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Journal articles on the topic 'Plastocyanine'

Author: Grafiati

Published: 4 June 2021

Last updated: 16 November 2024

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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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Crnogorac, Milan, and Nenad Kostic. "Effects of pH on kinetics of the structural rearrangement that gates the electron-transfer reaction between zinc cytochrome c and plastocyanin: Analysis of protonation states in a diprotein complex." Journal of the Serbian Chemical Society 68, no. 4-5 (2003): 327–37. http://dx.doi.org/10.2298/jsc0305327c.

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Electron transfer from zinc cytochrome c to copper(II)plastocyanin in the electrostatically- stabilized complex [Crnogorac MM, Shen C, Young S Hansson O, Kostic NM (1996) Biochemistry 35, 16465?74]. We study this rearrangement in four complexes Zncyt/pc(II), which zinc cytochrome c makes with the wild-type form and the single mutants Asp42Asn, Glu59Gln, and Glu60Gln of plastocyanin. The rate constant for the rearrangement, kF differs for the four forms of plastocyanin but is independent of pH from 5.4 to 9.0 in all four cases. That kF is affected by the single mutations but not by pH changes suggests that the residues Asp 42, Glu59, and Glu60 in the wild-type plastocyanin remain deprotonated (i.e., as anions) within the Zncyt/pc(II) complex throughout the pH range examined. This fact agrees with the notion that loss of salt bridges in the initial (redox-inactive) configuration of the complex is compensated by formation of new salt bridges in the rearranged (redox-active) configuration.

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12

Fitrasari, D., M. S. Arwansyah, K. Kawaguchi, A. Purqon, Suprijadi, and H. Nagao. "Theoretical Study of Dissociation Process of Plastocyanins by PaCS-MD Simulation." Journal of Physics: Conference Series 2207, no. 1 (March 1, 2022): 012021. http://dx.doi.org/10.1088/1742-6596/2207/1/012021.

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Abstract We present a procedure of calculation of free energy landscape of two proteins by using parallel cascade molecular dynamics (PaCS-MD) and multiple independent umbrella sampling (MIUS). The free energy landscape of two plastocyanins for association/dissociation process is investigate by using the present method. We find that binding free energy is around 1 kcal/mol and that the barrier energy at around the middle range between the equilibrium point and the dissociation state becomes about 1 kcal/mol from the association process. The present results suggest that the energy barrier may arise from hydrogen bonds between two plastocyanins. We also find that the effective interaction between two plastocyanins already vanishes at the distance of 2 Å from equilibrium state. The equilibrium point of the complex around 27.9 Å is a good agreement with the experimental result 27.8 Å

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13

Nishida, Yuzo. "Notes: Structural Features and Biological Functions in Blue Copper Proteins." Zeitschrift für Naturforschung C 42, no. 11-12 (December 1, 1987): 1358–60. http://dx.doi.org/10.1515/znc-1987-11-1239.

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A new idea that elucidates the electron carrier ability of plastocyanin (and of azurin) is proposed. It emphasizes the fact that two lobes of the d-orbital, where one unpaired electron of copper (II) ion lies, are not screened by the ligand atoms, which would facilitate the electron transfer between the d-orbital and the redox partners (cytochrom f and P-700 in the case of plastocyanin). Several evidences which support the above proposal are provided.

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14

Caccamo, Anna, Félix Vega de Luna, Khadija Wahni, Alexander N. Volkov, Jonathan Przybyla-Toscano, Antonello Amelii, Alexandre Kriznik, Nicolas Rouhier, Joris Messens, and Claire Remacle. "Ascorbate Peroxidase 2 (APX2) of Chlamydomonas Binds Copper and Modulates the Copper Insertion into Plastocyanin." Antioxidants 12, no. 11 (October 31, 2023): 1946. http://dx.doi.org/10.3390/antiox12111946.

