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Academic literature on the topic 'Plastocyanine'

Author: Grafiati

Published: 4 June 2021

Last updated: 16 November 2024

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Journal articles on the topic "Plastocyanine"

1

Moore, JM, DA Case, WJ Chazin, GP Gippert, TF Havel, R. Powls, and PE Wright. "Three-dimensional solution structure of plastocyanin from the green alga Scenedesmus obliquus." Science 240, no. 4850 (April 15, 1988): 314–17. http://dx.doi.org/10.1126/science.3353725.

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The solution conformation of plastocyanin from the green alga Scenedesmus obliquus has been determined from distance and dihedral angle constraints derived by nuclear magnetic resonance (NMR) spectroscopy. Structures were generated with distance geometry and restrained molecular dynamics calculations. A novel molecular replacement method was also used with the same NMR constraints to generate solution structures of S. obliquus plastocyanin from the x-ray structure of the homologous poplar protein. Scenedesmus obliquus plastocyanin in solution adopts a beta-barrel structure. The backbone conformation is well defined and is similar overall to that of poplar plastocyanin in the crystalline state. The distinctive acidic region of the higher plant plastocyanins, which functions as a binding site for electron transfer proteins and inorganic complexes, differs in both shape and charge in S. obliquus plastocyanin.

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2

Bond, Charles S., Derek S. Bendall, Hans C. Freeman, J. Mitchell Guss, Christopher J. Howe, Michael J. Wagner, and Matthew C. J. Wilce. "The structure of plastocyanin from the cyanobacterium Phormidium laminosum." Acta Crystallographica Section D Biological Crystallography 55, no. 2 (February 1, 1999): 414–21. http://dx.doi.org/10.1107/s0907444998012074.

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The crystal structure of the `blue' copper protein plastocyanin from the cyanobacterium Phormidium laminosum has been solved and refined using 2.8 Å X-ray data. P. laminosum plastocyanin crystallizes in space group P43212 with unit-cell dimensions a = 86.57, c = 91.47 Å and with three protein molecules per asymmetric unit. The final residual R is 19.9%. The structure was solved using molecular replacement with a search model based on the crystal structure of a close homologue, Anabaena variabilis plastocyanin (66% sequence identity). The molecule of P. laminosum plastocyanin has 105 amino-acid residues. The single Cu atom is coordinated by the same residues – two histidines, a cysteine and a methionine – as in other plastocyanins. In the crystal structure, the three molecules of the asymmetric unit are related by a non-crystallographic threefold axis. A Zn atom lies between each pair of neighbouring molecules in this ensemble, being coordinated by a surface histidine residue of one molecule and by two aspartates of the other.

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3

Haehnel, W., R. Ratajczak, and H. Robenek. "Lateral distribution and diffusion of plastocyanin in chloroplast thylakoids." Journal of Cell Biology 108, no. 4 (April 1, 1989): 1397–405. http://dx.doi.org/10.1083/jcb.108.4.1397.

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The lateral distribution of plastocyanin in the thylakoid lumen of spinach and pea chloroplasts was studied by combining immunocytochemical localization and kinetic measurements of P700+ reduction at high time resolution. In dark-adapted chloroplasts, the concentration of plastocyanin in the photosystem I containing stroma membranes exceeds that in photosystem II containing grana membranes by a factor of about two. Under these conditions, the reduction of P700+ with a halftime of 12 microseconds after a laser flash of saturating intensity indicates that to greater than 95% of total photosystem I a plastocyanin molecule is bound. An analysis of the labeling densities, the length of the different lumenal regions, and the total amounts of plastocyanin and P700 shows that most of the remaining presumable mobile plastocyanin is found in the granal lumen. This distribution of plastocyanin is consistent with a more negative surface charge density in the stromal than in the granal lumen. During illumination the concentration of plastocyanin in grana increases at the expense of that in stroma lamellae, indicating a light-driven diffusion from stroma to grana regions. Our observations provide evidence that a high concentration of plastocyanin in grana in the light favors the lateral electron transport from cytochrome b6/f complexes in appressed grana across the long distance to photosystem I in nonappressed stroma membranes.

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Fedorov, V. A., I. A. Volkhin, S. S. Khrushchev, T. K. Antal, and I. B. Kovalenko. "Role of Charged Amino Acid Residues of Plastocyanin in Interaction with Cytochrome B6f Complex and Photosystem I of Higher Plants: A Study Using the Brownian Dynamics Method." Mathematical Biology and Bioinformatics 18, no. 2 (November 22, 2023): 434–45. http://dx.doi.org/10.17537/2023.18.434.

