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Topic: Plastocyanin

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	Degradation of Plastocyanin in Copper-deficient Chlamydomonas reinhardtii -- Li and Merchant 270 (40): 23504 -- ...
		To understand the mechanism of plastocyanin degradation in vivo, the purified apoprotein was characterized relative to the holoprotein with respect to conformation and protease susceptibility.
		In the case of plastocyanin, the degradative activity is presumed to be lumen-localized, or at least thylakoid membrane-associated, since the fully processed form of the protein serves as the substrate for degradation.
		The peak at 597 nm is characteristic of copper-containing plastocyanin.
	www.jbc.org /cgi/content/full/270/40/23504 (6571 words)

	copper
		The general questions: In 1979, Paul Wood noted that Chlamydomonas cells could use either plastocyanin (a blue copper protein) or cytochrome c6 (a heme protein) for photosynthesis in vivo; the choice between them is determined by the supply of copper in the growth medium.
		The pattern of plastocyanin, cytochrome c6 and coprogen oxidase accumulation is normal in all crt1 strains indicating that the CRT1 does not encode a regulatory component; rather we propose that it defines a hitherto unknown aspect of photosystem I biochemistry.
		Since plastocyanin is the major sink for copper in the green algae (which lack a Cu/Zn superoxide dismutase and other abundant copper proteins), its degradation in copper-deficiency would ensure the re-distribution of this essential trace element to cytochrome oxidase in the respiratory pathway.
	www.chem.ucla.edu /dept/Faculty/copper.html (1062 words)

	Plastocyanin - Wikipedia, the free encyclopedia
		Plastocyanin is an important copper-containing protein involved in electron-transfer.
		In plant plastocyanins, acidic residues are located on either side of a highly conserved tyrosine.
		In cyanobacteria, the distribution of charged residues on the surface is different from eukaryotic plastocyanins and variations among different bacterial species is large.
	en.wikipedia.org /wiki/Plastocyanin (352 words)

	Plastocyanin
		The structure was determined from a crystal specimen that was perfectly twinned by hemihedry (twinning fraction of 1/2).
		Plastocyanin acts as the electron donor to PSI in photosynthesis in higher plants and some algae.
		Cytochrome c6 and plastocyanin are functionally interchangeable in species that can express both proteins.
	www.doe-mbi.ucla.edu /People/Yeates/Gallery/PC.html (89 words)

	Research Interests: Brian F. Volkman
		The solution structure of the plastocyanin from from the photosynthetic prokaryote Prochlorothrix hollandica has been determined by homonuclear 1H NMR spectroscopy and torsion angle dynamics, in a collaboration with Dr. Charles Babu and Dr. George S. Bullerjahn (Bowling Green State University).
		NMR Structure of the plastocyanin from Prochlorothrix hollandica.
		Plastocyanin (PC) is a small (~10 kDa), Type 1 copper protein that functions as an electron donor to Photosystem I (PSI) from cytochrome (cyt) f in both chloroplast systems and in some strains of cyanobacteria.
	www.nmrfam.wisc.edu /~volkman/research/plast.html (498 words)

	Plastocyanin and photosystem I
		Plastocyanin (Pc) is a small (10.5 kDa) Cu-containing protein which acts as an electron carrier between the cytochrome b
		To answer this we make site-specific mutations in regions that are thought to be important for the function of plastocyanin, in the "northern" hydrophobic patch and in the "eastern" acidic patches.
		(1997) The involvement of the two acidic patches of spinach plastocyanin in the reaction with photosystem 1.
	www.bcbp.gu.se /~orjan/res/pc-ps1-e.html (988 words)

	Sabeeha Merchant - Copper
		Accordingly, copper enzymes are found in electron transfer pathways, such as respiration (cytochrome oxidase) and photosynthesis (plastocyanin), and in enzymes/proteins that bind oxygen, such as oxidases (ferroxidase) and oxygen transport proteins (hemocyanin).
		Plastocyanin, a photosynthetic electron transfer catalyst, is the most abundant copper protein in these organisms.
		The degradation of plastocyanin, which is the most abundant copper protein in the Chlamydomonas cell, is important in the copper-deficient cell for re-allocation of copper to cytochrome oxidase, for which there are no effective “back up” mechanisms.
	www.chem.ucla.edu /dept/Faculty/merchant/copper.html (1632 words)

