C Neil Hunter

The University of Sheffield, Sheffield, England, United Kingdom

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Publications (248)1037.14 Total impact

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    Biochimica et Biophysica Acta (BBA) - Bioenergetics. 10/2014; 1837(10):1835–1846.
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    ABSTRACT: The cytochrome b6f (cytb6f) complex plays a central role in photosynthesis, coupling electron transport between photosystem II (PSII) and photosystem I to the generation of a transmembrane proton gradient used for the biosynthesis of ATP. Photosynthesis relies on rapid shuttling of electrons by plastoquinone (PQ) molecules between PSII and cytb6f complexes in the lipid phase of the thylakoid membrane. Thus, the relative membrane location of these complexes is crucial, yet remains unknown. Here, we exploit the selective binding of the electron transfer protein plastocyanin (Pc) to the lumenal membrane surface of the cytb6f complex using a Pc-functionalized atomic force microscope (AFM) probe to identify the position of cytb6f complexes in grana thylakoid membranes from spinach (Spinacia oleracea). This affinity-mapping AFM method directly correlates membrane surface topography with Pc-cytb6f interactions, allowing us to construct a map of the grana thylakoid membrane that reveals nanodomains of colocalized PSII and cytb6f complexes. We suggest that the close proximity between PSII and cytb6f complexes integrates solar energy conversion and electron transfer by fostering short-range diffusion of PQ in the protein-crowded thylakoid membrane, thereby optimizing photosynthetic efficiency.
    The Plant cell. 07/2014;
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    ABSTRACT: We describe a fast, simple method for the fabrication of re-usable, robust gold nanostructures over macroscopic (cm2) areas. A wide range of nanostructure morphologies is accessible in a combinatorial fashion. Self-assembled monolayers (SAMs) of alkylthiolates on chromium-primed polycrystalline gold films are patterned using a Lloyd's mirror interferometer and etched using mercaptoethylamine in ethanol in a rapid process that does not require access to clean-room facilities. The use of a Cr adhesion layer facilitates the cleaning of specimens by immersion in piranha solution, enabling their repeated re-use without significant change in their absorbance spectra over two years. A library of 200 different nanostructures was prepared, and found to exhibit a range of optical behavior. Annealing yielded structures with a uniformly high degree of crystallinity that exhibited strong plasmon bands. Using a combinatorial approach, correlations were established between the pre-annealing morphologies (determined by the fabrication conditions) and the post-annealing optical properties that enabled specimens to be prepared "to order" with a selected localized surface plasmon resonance. The refractive index sensitivity of gold nanostructures formed in this way was found to correlate closely with measurements reported for structures fabricated by other methods. Strong enhancements were observed in the Raman spectra of tetra-tert-butyl unsubstituted phthalocyanine (TTB-H2Pc). The shift in the position of the plasmon band after site-specific attachment of histidine-tagged green fluorescent protein (His-GFP) and bacteriochlorophyll a was measured for a range of nanostructured films, enabling the rapid identification of the one that yielded the largest shift. This approach offers a simple route to the production of durable, reusable, macroscopic arrays of gold nanostructures with precisely controllable morphologies.
    ACS Nano 07/2014; · 12.03 Impact Factor
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    ABSTRACT: A simple and robust nanolithographic method, that allows sub-100 nm chemical patterning on a range of oxide surfaces, was developed in order to fabricate nanoarrays of plant light harvesting LHCII complexes. The site-specific immobilization and the preserved functionality of the LHCII complexes were confirmed by fluorescence emission spectroscopy. Nanopatterned LHCII trimers could be reversibly switched between fluorescent and quenched states by controlling the detergent concentration in the imaging buffer. A three-fold quenching of the average fluorescence intensity was accompanied by a decrease in the average (amplitude weighted) fluorescence lifetime from approximately 2.24 ns to approximately 0.4 ns, attributed to the intrinsic ability of LHCII to switch between fluorescent and quenched states upon changes in its conformational state. The nanopatterning methodology was extended by immobilizing a second protein, the enhanced Green Fluorescent Protein (EGFP), onto LHCII-free areas of the chemically patterned surfaces. This very simple surface chemistry, which allows simultaneous selective immobilization and therefore sorting of the two types of protein molecules on the surface, is a key underpinning step towards the integration of LHCII into switchable biohybrid antenna constructs.