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Plastocyanin is an electron carrier protein in the electron transport chain of chloroplasts, carrying out the transfer of an electron from cytochrome f of the cytochrome b6f complex to photosystem I. Using the method of Brownian dynamics, the process of formation of the encounter complex of plastocyanin and photosystem I of higher plants was studied. The electrostatic properties of proteins were studied, and the most important amino acid residues for their interaction were identified. It was shown that plastocyanin contacts the positively charged alpha-helix protruding into the lumen of the F subunit of photosystem I with amino acid residues of both its “large” (D42, E43, D44, E45, D51) and “small” (E59, E60, D61) the negatively charged regions in 73 % of cases, and only the "large" region in 27 % of cases. A comparison of the study results with previously obtained data on the interaction of plastocyanin with cytochrome f made it possible to identify the role of charged amino acid residues of plastocyanin in the process of complex formation with photosystem I and cytochrome f. When interacting with cytochrome f, a positively charged region located near the small domain of cytochrome f and formed by amino acid residues K58, K65, K66, K187 and R209, attracts negatively charged amino acid residues D42, E43, D44, E45, D51 of the “large” region of plastocyanin, forming an electrostatic hinge contact around which rotation occurs when the final complex is formed. The “small” region of plastocyanin is involved in the stabilization of the final complex. Thus, both in the formation of the encounter complex with photosystem I, and in the reaction with cytochrome f the same negatively charged amino acid residues of plastocyanin are used.

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Höhner, Ricarda, Mathias Pribil, Miroslava Herbstová, Laura Susanna Lopez, Hans-Henning Kunz, Meng Li, Magnus Wood, et al. "Plastocyanin is the long-range electron carrier between photosystem II and photosystem I in plants." Proceedings of the National Academy of Sciences 117, no. 26 (June 15, 2020): 15354–62. http://dx.doi.org/10.1073/pnas.2005832117.

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In photosynthetic electron transport, large multiprotein complexes are connected by small diffusible electron carriers, the mobility of which is challenged by macromolecular crowding. For thylakoid membranes of higher plants, a long-standing question has been which of the two mobile electron carriers, plastoquinone or plastocyanin, mediates electron transport from stacked grana thylakoids where photosystem II (PSII) is localized to distant unstacked regions of the thylakoids that harbor PSI. Here, we confirm that plastocyanin is the long-range electron carrier by employing mutants with different grana diameters. Furthermore, our results explain why higher plants have a narrow range of grana diameters since a larger diffusion distance for plastocyanin would jeopardize the efficiency of electron transport. In the light of recent findings that the lumen of thylakoids, which forms the diffusion space of plastocyanin, undergoes dynamic swelling/shrinkage, this study demonstrates that plastocyanin diffusion is a crucial regulatory element of plant photosynthetic electron transport.

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Kropat, Janette, Sean D. Gallaher, Eugen I. Urzica, Stacie S. Nakamoto, Daniela Strenkert, Stephen Tottey, Andrew Z. Mason, and Sabeeha S. Merchant. "Copper economy in Chlamydomonas: Prioritized allocation and reallocation of copper to respiration vs. photosynthesis." Proceedings of the National Academy of Sciences 112, no. 9 (February 2, 2015): 2644–51. http://dx.doi.org/10.1073/pnas.1422492112.

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Inorganic elements, although required only in trace amounts, permit life and primary productivity because of their functions in catalysis. Every organism has a minimal requirement of each metal based on the intracellular abundance of proteins that use inorganic cofactors, but elemental sparing mechanisms can reduce this quota. A well-studied copper-sparing mechanism that operates in microalgae faced with copper deficiency is the replacement of the abundant copper protein plastocyanin with a heme-containing substitute, cytochrome (Cyt) c6. This switch, which is dependent on a copper-sensing transcription factor, copper response regulator 1 (CRR1), dramatically reduces the copper quota. We show here that in a situation of marginal copper availability, copper is preferentially allocated from plastocyanin, whose function is dispensable, to other more critical copper-dependent enzymes like Cyt oxidase and a ferroxidase. In the absence of an extracellular source, copper allocation to Cyt oxidase includes CRR1-dependent proteolysis of plastocyanin and quantitative recycling of the copper cofactor from plastocyanin to Cyt oxidase. Transcriptome profiling identifies a gene encoding a Zn-metalloprotease, as a candidate effecting copper recycling. One reason for the retention of genes encoding both plastocyanin and Cyt c6 in algal and cyanobacterial genomes might be because plastocyanin provides a competitive advantage in copper-depleted environments as a ready source of copper.