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Recent phylogenetic studies have unveiled a novel class of ascorbate peroxidases called “ascorbate peroxidase-related” (APX-R). These enzymes, found in green photosynthetic eukaryotes, lack the amino acids necessary for ascorbate binding. This study focuses on the sole APX-R from Chlamydomonas reinhardtii referred to as ascorbate peroxidase 2 (APX2). We used immunoblotting to locate APX2 within the chloroplasts and in silico analysis to identify key structural motifs, such as the twin-arginine transport (TAT) motif for lumen translocation and the metal-binding MxxM motif. We also successfully expressed recombinant APX2 in Escherichia coli. Our in vitro results showed that the peroxidase activity of APX2 was detected with guaiacol but not with ascorbate as an electron donor. Furthermore, APX2 can bind both copper and heme, as evidenced by spectroscopic, and fluorescence experiments. These findings suggest a potential interaction between APX2 and plastocyanin, the primary copper-containing enzyme within the thylakoid lumen of the chloroplasts. Predictions from structural models and evidence from 1H-NMR experiments suggest a potential interaction between APX2 and plastocyanin, emphasizing the influence of APX2 on the copper-binding abilities of plastocyanin. In summary, our results propose a significant role for APX2 as a regulator in copper transfer to plastocyanin. This study sheds light on the unique properties of APX-R enzymes and their potential contributions to the complex processes of photosynthesis in green algae.

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15

Kong, Liangliang, and Neil M. Price. "Identification of copper-regulated proteins in an oceanic diatom, Thalassiosira oceanica 1005." Metallomics 12, no. 7 (2020): 1106–17. http://dx.doi.org/10.1039/d0mt00033g.

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16

Bertini, Ivano, Donald A. Bryant, Stefano Ciurli, Alexander Dikiy, Claudio O. Fernández, Claudio Luchinat, Niyaz Safarov, Alejandro J. Vila, and Jindong Zhao. "Backbone Dynamics of Plastocyanin in Both Oxidation States." Journal of Biological Chemistry 276, no. 50 (August 16, 2001): 47217–26. http://dx.doi.org/10.1074/jbc.m100304200.

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A model-free analysis based on15NR1,15NR2, and15N-1H nuclear Overhauser effects was performed on reduced (diamagnetic) and oxidized (paramagnetic) forms of plastocyanin fromSynechocystissp. PCC6803. The protein backbone is rigid, displaying a small degree of mobility in the sub-nanosecond time scale. The loops surrounding the copper ion, involved in physiological electron transfer, feature a higher extent of flexibility in the longer time scale in both redox states, as measured from D2O exchange of amide protons and from NH-H2O saturation transfer experiments. In contrast to the situation for other electron transfer proteins, no significant difference in the dynamic properties is found between the two redox forms. A solution structure was also determined for the reduced plastocyanin and compared with the solution structure of the oxidized form in order to assess possible structural changes related to the copper ion redox state. Within the attained resolution, the structure of the reduced plastocyanin is indistinguishable from that of the oxidized form, even though small chemical shift differences are observed. The present characterization provides information on both the structural and dynamic behavior of blue copper proteins in solution that is useful to understand further the role(s) of protein dynamics in electron transfer processes.

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17

Schöttler, Mark A., Claudia Flügel, Wolfram Thiele, Sandra Stegemann, and Ralph Bock. "The plastome-encoded PsaJ subunit is required for efficient Photosystem I excitation, but not for plastocyanin oxidation in tobacco." Biochemical Journal 403, no. 2 (March 26, 2007): 251–60. http://dx.doi.org/10.1042/bj20061573.