	Surface interactions in the complex between cytochrome f and the E43Q/D44N and E59K/E60Q plastocyanin double mutants as ...
		Gross, E.L. and Curtiss, A. The interaction of nitrotyrosine-83 plastocyanin with cytochromes f and c: pH dependence and the effect of an additional negative charge on plastocyanin.
		Guss, J.M. and Freeman, H.C. Structure of oxidized poplar plastocyanin at 1.6 A resolution.
		Ubbink, M., Ejdebäck, M., Karlsson, B.G., and Bendall, D.S. The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics.
	www.proteinscience.org /cgi/content/full/10/12/2623 (2502 words)

	SURVEYING MOLECULAR INTERACTIONS WITH DOT
		Significant electrostatic potentials are concentrated on one-fourth (969 square Ångstroms) of the plastocyanin surface, with the greatest negative potential centered on the tyrosine 83 hydroxyl within the acidic patch, and on one-eighth (632 square Ångstroms) of the cytochrome c surface, with the greatest positive potential centered near the exposed heme edge.
		Direct interactions of the exposed Cu ligand in plastocyanin with the cytochrome c heme edge were not unfavorable sterically or electrostatically, but the analysis suggested they should occur no faster than randomly, indicating that such an interaction is not the primary pathway for electron transfer.
		Plastocyanin (the stationary molecule) is on the left, cytochrome c on the right.
	www.sdsc.edu /CCMS/Papers/DOT_sc95.html (3956 words)

	Faculty of Biological Sciences at BGSU
		Secondly, we are examining the structural requirements for productive electron transport in photosynthesis by studying the protein-protein interactions occurring between the copper protein plastocyanin and its reaction partners (Photosystem I and cytochrome f).
		Photoprocesses in self-assembled cationic porphyrins and plastocyanin complexes: ligation of plastocyanin tyrosine 83 onto metalloporphyrins and electron transfer fluorescence quenching.
		Plastocyanin — cytochrome f interactions: the influence of hydrophobic patch mutants studied by NMR.
	www.bgsu.edu /departments/biology/people/faculty/bullerjahn.html (374 words)

	Elizabeth L. Gross' Publications (Site not responding. Last check: 2007-10-11)
		The interaction of nitrotyrosine-83 plastocyanin with cytochromes f and c: pH dependence and the effect of an additional negative charge on plastocyanin.
		Factor analysis of the near-ultraviolet absorption spectrum of plastocyanin using bilinear, trilinear, and quadrilinear models.
		The effect of ethylenediamine chemical modification of plastocyanin on the rate of cytochrome f oxidation and P700+ reduction.
	www.biosci.ohio-state.edu /~egross/writings.html (210 words)

	The Structure and Unusual pH Dependence of Plastocyanin from the Fern Dryopteris crassirhizoma. THE PROTONATION OF AN ...
		The Structure and Unusual pH Dependence of Plastocyanin from the Fern Dryopteris crassirhizoma.
		plastocyanin from the fern Dryopteris crassirhizoma are presented.
		In the reactions of Dryopteris plastocyanin with inorganic
	www.jbc.org /cgi/content/abstract/274/17/11817 (388 words)

	Ubbink group: Research: Plastocyanin & Cytochrome f
		In these complexes, the hydrophobic patch of plastocyanin binds near the haem of the cytochrome, resulting in a short electron transfer distance between the iron and the copper.
		In the plant complex, plastocyanin uses also extensive electrostatic interactions, with negative charges on plastocyanin and positive charges on the cytochrome f.
		In the complex from the cyanobacterium Phormidium laminosum, plastocyanin approaches in a 'head-on' fashion, resulting in an almost purely hydrophobic complex.
	wwwchem.leidenuniv.nl /metprot/ubbink/Projects_pcf.htm (219 words)

	CyanoNews Vol. 14, Number 1: ISPP - Mobile electron carriers
		The main carrier for the organism is plastocyanin when copper is present in the growth media.
		John Whitmarsh described the electron transport kinetics of a mutant deficient in cytochrome c6 (by deletion of petJ) and plastocyanin (by deprivation of copper) and of a double mutant deficient in cytochromes c6 and c-M (by mutation of petJ and cytM) and plastocyanin (by deprivation of copper).
		However, with the double mutant, the low levels of plastocyanin would not be high enough to support the degree of electron transfer observed, suggesting that there is yet another mobile electron carrier in Synechocystis.
	www.vcu.edu /cyanonews/V14/ispp-cyt.htm (525 words)