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Kovalenko, Ilya, Vladimir Fedorov, Sergei Khruschev, Taras Antal, Galina Riznichenko, and Andrey Rubin. "Plastocyanin and Cytochrome f Complex Structures Obtained by NMR, Molecular Dynamics, and AlphaFold 3 Methods Compared to Cryo-EM Data." International Journal of Molecular Sciences 25, no. 20 (October 15, 2024): 11083. http://dx.doi.org/10.3390/ijms252011083.

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Plastocyanin is a small mobile protein that facilitates electron transfer through the formation of short-lived protein–protein complexes with cytochrome bf and photosystem 1. Due to the transient nature of plastocyanin–cytochrome f complex, the lack of a long-lived tight complex makes it impossible to determine its structure by X-ray diffraction analysis. Up to today, a number of slightly different structures of such complexes have been obtained by experimental and computer methods. Now, artificial intelligence gives us the possibility to predict the structures of intermolecular complexes. In this study, we compare encounter and final complexes obtained by Brownian and molecular dynamics methods, as well as the structures predicted by AlphaFold 3, with NMR and cryo-EM data. Surprisingly, the best match for the plastocyanin electron density obtained by cryo-EM was demonstrated by an AlphaFold 3 structure. The orientation of plastocyanin in this structure almost completely coincides with its orientation obtained by molecular dynamics calculation, and, at the same time, it is different from the orientation of plastocyanin predicted on the basis of NMR data. This is even more unexpected given that only NMR structures for the plastocyanin-cytochrome f complex are available in the PDB database, which was used to train AlphaFold 3.

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Merchant, S., and L. Bogorad. "Regulation by copper of the expression of plastocyanin and cytochrome c552 in Chlamydomonas reinhardi." Molecular and Cellular Biology 6, no. 2 (February 1986): 462–69. http://dx.doi.org/10.1128/mcb.6.2.462-469.1986.

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Plastocyanin and cytochrome c552 are interchangeable electron carriers in the photosynthetic electron transfer chains of some cyanobacteria and green algae (P. M. Wood, Eur. J. Biochem. 87:9-19, 1978; G. Sandmann et al., Arch. Microbiol. 134:23-27, 1983). Chlamydomonas reinhardi cells respond to the availability of copper in the medium and accordingly accumulate either plastocyanin (if copper is available) or cytochrome c552 (if copper is not available). The response occurs in both heterotrophically and phototrophically grown cells. We have studied the molecular level at which this response occurs. No immunoreactive polypeptide is detectable under conditions where the mature protein is not spectroscopically detectable. Both plastocyanin and cytochrome c552 appear to be translated (in vitro) from polyadenylated mRNA as precursors of higher molecular weight. RNA was isolated from cells grown either under conditions favorable for the accumulation of plastocyanin (medium with Cu2+) or for the accumulation of cytochrome c552 (without Cu2+ added to the medium). Translatable mRNA for preapoplastocyanin was detected in both RNA preparations, although mature plastocyanin was detected in C. reinhardi cells only when copper was added to the culture. Translatable mRNA for preapocytochrome, on the other hand, was detected only in cells grown under conditions where cytochrome c552 accumulates (i.e., in the absence of copper). We conclude that copper-mediated regulation of plastocyanin and cytochrome c552 accumulation is effected at different levels, the former at the level of stable protein and the latter at the level of stable mRNA.

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Merchant, S., and L. Bogorad. "Regulation by copper of the expression of plastocyanin and cytochrome c552 in Chlamydomonas reinhardi." Molecular and Cellular Biology 6, no. 2 (February 1986): 462–69. http://dx.doi.org/10.1128/mcb.6.2.462.