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The functions of several small subunits of the large photosynthetic multiprotein complex PSI (Photosystem I) are not yet understood. To elucidate the function of the small plastome-encoded PsaJ subunit, we have produced knockout mutants by chloroplast transformation in tobacco (Nicotiana tabacum). PsaJ binds two chlorophyll-a molecules and is localized at the periphery of PSI, close to both the Lhca2- and Lhca3-docking sites and the plastocyanin-binding site. Tobacco psaJ-knockout lines do not display a visible phenotype. Despite a 25% reduction in the content of redox-active PSI, neither growth rate nor assimilation capacity are altered in the mutants. In vivo, redox equilibration of plastocyanin and PSI is as efficient as in the wild-type, indicating that PsaJ is not required for fast plastocyanin oxidation. However, PsaJ is involved in PSI excitation: altered 77 K chlorophyll-a fluorescence emission spectra and reduced accumulation of Lhca3 indicate that antenna binding and exciton transfer to the PSI reaction centre are impaired in ΔpsaJ mutants. Under limiting light intensities, growth of ΔpsaJ plants is retarded and the electron-transport chain is far more reduced than in the wild-type, indicating that PSI excitation might limit electron flux at sub-saturating light intensities. In addition to defining in vivo functions of PsaJ, our data may also have implications for the interpretation of the crystal structure of PSI.

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18

Morand, Larry Z., Melinda K. Frame, Kim K. Colvert, Dale A. Johnson, David W. Krogmann, and Danny J. Davis. "Plastocyanin cytochrome f interaction." Biochemistry 28, no. 20 (October 1989): 8039–47. http://dx.doi.org/10.1021/bi00446a011.

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19

Detlefsen, David J., E. Pichersky, and V. L. Pecoraro. "Pre-plastocyanin fromLycopersicon esculentum." Nucleic Acids Research 17, no. 15 (1989): 6414–15. http://dx.doi.org/10.1093/nar/17.15.6414.

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20

Dimitrov, Mitko I., Anthony A. Donchev, and Tsezi A. Egorov. "Microheterogeneity of parsley plastocyanin." FEBS Letters 265, no. 1-2 (June 4, 1990): 141–45. http://dx.doi.org/10.1016/0014-5793(90)80904-w.

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21

Gross, Elizabeth L. "Plastocyanin: Structure and function." Photosynthesis Research 37, no. 2 (August 1993): 103–16. http://dx.doi.org/10.1007/bf02187469.

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22

Draheim, J. E., G. P. Anderson, R. L. Pan, L. M. Rellick, J. W. Duane, and E. L. Gross. "Conformational changes in plastocyanin." Archives of Biochemistry and Biophysics 237, no. 1 (February 1985): 110–17. http://dx.doi.org/10.1016/0003-9861(85)90259-0.

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23

Hibino, Takashi, A. Douwe de Boer, Peter J. Weisbeek, and Teruhiro Takabe. "Reconstitution of mature plastocyanin from precursor apo-plastocyanin expressed in Escherichia coli." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1058, no. 2 (June 1991): 107–12. http://dx.doi.org/10.1016/s0005-2728(05)80226-9.

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24

Church, W. B., T. P. J. Garrett, H. C. Freeman, and B. P. Schoenborn. "Neutron structure analysis of plastocyanin." Acta Crystallographica Section A Foundations of Crystallography 43, a1 (August 12, 1987): C13. http://dx.doi.org/10.1107/s0108767387085192.

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25

Dimitrov, Mitko I., Anthony A. Donchev, and Tsezi A. Egorov. "Twin plastocyanin dimorphism in tobacco." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1203, no. 2 (December 1993): 184–90. http://dx.doi.org/10.1016/0167-4838(93)90081-2.

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26

Miramar, M. Dolores, Luis A. Inda, Lígia M. Saraiva, and M. Luisa Peleato. "Plastocyanin/cytochromec6 interchange inScenedesmus vacuolatus." Journal of Plant Physiology 160, no. 12 (January 2003): 1483–86. http://dx.doi.org/10.1078/0176-1617-01009.

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27

Kilpatrick, L. K., and T. G. Spiro. "UVRR spectroscopy of parsley plastocyanin." Journal of Inorganic Biochemistry 36, no. 3-4 (August 1989): 244. http://dx.doi.org/10.1016/0162-0134(89)84287-4.