    Langmuir : the ACS journal of surfaces and colloids. 07/2014;
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    ABSTRACT: In this study, we use the photosynthetic purple bacterium Rhodobacter sphaeroides to find out how the acclimation of photosynthetic apparatus to growth conditions influence the rates of energy migration towards the reaction center traps and the efficiency of charge separation at the reaction centers. To answer these questions we measured the spectral and picosecond kinetic fluorescence responses as a function of excitation intensity in membranes prepared from cells grown under different illumination conditions. A kinetic model analysis yielded the microscopic rate constants that characterize the energy transfer and trapping inside the photosynthetic unit as well as the dependence of exciton trapping efficiency on the ratio of the peripheral LH2 and core LH1 antenna complexes, and on the wavelength of the excitation light. A high quantum efficiency of trapping over 80% was observed in most cases, which decreased toward shorter excitation wavelengths within the near infrared absorption band. At a fixed excitation wavelength the efficiency declines with the LH2/LH1 ratio. From the perspective of the ecological habitat of the bacteria the higher population of peripheral antenna facilitates growth under dim light even though the energy trapping is slower in low light adapted membranes. The similar values for the trapping efficiencies in all samples imply a robust photosynthetic apparatus that functions effectively at a variety of light intensities.
    Biochimica et biophysica acta. 06/2014;
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    ABSTRACT: Most of the chlorophylls and bacteriochlorophylls utilised for light harvesting by phototrophic organisms carry an ethyl group at the C8 position of the molecule, the product of a C8-vinyl reductase acting on a chlorophyll/bacteriochlorophyll biosynthetic precursor. Two unrelated classes of C8-vinyl reductase are known to exist, BciA and BciB, found in the purple phototroph Rhodobacter sphaeroides and the cyanobacterium Synechocystis sp. PCC6803, respectively. We constructed strains of each bacterium with the native C8-vinyl reductase swapped for the other class of the enzyme, and combined these replacements with a series of deletions of the native bch and chl genes. In vivo data indicate that the preferred substrates for both classes of the enzyme is C8-vinyl chlorophyllide, with C8-vinyl protochlorophyllide reduced only under conditions in which this pigment accumulates as a result of perturbed formation of chlorophyllide.
    The Biochemical journal. 06/2014;
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    ABSTRACT: A new cysteine-based methacrylic monomer (CysMA) was conveniently synthesized via selective thia-Michael addition of a commercially-available methacrylate-acrylate precursor in aqueous solution without recourse to protecting group chemistry. Poly(cysteine methacrylate) (PCysMA) brushes were grown from the surface of silicon wafers by atom-transfer radical polymerization. Brush thicknesses of ca. 27 nm were achieved within 270 min at 20 oC. Each CysMA residue comprises a primary amine and a carboxylic acid. Surface zeta potential and atomic force microscopy (AFM) studies of the pH-responsive PCysMA brushes confirm that they are highly extended either below pH 2 or above pH 9.5, since they possess either cationic or anionic character, respectively. At intermediate pH, PCysMA brushes are zwitterionic. At physiological pH, they exhibit excellent resistance to biofouling and negligible cytotoxicity. PCysMA brushes undergo photodegradation: AFM topographical imaging indicates significant mass loss from the brush layer, while XPS studies confirm that exposure to UV radiation produces surface aldehyde sites that can be subsequently derivatized with amines. UV exposure using a photomask yielded sharp, well-defined micro-patterned PCysMA brushes functionalized with aldehyde groups that enable conjugation to green fluorescent protein (GFP). Nano-patterned PCysMA brushes were obtained using interference lithography and confocal microscopy again confirmed the selective conjugation of GFP. Finally, PCysMA undergoes complex base-catalyzed degradation in alkaline solution, leading to the elimination of several small molecules. However, good long-term chemical stability was observed when PCysMA brushes were immersed in aqueous solution at physiological pH.