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Plastocyanin and cytochrome c552 are interchangeable electron carriers in the photosynthetic electron transfer chains of some cyanobacteria and green algae (P. M. Wood, Eur. J. Biochem. 87:9-19, 1978; G. Sandmann et al., Arch. Microbiol. 134:23-27, 1983). Chlamydomonas reinhardi cells respond to the availability of copper in the medium and accordingly accumulate either plastocyanin (if copper is available) or cytochrome c552 (if copper is not available). The response occurs in both heterotrophically and phototrophically grown cells. We have studied the molecular level at which this response occurs. No immunoreactive polypeptide is detectable under conditions where the mature protein is not spectroscopically detectable. Both plastocyanin and cytochrome c552 appear to be translated (in vitro) from polyadenylated mRNA as precursors of higher molecular weight. RNA was isolated from cells grown either under conditions favorable for the accumulation of plastocyanin (medium with Cu2+) or for the accumulation of cytochrome c552 (without Cu2+ added to the medium). Translatable mRNA for preapoplastocyanin was detected in both RNA preparations, although mature plastocyanin was detected in C. reinhardi cells only when copper was added to the culture. Translatable mRNA for preapocytochrome, on the other hand, was detected only in cells grown under conditions where cytochrome c552 accumulates (i.e., in the absence of copper). We conclude that copper-mediated regulation of plastocyanin and cytochrome c552 accumulation is effected at different levels, the former at the level of stable protein and the latter at the level of stable mRNA.

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Qiao, Y., H. F. Li, S. M. Wong, and Z. F. Fan. "Plastocyanin Transit Peptide Interacts with Potato virus X Coat Protein, While Silencing of Plastocyanin Reduces Coat Protein Accumulation in Chloroplasts and Symptom Severity in Host Plants." Molecular Plant-Microbe Interactions® 22, no. 12 (December 2009): 1523–34. http://dx.doi.org/10.1094/mpmi-22-12-1523.

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Potato virus X coat protein (PVXCP) is, through communication with host proteins, involved in processes such as virus movement and symptom development. Here, we report that PVXCP also interacts with the precursor of plastocyanin, a protein involved in photosynthesis, both in vitro and in vivo. Yeast two-hybrid analysis indicated that PVXCP interacted with only the plastocyanin transit peptide. In subsequent bimolecular fluorescence complementation assays, both proteins were collocated within chloroplasts. Western blot analyses of chloroplast fractions showed that PVXCP could be detected in the envelope, stroma, and lumen fractions. Transmission electron microscopy demonstrated that grana were dilated in PVX-infected Nicotiana benthamiana. Furthermore, virus-induced gene silencing of plastocyanin by prior infection of N. benthamiana using a Tobacco rattle virus vector reduced the severity of symptoms that developed following subsequent PVX infection as well as the accumulation of PVXCP in isolated chloroplasts. However, PVXCP could not be detected in pea chloroplasts in an in vitro re-uptake assay using the plastocyanin precursor protein. Taken together, these data suggest that PVXCP interacts with the plastocyanin precursor protein and that silencing the expression of this protein leads to reduced PVXCP accumulation in chloroplasts and ameliorates symptom severity in host plants.

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Dissertations / Theses on the topic "Plastocyanine"

1

Durell, Stewart Richard. "Biophysical studies of plastocyanin /." The Ohio State University, 1989. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487673114114086.

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He, Shiping. "Protein engineering of pea plastocyanin." Thesis, University of Cambridge, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.295349.

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Hani, Umama. "Regulation of cyclic and pseudocyclic electron transport." Electronic Thesis or Diss., université Paris-Saclay, 2024. http://www.theses.fr/2024UPASB044.

