Electron Transfer Between Membrane Complexes and Soluble Proteins in Photosynthesis

Hervás, Manuel; Navarro, J. A.; Rosa, Miguel A. De la

doi:10.1002/chin.200403271

Cited by 33 publications

(75 citation statements)

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“…The donor proteins to PS I are always acidic in eukaryotes and a positively charged docking site in the photosystem seems to be well conserved, resulting in attractive PS I-donor interactions (Herva´s et al 2003a). However, in cyanobacteria, the PS I docking site in plastocyanin and Cyt c 6 can be acidic, neutral or basic (Figure 1), the isoelectric points evolved in parallel, and the role of electrostatic forces in their interaction with PS I varies accordingly.…”

Section: Introductionmentioning

confidence: 98%

“…In photosynthetic organisms, the transfer of electrons from cytochromes b 6 )f to photosystem I (PS I) -which are both membrane-embedded complexes -is performed by the soluble metalloproteins cytochrome c 6 (Cyt c 6 ) and plastocyanin (Herva´s et al 2003a). The reaction mechanism of PSI reduction has been extensively analyzed in a wide variety of organisms, revealing three different kinetic models that appear to correspond to a gradual evolutionary increase in efficiency (Hope 2000;De la Rosa et al 2002;Herva´s et al 2003a).…”

Section: Introductionmentioning

confidence: 99%

“…The reaction mechanism of PSI reduction has been extensively analyzed in a wide variety of organisms, revealing three different kinetic models that appear to correspond to a gradual evolutionary increase in efficiency (Hope 2000;De la Rosa et al 2002;Herva´s et al 2003a). The kinetic models of the reaction of either plastocyanin or Cyt c 6 isolated from the same organism and PSI are similar and exhibit similar rate constants.…”

Section: Introductionmentioning

confidence: 99%

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Cyanobacterial Photosystem I lacks specificity in its interaction with cytochrome c6 electron donors

Hervás

Díaz-Quintana

Kerfeld³

et al. 2005

Photosynth Res

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In cyanobacteria, plastocyanin and cytochrome c(6), the alternate donor proteins to Photosystem I, can be acidic, neutral or basic; the role of electrostatics in their interaction with photosystem I varies accordingly. In order to elucidate whether these changes in the electron donors' properties correlate with complementary changes in the docking site of the corresponding photosystem, we have investigated the kinetics of reactions between three cytochrome c(6) with isoelectric points of 5.6, 7.0 and 9.0, with Photosystem I particles from the same three genera of cyanobacteria which provided the cytochromes. The model systems compared here thus sample the full range of charge properties observed in cytochromes c(6): acidic, basic and neutral. The rate constants and dependence on ionic strength for photosystem I reduction were distinctive for each cytochrome c(6), but independent of Photosystem I. We conclude that the specific structural features of each cytochrome c(6) dictate their different kinetic behaviours, whereas the three photosystems are relatively indiscriminate in docking with the electron donors.

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Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Cyanobacterial Photosystem I lacks specificity in its interaction with cytochrome c6 electron donors

Hervás

Díaz-Quintana

Kerfeld³

et al. 2005

Photosynth Res

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“…PSI reduction has been extensively analysed in vitro in a wide variety of organisms, revealing that the kinetic mechanisms for the reaction of either Pc or Cyt c 6 with PSI from the same organism are similar, although they have increased in complexity and efficiency while evolving from prokaryotic cyanobacteria to algal and plant eukaryotic organisms (Hope 2000;De la Rosa et al 2002;Hervás et al 1995Hervás et al , 2003.…”

Section: Introductionmentioning

confidence: 99%

“…In photosynthetic organisms, the transfer of electrons from the cytochrome b 6 -f to photosystem I (PSI) complexeswhich are both membrane-embedded-is carried out by the two soluble metalloproteins cytochrome c 6 (Cyt c 6 ) and plastocyanin (Pc) (Hervás et al 2003). PSI reduction has been extensively analysed in vitro in a wide variety of organisms, revealing that the kinetic mechanisms for the reaction of either Pc or Cyt c 6 with PSI from the same organism are similar, although they have increased in complexity and efficiency while evolving from prokaryotic cyanobacteria to algal and plant eukaryotic organisms (Hope 2000;De la Rosa et al 2002;Hervás et al 1995Hervás et al , 2003.…”