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28

Redinbo, Matthew R., Todd O. Yeates, and Sabeeha Merchant. "Plastocyanin: Structural and functional analysis." Journal of Bioenergetics and Biomembranes 26, no. 1 (February 1994): 49–66. http://dx.doi.org/10.1007/bf00763219.

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29

García-Cañas, Raquel, Joaquín Giner-Lamia, Francisco J. Florencio, and Luis López-Maury. "A protease-mediated mechanism regulates the cytochrome c6/plastocyanin switch in Synechocystis sp. PCC 6803." Proceedings of the National Academy of Sciences 118, no. 5 (January 25, 2021): e2017898118. http://dx.doi.org/10.1073/pnas.2017898118.

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After the Great Oxidation Event (GOE), iron availability was greatly decreased, and photosynthetic organisms evolved several alternative proteins and mechanisms. One of these proteins, plastocyanin, is a type I blue-copper protein that can replace cytochrome c6 as a soluble electron carrier between cytochrome b6f and photosystem I. In most cyanobacteria, expression of these two alternative proteins is regulated by copper availability, but the regulatory system remains unknown. Herein, we provide evidence that the regulatory system is composed of a BlaI/CopY-family transcription factor (PetR) and a BlaR-membrane protease (PetP). PetR represses petE (plastocyanin) expression and activates petJ (cytochrome c6), while PetP controls PetR levels in vivo. Using whole-cell extracts, we demonstrated that PetR degradation requires both PetP and copper. Transcriptomic analysis revealed that the PetRP system regulates only four genes (petE, petJ, slr0601, and slr0602), highlighting its specificity. Furthermore, the presence of petE and petRP in early branching cyanobacteria indicates that acquisition of these genes could represent an early adaptation to decreased iron bioavailability following the GOE.

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30

Christensen, H. E. M., L. S. Conrad, and J. Ulstrup. "Electron transfer in the plastocyanin/cytochrome F and the NO2-TYR83-plastocyanin/cytochrome F systems." Journal of Inorganic Biochemistry 43, no. 2-3 (August 1991): 94. http://dx.doi.org/10.1016/0162-0134(91)84090-v.

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31

Getov, V. I., G. R. Toromanov, G. K. Kostov, M. I. Dimitrov, and A. Ch Shosheva. "Reversible unfolding of poplar iso-plastocyanins." Journal of Thermal Analysis and Calorimetry 98, no. 3 (July 3, 2009): 877–83. http://dx.doi.org/10.1007/s10973-009-0141-1.

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32

Nordling, Margareta, Torbjörn Olausson, and Lennart G. Lundberg. "Expression of spinach plastocyanin inE. coli." FEBS Letters 276, no. 1-2 (December 10, 1990): 98–102. http://dx.doi.org/10.1016/0014-5793(90)80517-m.

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33

Kachalova, G. S., G. P. Bourenkov, H. D. Bartunik, M. I. Dimitrov, A. A. Donchev, and A. Ch Shosheva. "Crystal structure of poplar plastocyanin b." Acta Crystallographica Section A Foundations of Crystallography 58, s1 (August 6, 2002): c303. http://dx.doi.org/10.1107/s0108767302097118.

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34

Di Bilio, Angel J., Christopher Dennison, Harry B. Gray, Benjamin E. Ramirez, A. Geoffrey Sykes, and Jay R. Winkler. "Electron Transfer in Ruthenium-Modified Plastocyanin." Journal of the American Chemical Society 120, no. 30 (August 1998): 7551–56. http://dx.doi.org/10.1021/ja972625b.

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35

Suzuki, Shinnichiro, Satoshi Sawada, Akitsugu Nakahara, and Takuo Nakajima. "Spectroscopic characterization of plastocyanin from hornwort." Biochemical and Biophysical Research Communications 136, no. 2 (April 1986): 610–15. http://dx.doi.org/10.1016/0006-291x(86)90484-5.