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La photosynthèse, principale voie de production d'énergie dans les environnements naturels, repose sur des flux d'électrons intervenant dans plusieurs complexes dans la membrane des thylakoïdes des organismes photosynthétiques. Le flux principal est le transport « linéaire » des électrons qui implique leur transfert de l'eau au NADP⁺, le tout couplé à la synthèse d'ATP. L'oxydation de l'eau photosynthétique est catalysée par les clusters de manganèse (Mn₄CaO₅) au niveau du photosystème II (PSII). Pour assurer un équilibre optimal entre la quantité d'énergie produite et consommée, les organismes photosynthétiques détournent une partie de l'énergie lumineuse récoltée des voies de transport d'électrons "linéaires" vers des voies "alternatives". Parmi ces voies, on trouve les transports cyclique et pseudocyclique des électrons autour du photosystème I (PSI), qui fournit de l'ATP supplémentaire pour répondre aux besoins métaboliques. En outre, des systèmes redox spécialisés appelés "thiorédoxines" sont responsables du maintien de l'état redox et de l'acclimatation rapide des plantes à un environnement changeant. Dans le cas contraire, cela peut conduire à des niveaux toxiques d'espèces réactives de l'oxygène (ROS) dans les cellules. Nous avons étudié les effets de l'excès et de la carence en manganèse (Mn) sur le transport des électrons au cours de la photosynthèse chez l'hépatique Marchantia polymorpha. Nous avons montré que l'homéostasie du Mn a un effet sur le métabolisme mais aussi sur la photosynthèse. De plus, nous avons étudié les changements redox in vivo du P700 et du la plastocyanine (PC) en utilisant le spectrophotomètre KLAS-NIR. Il semble que la carence en Mn permet une augmentation du transport cyclique des électrons (TCE) ce qui indique la présence de supercomplexes contenant le PSI et le complexe du cytochrome b6f. Dans un second temps, nous nous sommes concentrées sur la régulation redox de la réduction de l'oxygène (transport d'électrons pseudocyclique) du côté de l'accepteur du PSI. En utilisant la spectroscopie RPE par piégeage indirect de spin, nous avons montré que des plantes sauvages d'Arabidopsis thaliana génèrent plus de ROS en photopériode de jour court (JC) qu'en photopériode de jour long (JL). En outre, nous avons mis en évidence le rôle de plusieurs acteurs, y compris les thiorédoxines et plusieurs protéines du lumen et du stroma dans la régulation redox. De plus, j'ai découvert que le transfert du pouvoir réducteur du stroma au lumen est médié par une protéine appelée CCDA. Par ailleurs, l'attachement réversible de Trxm à la membrane des thylakoïdes agit comme une force motrice pour l’accumulation des ROS en JC. Dans l'ensemble, les résultats établissent un lien étroit entre le transport cyclique et pseudocyclique des électrons en termes de régulations redox médiées par les thiorédoxines. Une voie est également ouverte quant à une exploration plus approfondie du TCE dans différentes conditions de stress
Photosynthesis acts as the main gateway for energy production in natural environments and relies on the electron flow via several complexes in the thylakoid membrane of photosynthetic organisms. The major flux is “linear” electron transport, which involves the transfer of electrons from water to NADP⁺, coupled with the ATP synthesis. Photosynthetic water oxidation is catalyzed by manganese cluster (Mn₄CaO₅) at photosystem II (PSII). To ensure an optimal balance between the amount of energy produced and consumed, photosynthetic organisms divert part of the harvested light energy from “linear” to “alternative” electron transport pathways. Among those pathways are cyclic and pseudocyclic electron transport around Photosystem I (PSI), which supplies extra ATP to meet metabolic demands. Moreover, specialized redox systems, called " thioredoxins " are responsible for maintaining the redox status and fast acclimation of plants to constantly fluctuating environments, which could otherwise lead to toxic levels of reactive oxygen species (ROS) production. We studied the effects of manganese (Mn) excess and deficiency on photosynthetic electron transport in the liverwort Marchantia polymorpha. We have shown that Mn homeostasis has an effect at both metabolic and photosynthetic levels. Moreover, we have studied the in vivo redox changes of P700 and PC using KLAS-NIR spectrophotometer and have shown that Mn deficiency seems to enhance cyclic electron transport (CET), that may indicate the presence of supercomplexes containing PSI and cytochrome b6f complex. The second part of this PhD focused on the redox regulation of oxygen reduction (pseudocyclic electron transport) at the PSI acceptor side. By using indirect spin trapping EPR spectroscopy, we have shown that Arabidopsis thaliana wild type plants generate more ROS in short day (SD) photoperiod than in long day (LD) photoperiod. Further, the current study highlighted the role of several players in redox regulation; including thioredoxins and several other lumenal and stromal proteins. Moreover, I explored that the transfer of reducing powers from stroma to lumen is mediated by a protein called CCDA and that reversible attachment of Trxm to the thylakoid membrane acts as the driving force for higher ROS under the SD light regime. Overall, this research establishes a strong connection between cyclic and pseudocyclic electron transport in terms of thioredoxins mediated redox regulations and also paves the way to further explore CET under different stress conditions

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Driscoll, P. C. "'1H NMR studies of plastocyanin in solution." Thesis, University of Oxford, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.382519.

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Chua, Y. L. "Chromatin structure of the pea plastocyanin gene." Thesis, University of Cambridge, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.597674.