	References - plastocyanin - HORT640 - Metabolic Plant Physiology - Department of Horticulture and Landscape ...
		Clarke AK, Campbell D 1996 Inactivation of the petE gene for plastocyanin lowers photosynthetic capacity and exacerbates chilling-induced photoinhibition in the cyanobacterium Synechococcus.
		Kindle KL 1998 Amino-terminal and hydrophobic regions of the Chlamydomonas reinhardtii plastocyanin transit peptide are required for efficient protein accumulation in vivo.
		Schottler MA, Kirchhoff H, Weis E 2004 The role of plastocyanin in the adjustment of the photosynthetic electron transport to the carbon metabolism in tobacco.
	www.hort.purdue.edu /rhodcv/hort640c/referen/plastoc.htm (784 words)

	Plastocyanin 2 Abstract (Site not responding. Last check: 2007-10-11)
		Self-consistent analysis of the absorption band and resulting resonance Raman excitation profiles for each of the plastocyanins demonstrates that many of the derived molecular parameters are similar, including the zero-zero energy, the transition moment, and the homogeneous and inhomogeneous linewidths.
		These results demonstrate that the protein environment is strongly coupled to the copper site and that a significant portion of the protein, which is not involved in binding of redox partners, determines the copper site coordination geometry and resulting redox potential.
		An important result is that the mode-specific protein component of the reorganization energy on the 20 fs timescale is sensitive to protein composition differences that are at least 8 A from the charge transfer site.
	www.chem.ualberta.ca /~gloppnow/pc2short.htm (187 words)

	BioMed Central \| Full text \| Functionally specified protein signatures distinctive for each of the different blue ...
		The blue copper proteins chosen for the study were plantacyanin, plastocyanin, cucumber basic protein, stellacyanin, dicyanin, umecyanin, uclacyanin, cusacyanin, rusticyanin, sulfocyanin, halocyanin, azurin, pseudoazurin, amicyanin and nitrite reductase which were identified in both eukaryotes and prokaryotes.
		Plastocyanins are found both in eukaryotes and prokaryotes.
		From Table 4 it is seen that plastocyanin has cyt b-heme (PS00192), cyt b QO(PS00193), photosystem1 PSAAB (PS00419), photosystem1 PSAGK(PS01026), Reiske 1 (PS00199) and Reiske 11(PS00200) as the signatures.
	www.biomedcentral.com /1471-2105/5/127 (3492 words)

	General preparation. (via CobWeb/3.1 planetlab2.tamu.edu) (Site not responding. Last check: 2007-10-11)
		For plastocyanin, I will define two new types of residues: HIC, which will be a histidine coupled to a copper ion, and which will take the place of HIS 37 in the "real" sequence; and MEM, which is a modified methionine where the sulfur atom is of type "SM" rather than type "S".
		Since residue 84 in plastocyanin has the sulfur atom bonded to the copper ion, I changed its name from CYS to CYX.
		This is pretty easy for plastocyanin, since the two histidine side chains are both bound to copper through the ND1 nitrogen.
	amber.scripps.edu.cob-web.org:8888 /tutorial/plastocyanin/pcy-tutorial-sh-1.html (1299 words)

	UPenn - SAS - Biology - People - Faculty
		The long term goal here is to discover the signaling pathway, from the sensing mechanism to the target genes and proteins that determines the operation of the photosynthetic apparatus as a function of iron nutrition.
		To elucidate binding and electron transfer mechanisms between PSI and its electron transfer donors plastocyanin or cytochrome c6 we are using site-directed mutagenesis and biolistic transformation of Chlamydomonas reinhardtii to alter the chloroplast encoded reaction-center forming subunits PsaA and PsaB.
		The protein-protein interaction between the modified PSI complexes and endogenous donors plastocyanin or cytochrome c6, all purified from C. reinhardtii, are analyzed by flash absorption spectroscopy in cooperation with Prof.
	www.bio.upenn.edu /faculty/hippler (2019 words)