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36

Wynn, R. Max, and Richard Malkin. "Interaction of plastocyanin with photosystem I: a chemical cross-linking study of the polypeptide that binds plastocyanin." Biochemistry 27, no. 16 (August 1988): 5863–69. http://dx.doi.org/10.1021/bi00416a007.

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37

Tröger, W., C. Lippert, T. Butz, K. Sigfridsson, Ö. Hansson, E. McLaughlin, R. Bauer, E. Danielsen, L. Hemmingsen, and M. J. Bjerrum. "Small Scale Intramolecular Flexibility in 111mCd-Plastocyanin." Zeitschrift für Naturforschung A 51, no. 5-6 (June 1, 1996): 431–36. http://dx.doi.org/10.1515/zna-1996-5-618.

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Abstract The effect of mutations in the vicinity of the putative electron transfer path on the metal center of the electron transfer protein plastocyanin (spinacea) is investigated by monitoring the nuclear quadrupole interaction of 111mCd in Cd-derivatives of the protein via time differential perturbed angular correlation. The spectra for the wild type protein and the mutants were rather similar. All spectra exhibit a peculiar line profile which points towards a small scale intramolecular flexibility of the metal center.

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38

Voelker, Rodger, Janet Mendel-Hartvig, and Alice Barkan. "Transposon-Disruption of a Maize Nuclear Gene, tha1, Encoding a Chloroplast SecA Homologue: In Vivo Role of cp-SecA in Thylakoid Protein Targeting." Genetics 145, no. 2 (February 1, 1997): 467–78. http://dx.doi.org/10.1093/genetics/145.2.467.

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A nuclear mutant of maize, tha1, which exhibited defects in the translocation of proteins across the thylakoid membrane, was described previously. A transposon insertion at the tha1 locus facilitated the cloning of portions of the tha1 gene. Strong sequence similarity with secA genes from bacteria, pea and spinach indicates that tha1 encodes a SecA homologue (cp-SecA). The tha1-ref allele is either null or nearly so, in that tha1 mRNA is undetectable in mutant leaves and cp-SecA accumulation is reduced ≥40-fold. These results, in conjunction with the mutant phenotype described previously, demonstrate that cp-SecA functions in vivo to facilitate the translocation of OEC33, PSI-F and plastocyanin but does not function in the translocation of OEC23 and OEC16. Our results confirm predictions for cp-Sed function made from the results of in vitro experiments and establish several new functions for cp-SecA, including roles in the targeting of a chloroplast-encoded protein, cytochrome f, and in protein targeting in the etioplast, a nonphotosynthetic plastid type. Our finding that the accumulation of properly targeted plastocyanin and cytochrome f in tha1-ref thylakoid membranes is reduced only a few-fold despite the near or complete absence of cp-SecA suggests that cp-SecA facilitates but is not essential in vivo for their translocation across the membrane.

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39

Schansker, Gert, Alaka Srivastava, Govindjee, and Reto J. Strasser. "Characterization of the 820-nm transmission signal paralleling the chlorophyll a fluorescence rise (OJIP) in pea leaves." Functional Plant Biology 30, no. 7 (2003): 785. http://dx.doi.org/10.1071/fp03032.

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Monitoring transmission changes at 820 nm, a measure of the redox states of plastocyanin (PC) and P700, is a good complementary technique for chlorophyll (chl) a fluorescence induction measurements. A thorough characterization of the properties of the 820-nm transmission kinetics during the first second after a dark-to-light transition is provided here for pea (Pisum sativum L.) leaves. The data indicate that plastocyanin in a dark-adapted leaf is in the reduced state. Three photosystem I (PSI)-related components, PC, P700 and ferredoxin, can contribute to the 820-nm transmission signal. The contribution of ferredoxin, however, is only approximately 5%, thus, it can be neglected for further analysis. Here, we show that by monitoring the sequential oxidation of PC and P700 during a far-red pulse and analysing the re-reduction kinetics it is possible to assign the three re-reduction components to PC (τ = 7–14 s) and P700 (τ = 35–55 ms and 1.2–1.6 s). Our data indicate that the faster re-reduction phase (τ =�35–55 ms) may represent a recombination reaction between P700+ and the acceptor side of PSI. This information made it possible to show that the ratio between the potential contributions of PC : P700 is 50 : 50 in pea and Camellia leaves and 40 : 60 in sugar beet leaves.

