69), later work showed clear specificity for thioredoxin f (70). The redox titration depicted in Figure 5 is the first reported for γ subunit reduction.…”

Mechanism of Activation of the Chloroplast ATP Synthase

“…Surprisingly, it reports for the first time kinetic data about the interaction between Trx and the isolated CF 1 (with or without its ⑀ subunit). Previous data included qualitative studies of the interaction between CF 1 and different Trxs (22,23), quantitative studies of this interaction at equilibrium using fluorescent probes (23), and kinetic studies of this interaction in thylakoids (21). These different approaches are complementary.…”

Chloroplast thioredoxin mutants without active-site cysteines facilitate the reduction of the regulatory disulphide bridge on the γ-subunit of chloroplast ATP synthase

“…six times that with Trx-m [16]. This difference was not observed for soluble CF " (Figure 3) and is in agreement with an earlier report that E. coli Trx and Trx-m have the same efficiency [28]. The difference in second-order rate constants observed for Trx-m and Trx-f activation of CF o CF " is probably due to the fact that Schwarz et al [16] were comparing Trx effects on the membrane-embedded enzyme in the presence of a proton gradient.…”

“…However, no differences were found in this experiment [27]. Furthermore, little is known of the difference between Trx-f and Trxm for the activation of CF " [19,28]. Comparing the effects of recombinant chloroplast Trx-f and Trx-m on the acceleration kinetics of membrane-bound Cf o CF " , Schwarz et al [16] found that Trx-f was a better reductant for this complex.…”

Differential Effects of Chilling-Induced Photooxidation on the Redox Regulation of Photosynthetic Enzymes

“…This cystine disulfide is the target of thioredoxin in the physiological reduction pathway (65)(66)(67)(68). Although there was an initial suggestion of no differential selectivity between thioredoxin f and thioredoxin m in γ subunit reduction (69), later work showed clear specificity for thioredoxin f (70). The redox titration depicted in Figure 5 is the first reported for γ subunit reduction.…”

Mechanism of Activation of the Chloroplast ATP Synthase

“…Surprisingly, it reports for the first time kinetic data about the interaction between Trx and the isolated CF 1 (with or without its ⑀ subunit). Previous data included qualitative studies of the interaction between CF 1 and different Trxs (22,23), quantitative studies of this interaction at equilibrium using fluorescent probes (23), and kinetic studies of this interaction in thylakoids (21). These different approaches are complementary.…”