    Journal of the American Chemical Society 06/2014; · 10.68 Impact Factor
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    ABSTRACT: The Tat system transports folded proteins across the bacterial plasma membrane. The mechanism is believed to involve coalescence of a TatC-containing unit with a separate TatA complex, but the full translocation complex has never been visualised and the assembly process is poorly defined. We report the analysis of the Bacillus subtilis TatAyCy system, which occurs as separate TatAyCy and TatAy complexes at steady state, using single-particle electron microscopy (EM) and advanced atomic force microscopy (AFM) approaches. We show that a P2A mutation in the TatAy subunit leads to apparent super-assembly of Tat complexes. Purification of TatCy-containing complexes leads to a large increase in the TatA:TatC ratio, suggesting that TatAy(P2A) complexes may have attached to the TatAyCy complex. EM and AFM analysis shows that the wild-type TatAyCy complex purifies as roughly spherical complexes of 9-16 nm diameter, whereas the P2A mutation leads to accumulation of large (up to 500 nm long) fibrils that are chains of numerous complexes. Time lapsed AFM imaging, recorded on fibrils under liquid, shows that they adopt a variety of tightly curved conformations, with radii of curvature of 10 - 12 nm comparable to the size of single TatAy(P2A) complexes. The combined data indicate that the mutation leads to super-assembly of TatAy(P2A) complexes and we propose that an individual TatAy(P2A) complex assembles initially with a TatAy(P2A)Cy complex, after which further TatAy(P2A) complexes attach to each other. The data further suggest that the N-terminal extracytoplasmic domain of TatAy plays an essential role in Tat complex interactions.
    Biochimica et biophysica acta. 05/2014;
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    ABSTRACT: Macromolecular membrane assemblies of chlorophyll-protein complexes efficiently harvest and trap light energy for photosynthesis. To investigate the delivery of chlorophylls to the newly synthesized photosystem apoproteins, a terminal enzyme of chlorophyll biosynthesis, chlorophyll synthase (ChlG), was tagged in the cyanobacterium Synechocystis PCC 6803 (Synechocystis) and used as bait in pull-down experiments. We retrieved an enzymatically active complex comprising ChlG and the high-light-inducible protein HliD, which associates with the Ycf39 protein, a putative assembly factor for photosystem II, and with the YidC/Alb3 insertase. 2D electrophoresis and immunoblotting also provided evidence for the presence of SecY and ribosome subunits. The isolated complex contained chlorophyll, chlorophyllide, and carotenoid pigments. Deletion of hliD elevated the level of the ChlG substrate, chlorophyllide, more than 6-fold; HliD is apparently required for assembly of FLAG-ChlG into larger complexes with other proteins such as Ycf39. These data reveal a link between chlorophyll biosynthesis and the Sec/YidC-dependent cotranslational insertion of nascent photosystem polypeptides into membranes. We expect that this close physical linkage coordinates the arrival of pigments and nascent apoproteins to produce photosynthetic pigment-protein complexes with minimal risk of accumulating phototoxic unbound chlorophylls.
    The Plant Cell 03/2014; · 9.25 Impact Factor
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    Daniel P. Canniffe, C. Neil Hunter
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    ABSTRACT: Bacteriochlorophyll b has the most red-shifted absorbance maximum of all naturally-occurring photopigments. It has a characteristic ethylidene group at the C8 position in place of the more common ethyl group, the product of a C8-vinyl reductase, which is carried by the majority of chlorophylls and bacteriochlorophylls used in photosynthesis. The subsequent and first step exclusive to bacteriochlorophyll biosynthesis, the reduction of the C7 = C8 bond, is catalyzed by chlorophyllide oxidoreductase. It has been demonstrated that the enzyme from bacteriochlorophyll a-utilizing bacteria can catalyze the formation of compounds carrying an ethyl group at C8 from both ethyl- and vinyl-carrying substrates, indicating a surprising additional C8-vinyl reductase function, while the enzyme from organisms producing BChl b could only catalyze C7 = C8 reduction with a vinyl substrate, but this product carried an ethylidene group at the C8 position. We have replaced the native chlorophyllide oxidoreductase-encoding genes of Rhodobacter sphaeroides with those from Blastochloris viridis, but the switch from bacteriochlorophyll a to b biosynthesis is only detected when the native conventional C8-vinyl reductase is absent. We propose a non-enzymatic mechanism for ethylidene group formation based on the absence of cellular C8-vinyl reductase activity.