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The pea plastocyanin gene (PetE) is a single-copy, nuclear photosynthesis gene. Pea PetE is flanked by an enhancer/5' matrix attachment region (MAR) and a 3' MAR. When linked upstream to uidA directed by the CaMV 35S promoter, the enhancer/5' MAR increased reporter gene expression in transgenic tobacco plants. In contrast, the 3' MAR increased expression only when linked downstream of the reporter gene. The 3' MAR, but not the 5' MAR, decreased variation in reporter gene expression. These results indicate that the two MARs surrounding PetE have different effects on transgene expression. The chromatin structure of PetE was examined at three different transcriptional states by investigating the nuclease accessibility of the gene in pea roots, etiolated shoots and green shoots. Time-course digestions of nuclei with micrococcal nuclease and DNaseI indicated that the enhancer/5' MAR and promoter regions were more resistant to digestion in the inactive gene in pea roots than the same regions in the active gene in shoots, whereas the transcribed region of PetE was digested similarly amongst the tissues. PetE transcription is hence accompanied by changes in the nuclease accessibility of the enhancer/5' MAR and promoter regions only. The acetylation states of histone H3 and H4 proteins associated with PetE were analysed by chromatin immunoprecipitation with antibodies specific for acetylated or non-acetylated histone tails followed by polymerase chain reaction quantification. Comparison of pea tissue indicated that histone acetylation was associated with increased PetE transcription in green shoots. Moreover, acetylation of both histone H3 and H4 proteins was targeted to the enhancer/5' MAR and promoter regions in green shoots, suggesting that only specific nucleosomes along the gene were modified.

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Wagner, Michael Johannes. "Interaction between cyanobacterial plastocyanin and cytochrome f." Thesis, University of Cambridge, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.627130.

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Javadi, Morteza. "Plastocyanin evaluation in wheat (T. aestivum L.)." The Ohio State University, 1988. http://rave.ohiolink.edu/etdc/view?acc_num=osu1298400458.

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Bottin, Hervé. "Etude du transfert d'electron dans le photosysteme 1 des vegetaux superieurs par spectroscopie d'absorption par eclairs." Paris 6, 1987. http://www.theses.fr/1987PA066147.

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Helliwell, Christopher Andrew. "Regulation of expression of the pea plastocyanin gene." Thesis, University of Cambridge, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.338311.

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Last, David Ian. "Structure and expression of the pea plastocyanin gene." Thesis, University of Cambridge, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.256631.

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Books on the topic "Plastocyanine"

1

Jansson, Hanna. Plastocyanin--a transient link in the photosynthetic electron transfer chain. Göteborg: Department of Chemistry, Biochemistry and Biophysics, Göteborg University, 2007.

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H, Golbeck John, ed. Photosystem I: The light-driven plastocyanin : ferredoxin oxidoreductase. Dordrecht: Springer, 2006.

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3

Jäger, Karin. Proteinbiosynthese von Plastocyanin und Cytochrom c-553 in der Grünalge Scenedesmus acutus. Konstanz: Hartung-Gorre, 1985.

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Jäger, Karin. Proteinbiosynthese von Plastocyanin und Cytochrom c-553 in der Grünalge Scenedesmus acutus. Konstanz: Hartung-Gorre, 1985.

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Dimitrov, Mitko Ivanov. Story of the Scientific Discovery of Plastocyanin Dimorphism. Cambridge Scholars Publishing, 2024.

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Golbeck, John H. Photosystem I : The Light-Driven Plastocyanin: Ferredoxin Oxidoreductase. Springer Netherlands, 2010.

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Dimitrov, Mitko Ivanov. Story of the Scientific Discovery of Plastocyanin Dimorphism. Cambridge Scholars Publishing, 2023.

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Illerhaus, Jürgen. Struktur und Funtionsuntersuchungen am intakten Cytochrom-bf-Komplex: Wechselwirkung mit Plastocyanin. 1998.

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Book chapters on the topic "Plastocyanine"

1

Bertini, Ivano, and Roberta Pierattelli. "Plastocyanin." In Encyclopedia of Metalloproteins, 1694–98. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_92.

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Schomburg, D., M. Salzmann, and D. Stephan. "Plastoquinol-plastocyanin reductase." In Enzyme Handbook 7, 715–19. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78521-4_136.