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40

Dimitrov, Mitko I., Caesii A. Egorov, Anthony A. Donchev, and Boris P. Atanasov. "Complete amino acid sequence of poplar plastocyaninb." FEBS Letters 226, no. 1 (December 21, 1987): 17–22. http://dx.doi.org/10.1016/0014-5793(87)80542-2.

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41

Li, Hong Hua, and Sabeeha Merchant. "Degradation of Plastocyanin in Copper-deficientChlamydomonas reinhardtii." Journal of Biological Chemistry 270, no. 40 (October 6, 1995): 23504–10. http://dx.doi.org/10.1074/jbc.270.40.23504.

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42

Suzuki, Shinnichiro, Takeshi Sakurai, and Takuo Nakajima. "Characterization of Plastocyanin Isolated From Brazilian Elodea." Plant and Cell Physiology 28, no. 5 (July 1987): 825–31. http://dx.doi.org/10.1093/oxfordjournals.pcp.a077363.

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43

Robinson, David, and Nicholas A. Besley. "Modelling the spectroscopy and dynamics of plastocyanin." Physical Chemistry Chemical Physics 12, no. 33 (2010): 9667. http://dx.doi.org/10.1039/c001805h.

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44

Rush, J. D., F. Levine, and W. H. Koppenol. "The electron-transfer site of spinach plastocyanin." Biochemistry 27, no. 16 (August 1988): 5876–84. http://dx.doi.org/10.1021/bi00416a009.

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45

Ejdebäck, Mikael, Anders Bergkvist, B. Göran Karlsson, and Marcellus Ubbink. "Side-Chain Interactions in the Plastocyanin−CytochromefComplex†." Biochemistry 39, no. 17 (May 2000): 5022–27. http://dx.doi.org/10.1021/bi992757c.

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46

Schmidt, Lars, Hans E. M. Christensen, and Pernille Harris. "Structure of plastocyanin from the cyanobacteriumAnabaena variabilis." Acta Crystallographica Section D Biological Crystallography 62, no. 9 (August 19, 2006): 1022–29. http://dx.doi.org/10.1107/s0907444906023638.

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47

Crowley, Peter B., Gottfried Otting, Beatrix G. Schlarb-Ridley, Gerard W. Canters, and Marcellus Ubbink. "Hydrophobic Interactions in a Cyanobacterial Plastocyanin−CytochromefComplex." Journal of the American Chemical Society 123, no. 43 (October 2001): 10444–53. http://dx.doi.org/10.1021/ja0112700.

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48

Hirota, Shun, Hisano Okumura, Takayo Kondoh, Noriaki Funasaki, Teruhiro Takabe, and Yoshihito Watanabe. "Reduction of plastocyanin by tyrosine-containing oligopeptides." Journal of Inorganic Biochemistry 100, no. 11 (November 2006): 1871–78. http://dx.doi.org/10.1016/j.jinorgbio.2006.07.009.

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49

Nakayama, H., H. A. O. Hill, and D. Datta. "Electrochemistry of small protein, plastocyanin and ferredoxin." Journal of Inorganic Biochemistry 51, no. 1-2 (July 1993): 43. http://dx.doi.org/10.1016/0162-0134(93)85081-i.

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50

Illerhaus, Jürgen, Lothar Altschmied, Jan Reichert, Elena Zak, Reinhold G. Herrmann, and Wolfgang Haehnel. "Dynamic Interaction of Plastocyanin with the CytochromebfComplex." Journal of Biological Chemistry 275, no. 23 (June 2, 2000): 17590–95. http://dx.doi.org/10.1074/jbc.275.23.17590.

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