Section: Introductionmentioning

confidence: 99%

Effect of crowding on the electron transfer process from plastocyanin and cytochrome c6 to photosystem I: a comparative study from cyanobacteria to green algae

Hervás

Navarro

2011

Photosynth Res

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Plastocyanin and cytochrome c(6), the alternate donor proteins to photosystem I, can be acidic, neutral or basic; the role of electrostatics in their interaction with photosystem I vary accordingly for cyanobacteria, algae and plants. The effect of different crowding agents on the kinetics of the reaction between plastocyanin or cytochrome c(6) and photosystem I from three different cyanobacteria, Synechocystis PCC 6803, Nostoc PCC 7119 and Arthrospira maxima, and a green alga, Monoraphidium braunii, has been investigated by laser flash photolysis, in order to elucidate how molecular crowding affects the interaction between the two donor proteins and photosystem I. The negative effect of viscosity on the interaction of the two donors with photosystem I for the three cyanobacterial systems is very similar, as studied by increasing sucrose concentration. Bovine serum albumin seems to alter the different systems in a specific way, probably by means of electrostatic interactions with the donor proteins. Ficoll and dextran behave in a parallel manner, favouring the interaction by an average factor of 2, although this effect is somewhat less pronounced in Nostoc. With regards to the eukaryotic system, a strong negative effect of viscosity is able to overcome the favourable effect of any crowding agent, maybe due to stronger donor/photosystem I electrostatic interactions or the structural nature of the eukaryotic photosystem I-enriched membrane particles.

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A general exit strategy of monoheme cytochromes c and c₂ in electron transfer complexes?

et al. 2015

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Using our previously reported maps of the electrostatic surface of horse heart ferri-and ferro-cyt c, comparisons were made between the complementary electrostatic surfaces of three cyt c peroxidase-cyt c complexes and the photosynthetic reaction center-cyt c complex, considering both iron oxidation states. The results obtained were consistent with a sliding mechanism for the electron shuttle on the surface of the protein complexes, promoted by the change in iron oxidation state. This mechanism was found to be in agreement with theoretical and NMR studies reported in the literature. Importantly, the analysis also provided a rationale for recognition of nonproductive associations. As we have previously reported the same conclusion on examination of redox partners of cyt c in the mitochondrial respiratory pathway, our hypothesis is that the proposed mechanism could represent a general exit strategy of monoheme cyts c and c 2 in electron transfer complexes. V C 2015 IUBMB Life, 67(9):694-700, 2015

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Electron Transfer Between Membrane Complexes and Soluble Proteins in Photosynthesis

Cited by 33 publications

References 1 publication

Cyanobacterial Photosystem I lacks specificity in its interaction with cytochrome c6 electron donors

Cyanobacterial Photosystem I lacks specificity in its interaction with cytochrome c6 electron donors

Effect of crowding on the electron transfer process from plastocyanin and cytochrome c6 to photosystem I: a comparative study from cyanobacteria to green algae

A general exit strategy of monoheme cytochromes c and c₂ in electron transfer complexes?

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Electron Transfer Between Membrane Complexes and Soluble Proteins in Photosynthesis

Cited by 33 publications

References 1 publication

Cyanobacterial Photosystem I lacks specificity in its interaction with cytochrome c6 electron donors

Cyanobacterial Photosystem I lacks specificity in its interaction with cytochrome c6 electron donors

Effect of crowding on the electron transfer process from plastocyanin and cytochrome c6 to photosystem I: a comparative study from cyanobacteria to green algae

A general exit strategy of monoheme cytochromes c and c2 in electron transfer complexes?

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A general exit strategy of monoheme cytochromes c and c₂ in electron transfer complexes?