    Biochimica et Biophysica Acta (BBA) - Bioenergetics. 01/2014;
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    ABSTRACT: The Tat system transports folded proteins across the bacterial plasma membrane. The mechanism is believed to involve coalescence of a TatC-containing unit with a separate TatA complex, but the full translocation complex has never been visualised and the assembly process is poorly defined. We report the analysis of the Bacillus subtilis TatAyCy system, which occurs as separate TatAyCy and TatAy complexes at steady state, using single-particle electron microscopy (EM) and advanced atomic force microscopy (AFM) approaches. We show that a P2A mutation in the TatAy subunit leads to apparent super-assembly of Tat complexes. Purification of TatCy-containing complexes leads to a large increase in the TatA:TatC ratio, suggesting that TatAyP2A complexes may have attached to the TatAyCy complex. EM and AFM analysis shows that the wild-type TatAyCy complex purifies as roughly spherical complexes of 9-16 nm diameter, whereas the P2A mutation leads to accumulation of large (up to 500 nm long) fibrils that are chains of numerous complexes. Time lapsed AFM imaging, recorded on fibrils under liquid, shows that they adopt a variety of tightly curved conformations, with radii of curvature of 10 – 12 nm comparable to the size of single TatAyP2A complexes. The combined data indicate that the mutation leads to super-assembly of TatAyP2A complexes and we propose that an individual TatAyP2A complex assembles initially with a TatAyP2ACy complex, after which further TatAyP2A complexes attach to each other. The data further suggest that the N-terminal extracytoplasmic domain of TatAy plays an essential role in Tat complex interactions.
    Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 01/2014; · 4.81 Impact Factor
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    ABSTRACT: Photosynthesis converts absorbed solar energy to a protonmotive force, which drives ATP synthesis. The membrane network of chlorophyll–protein complexes responsible for light absorption, photochemistry and quinol (QH2) production has been mapped in the purple phototrophic bacterium Rhodobacter (Rba.) sphaeroides using atomic force microscopy (AFM), but the membrane location of the cytochrome bc1 (cytbc1) complexes that oxidise QH2 to quinone (Q) to generate a protonmotive force is unknown. We labelled cytbc1 complexes with gold nanobeads, each attached by a Histidine10 (His10)-tag to the C-terminus of cytc1. Electron microscopy (EM) of negatively stained chromatophore vesicles showed that the majority of the cytbc1 complexes occur as dimers in the membrane. The cytbc1 complexes appeared to be adjacent to reaction centre light-harvesting 1-PufX (RC-LH1-PufX) complexes, consistent with AFM topographs of a gold-labelled membrane. His-tagged cytbc1 complexes were retrieved from chromatophores partially solubilised by detergent; RC-LH1-PufX complexes tended to co-purify with cytbc1, whereas LH2 complexes became detached, consistent with clusters of cytbc1 complexes close to RC-LH1-PufX arrays, but not with a fixed, stoichiometric cytbc1-RC-LH1-PufX supercomplex. This information was combined with a quantitative mass spectrometry (MS) analysis of the RC, cytbc1, ATP synthase, cytaa3 and cytcbb3 membrane protein complexes, to construct an atomic-level model of a chromatophore vesicle comprising 67 LH2 complexes, 11 LH1-RC-PufX dimers & 2 RC-LH1-PufX monomers, 4 cytbc1 dimers and 2 ATP synthases. Simulation of the interconnected energy, electron and proton transfer processes showed a half-maximal ATP turnover rate for a light intensity equivalent to only 1% of bright sunlight. Thus, the photosystem architecture of the chromatophore is optimised for growth at low light intensities.
    Biochimica et Biophysica Acta 01/2014; · 4.66 Impact Factor
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    ABSTRACT: The first committed step in chlorophyll biosynthesis is catalysed by magnesium chelatase (E.C., which uses the free energy of ATP hydrolysis to insert a Mg2+ ion into the ring of protoporphyrin IX. We have characterised magnesium chelatase from the thermophilic cyanobacterium Thermosynechococcus elongatus. This chelatase is thermostable, with subunit melting temperatures between 55 and 63 ˚C and optimal activity at 50 ˚C. The T. elongatus chelatase (kcat of 0.16 µM min-1 ) shows a Michaelis-Menten type response to both Mg2+ (Km of 2.3 mM) and MgATP2- (Km of 0.8 mM). The response to porphyrin is more complex; porphyrin inhibits at high concentrations of ChlH, but when the concentration of ChlH is comparable to the other two subunits the response is of the Michaelis-Menten type (at 0.4 µM ChlH, Km is 0.2 µM). Hybrid magnesium chelatases containing a mixture of subunits from the mesophilic Synechocystis and Thermosynechococcus enzymes are active. We generated all six possible hybrid magnesium chelatases; the hybrid chelatase containing Thermosynechococcus ChlD and Synechocystis ChlI and ChlH is not cooperative towards Mg2+, in contrast to the Synechocystis magnesium chelatase. This loss of cooperativity reveals the significant regulatory role of Synechocystis ChlD.