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Durell, S., E. Gross, and J. Labanowski. "Modeling of Electrostatic Effects in Plastocyanin." In Current Research in Photosynthesis, 2217–20. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_507.

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Sykes, A. G. "Plastocyanin and the blue copper proteins." In Long-Range Electron Transfer in Biology, 175–224. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/3-540-53260-9_7.

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Reichert, J., L. Altschmied, R. B. Klösgen, R. G. Herrmann, and W. Haehnel. "Interaction of Spinach Plastocyanin with Photosystem I." In Photosynthesis: from Light to Biosphere, 1671–74. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-009-0173-5_392.

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Drepper, Friedel, Michael Hippler, and Wolfgang Haehnel. "Dynamic Interaction between Plastocyanin and Photosystem I." In Photosynthesis: from Light to Biosphere, 1675–78. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-009-0173-5_393.

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Haehnel, Wolfgang, Rafael Ratajczak, and Rowan Mitchell. "On the Electron Transfer from Plastocyanin to P700." In Progress in Photosynthesis Research, 521–24. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3535-8_123.

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De la Rosa, Miguel A., Manuel Hervás, Antonio Díaz-Quintana, Berta De la Cerda, Fernando P. Molina-Heredia, Alexis Balme, Christine Cavazza, and José A. Navarro. "From Cytochrome C6 to Plastocyanin. An Evolutionary Approach." In Photosynthesis: Mechanisms and Effects, 1499–504. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_353.

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Gray, J. C., K. H. Pwee, R. E. Slatter, and P. Dupree. "Regulation of Expression of the Pea Plastocyanin Gene." In Regulation of Chloroplast Biogenesis, 23–29. Boston, MA: Springer US, 1992. http://dx.doi.org/10.1007/978-1-4615-3366-5_4.

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Lee, Byung Hyun, Takashi Hibino, Tetsuko Takabe, and Teruhiro Takabe. "Site-Directed Mutagenesis of Acidic Patches of Plastocyanin." In Photosynthesis: from Light to Biosphere, 1667–70. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-009-0173-5_391.

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Conference papers on the topic "Plastocyanine"

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Nakashima, Satoru, Yutaka Nagasawa, Kazushige Seike, Tadashi Okada, Maki Sato, and Takamitsu Kohzuma. "Induced Coherent Protein Dynamics in Charge-Transfer Reaction of Plastocyanin." In International Conference on Ultrafast Phenomena. Washington, D.C.: OSA, 2000. http://dx.doi.org/10.1364/up.2000.wb4.

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Nagasawa, Yutaka, Kenji Fujita, Tetsuro Katayama, Yukihide Ishibashi, Hiroshi Miyasaka, Teruhiro Takabe, Satoshi Nagao, and Shun Hirota. "Coherent Nuclear Motion of Blue Copper Protein; Plastocyanin: Comparing LMCT and d-d Excitation." In International Conference on Ultrafast Phenomena. Washington, D.C.: OSA, 2010. http://dx.doi.org/10.1364/up.2010.the4.

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Ramos, Sashary, Megan Thielges, Rachel Horness, and Amanda Le Sueur. "CHARACTERIZATION OF THE HIGHLY DYNAMIC INTERFACE IN THE PLASTOCYANIN-CYTOCHROME f COMPLEX BY SITE-SPECIFIC 2D IR." In 74th International Symposium on Molecular Spectroscopy. Urbana, Illinois: University of Illinois at Urbana-Champaign, 2019. http://dx.doi.org/10.15278/isms.2019.tf01.

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BEHESHTI, AZIZOLLA, AHMAD REZA RAHMANI, and MOAYAD HOSAINI SADR. "SYNTHESIS AND CRYSTAL STRUCTURE STUDIES OF Cu(I) COMPLEXES WITH PYRAZOLYBORATEO LIGANDS: AN APPROACH TO SYNTHETIC MODEL OF THE ACTIVE SITE OF BLUE COPPER PROTEINS SUCH AS PLASTOCYANIN." In Proceedings of the 8th Asian Conference. WORLD SCIENTIFIC, 2002. http://dx.doi.org/10.1142/9789812776259_0097.

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Reports on the topic "Plastocyanine"

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Thielges, Megan. Mechanisms underlying plastocyanin-cytochrome f electron transfer investigated via site-specific linear and two-dimensional infrared spectroscopy. Office of Scientific and Technical Information (OSTI), July 2022. http://dx.doi.org/10.2172/1878605.

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