	INI : Abstracts : SMCW03 : Role of Charges on Cytochrome f from the Cyanobacterium Phormidium laminosum in its ... (Site not responding. Last check: 2007-10-11)
		The role of charge on the surface of cytochrome f from the cyanobacterium Phormidium laminosum in the reaction with plastocyanin was investigated in vitro using site-directed mutagenesis.
		The dependence of the bimolecular rate constant of reaction on ionic strength was determined for the reactions of the cytochrome f mutants with wild-type and mutant forms of plastocyanin.
		The kinetic evidence from this study and that of Schlarb-Ridley et al., 2002, appears to conflict with the NMR structure of the P. laminosum complex [Crowley, P., et al., 2001, J.Am.Chem.Soc., 123, 10444-10453], which suggests the absence of electrostatic interactions in the final complex.
	www.newton.cam.ac.uk /programmes/SMC/Posters3/hart.html (274 words)

	Two P-Type ATPases Are Required for Copper Delivery in Arabidopsis thaliana Chloroplasts -- Abdel-Ghany et al. 17 (4): ...
		The precursor of plastocyanin was used as a control for import and fractionation.
		Plastocyanin is active in the thylakoid lumen, and CSD2 is active
		The bands were identified as either holoplastocyanin or apoplastocyanin by comparison with control native gels (middle and bottom gels) on which purified plastocyanin (PC) was present in either the holo form (untreated) or the apo form (ascorbate + KCN treated).
	www.plantcell.org /cgi/content/full/17/4/1233 (8720 words)

	Functional relationship of cytochrome c6 and plastocyanin in Arabidopsis : Nature (Site not responding. Last check: 2007-10-11)
		Although protein components in the electron transport chain are largely conserved among plants, algae and prokaryotes, there is thought to be a major difference concerning a soluble protein in the thylakoid lumen.
		In contrast, only plastocyanin has been found to play the same role in higher plants.
		Genetic analysis demonstrated that neither plastocyanin nor Atc6 was absolutely essential for Arabidopsis growth and development.
	nature.com /nature/journal/v417/n6888/abs/417567a.html;jsessionid=36... (252 words)

	Gene Synthesis, Expression, and Mutagenesis of the Blue Copper Proteins Azurin and Plastocyanin -- Chang et al. 88 (4): ...
		The leader sequence for azurin has been placed before the genes directing plastocyanin and azurin transport to the periplasmic space when the genes are expressed in Escherichia coli.
		While the plastocyanin mutants do not appear to bind copper, the azurin variants all bind copper and show characteristic type I blue copper centers.
		In particular, the electronic spectra reflect the dominance of the charge transfer interaction between copper and the thiolate of Cys-112, being relatively insensitive to changes in Met-121 or His-46.
	www.pnas.org /cgi/content/abstract/88/4/1325 (353 words)

	Side-Chain Interactions in the Plastocyanin-Cytochrome f Complex
		Cytochrome f and plastocyanin are redox partners in the photosynthetic electron-transfer chain.
		Cytochrome f was added to plastocyanin up to 0.3 M equiv, and the plastocyanin proton chemical shifts were measured.
		Nineteen percent demonstrate significant chemical-shift changes and these protons are located in the hydrophobic patch (including the copper ligands) and the acidic patches of plastocyanin, demonstrating that both areas are part of the interface in the complex.
	pubs.acs.org /cgi-bin/abstract.cgi/bichaw/2000/39/i17/abs/bi992757c.html (354 words)

	Brownian dynamics simulations of the interaction of chlamydomonas cytochrome f with plastocyanin and cytochrome c(6) ... (Site not responding. Last check: 2007-10-11)
		Brownian dynamics simulations of the interaction of chlamydomonas cytochrome f with plastocyanin and cytochrome c(6)
		ABSTRACT The interaction of Chlamydomonas cytochrome f (cyt f) with either Chlamydomonas plastocyanin (PC) or Chlamydomonas cytochrome c^sub 6^ (cyt c^sub 6^) was studied using Brownian dynamics simulations.
		The two electron acceptors (PC and cyt c^sub 6^) were found to be essentially interchangeable despite a lack of sequence homology and different secondary structures ([beta]-sheet for PC and [alpha]-helix for cyt c^sub 6^).
	www.findarticles.com /p/articles/mi_qa3938/is_200309/ai_n9288691 (771 words)

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