    Biochemical Journal 10/2013; · 4.65 Impact Factor
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    ABSTRACT: Reaction center-light harvesting 1 (RC-LH1) complexes are the fundamental units of bacterial photosynthesis, which use solar energy to power the reduction of quinone to quinol prior to the formation of the proton gradient that drives ATP synthesis. The dimeric RC-LH1-PufX complex of Rhodobacter sphaeroides is composed of 64 polypeptides and 128 cofactors, including 56 LH1 bacteriochlorophyll a (BChl a) molecules that surround and donate energy to the two RCs. The 3D structure was determined to 8 Å by X-ray crystallography, and a model was built with constraints provided by electron microscopy (EM), nuclear magnetic resonance (NMR), mass spectrometry (MS), and site-directed mutagenesis. Each half of the dimer complex consists of a RC surrounded by an array of 14 LH1 αβ subunits, with two BChls sandwiched between each αβ pair of transmembrane helices. The N- and C-terminal extrinsic domains of PufX promote dimerization by interacting with the corresponding domains of an LH1 β polypeptide from the other half of the RC-LH1-PufX complex. Close contacts between PufX, an LH1 αβ subunit, and the cytoplasmic domain of the RC-H subunit prevent the LH1 complex from encircling the RC and create a channel connecting the RC QB site to an opening in the LH1 ring, allowing Q/QH2 exchange with the external quinone pool. We also identified a channel that connects the two halves of the dimer, potentially forming a long-range pathway for quinone migration along rows of RC-LH1-PufX complexes in the membrane. The structure of the RC-LH1-PufX complex explains the crucial role played by PufX in dimer formation, and it shows how quinone traffic traverses the LH1 complex as it shuttles between the RC and the cytochrome bc1 complex.
    Biochemistry 10/2013; · 3.38 Impact Factor
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    ABSTRACT: Self-assembled monolayers of alkylthiolates on gold and alkylsilanes on silicon dioxide have been patterned photocatalytically on sub-100 nm length-scales using both apertured near-field and apertureless methods. Apertured lithography was carried out by means of an argon ion laser (364 nm) coupled to cantilever-type near-field probes with a thin film of titania deposited over the aperture. Apertureless lithography was carried out with a helium-cadmium laser (325 nm), to excite titanium-coated, contact-mode atomic force microscope (AFM) probes. This latter approach is readily implementable on any commercial AFM system. Photodegradation occurred in both cases through the localized photocatalytic degradation of the monolayer. For alkanethiols, degradation of one thiol exposed the bare substrate, enabling refunctionalization of the bare gold by a second, contrasting thiol. For alkylsilanes, degradation of the adsorbate molecule provided a facile means for protein patterning. Lines were written in a protein-resistant film formed by the adsorption of oligo(ethylene glycol) trichlorosilanes on glass, leading to the formation of sub-100 nm adhesive, aldehyde-functionalized regions. These were derivatized with aminobutylnitrilotriacetic acid, and complexed with Ni2+, enabling the binding of histidine-labeled green fluorescent protein, which yielded bright fluorescence from 70-nm-wide lines that could be imaged clearly in a confocal microscope.
    ACS Nano 08/2013; · 12.03 Impact Factor
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    ABSTRACT: Chlorosomes, the major antenna complexes in green sulphur bacteria, filamentous anoxygenic phototrophs, and phototrophic acidobacteria, are attached to the cytoplasmic side of the inner cell membrane and contain thousands of bacteriochlorophyll (BChl) molecules that harvest light and channel the energy to membrane-bound reaction centres. Chlorosomes from phototrophs representing three different phyla, Chloroflexus (Cfx.) aurantiacus, Chlorobaculum (Cba.) tepidum and the newly discovered "Candidatus (Ca.) Chloracidobacterium (Cab.) thermophilum" were analysed using PeakForce Tapping atomic force microscopy (PFT-AFM). Gentle PFT-AFM imaging in buffered solutions that maintained the chlorosomes in a near-native state revealed ellipsoids of variable size, with surface bumps and undulations that differ between individual chlorosomes. Cba. tepidum chlorosomes were the largest (133×57×36 nm; 141,000 nm(3) volume), compared with chlorosomes from Cfx. aurantiacus (120×44×30 nm; 84,000 nm(3)) and "Ca. Cab. thermophilum" (99×40×31 nm; 65,000 nm(3)). Reflecting the contributions of thousands of pigment-pigment stacking interactions to the stability of these supramolecular assemblies, analysis by nanomechanical mapping shows that chlorosomes are highly stable and that their integrity is disrupted only by very strong forces of 1000-2000 pN. AFM topographs of "Ca. Cab. thermophilum" chlorosomes that had retained their attachment to the cytoplasmic membrane showed that this membrane dynamically changes shape and is composed of protrusions of up to 30 nm wide and 6 nm above the mica support, possibly representing different protein domains. Spectral imaging revealed significant heterogeneity in the fluorescence emission of individual chlorosomes, likely reflecting the variations in BChl c homolog composition and internal arrangements of the stacked BChls within each chlorosome.
    Biochimica et Biophysica Acta 07/2013; · 4.66 Impact Factor
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    ABSTRACT: Electron transfer pathways in photosynthesis involve interactions between membrane-bound complexes such as reaction centres with an extrinsic partner. In this study, the biological specificity of electron transfer between the reaction centre-light-harvesting 1-PufX complex and its extrinsic electron donor, cytochrome c 2, formed the basis for mapping the location of surface-attached RC-LH1-PufX complexes using atomic force microscopy (AFM). This nano-mechanical mapping method used an AFM probe functionalised with cyt c 2 molecules to quantify the interaction forces involved, at the single-molecule level under native conditions. With surface-bound RC-His12-LH1-PufX complexes in the photo-oxidised state, the mean interaction force with cyt c 2 is approximately 480 pN with an interaction frequency of around 66 %. The latter value lowered 5.5-fold when chemically reduced RC-His12-LH1-PufX complexes are imaged in the dark to abolish electron transfer from cyt c 2 to the RC. The correspondence between topographic and adhesion images recorded over the same area of the sample shows that affinity-based AFM methods are a useful tool when topology alone is insufficient for spatially locating proteins at the surface of photosynthetic membranes.
    Photosynthesis Research 03/2013; · 3.15 Impact Factor
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    ABSTRACT: Native length bacterial light-harvesting peptides carrying covalently attached designer chromophores have been created that self-assemble with native bacteriochlorophyll a (BChl a) to afford stable antennas with enhanced spectral coverage. Native (or native-like) [small alpha]- and [small beta]-peptides interact with each other and BChl a to form a heterodimeric ([small alpha][small beta]-dyad) unit that can then oligomerize to form biohybrid analogs of the bacterial core light-harvesting complex (LH1). Pairs of distinct synthetic chromophores were incorporated in [small alpha][small beta]-dyads at selected distances from the BChl a target site (position 0). Two designs were explored. One design used green-yellow absorbing/emitting Oregon Green at the -34 position (toward the N-terminus relative to the BChl a coordination site) of [small beta] and orange-red absorbing/emitting Rhodamine Red at the -20 position of [small alpha], which combine with BChl a to give homogeneous oligomers. A second design used two different [small beta]-peptide conjugates, one with Oregon Green at the -34 position and the second with a near-infrared absorbing/emitting synthetic bacteriochlorin at the -14 position, which combine with [small alpha] and BChl a to give a heterogeneous mixture of oligomers. The designs afford antennas with [similar]45 to [similar]60 pigments, provide enhanced spectral coverage across the visible and near-infrared regions relative to native antennas, and accommodate pigments at remote sites that contribute to solar light harvesting via an energy-transfer cascade. The efficiencies of energy-transfer to the BChl a target in the biohybrid antennas are comparable to native antennas, as revealed by static and time-resolved absorption and emission studies. The results show that the biohybrid approach, where designer chromophores are integrated via semisynthesis with native-like scaffolding, constitutes a versatile platform technology for rapid prototyping of antennas for solar energy capture without the laborious synthesis typically required for creating artificial photosynthetic light-harvesting architectures.
    Chemical Science. 01/2013; 4(10):3924-3933.

Publication Stats

5k Citations
1,037.14 Total Impact Points


  • 1989–2014
    • The University of Sheffield
      • • Department of Molecular Biology and Biotechnology
      • • Department of Chemistry
      • • Centre for Photosynthesis Research (Robert Hill Institute)
      Sheffield, England, United Kingdom
  • 2005–2012
    • University of Tartu
      • Institute of Physics
      Tartu, Tartumaa, Estonia
  • 2006–2011
    • University of Illinois, Urbana-Champaign
      • • Beckman Institute for Advanced Science and Technology
      • • Department of Physics
      Urbana, IL, United States
    • Jagiellonian University
      Cracovia, Lesser Poland Voivodeship, Poland
  • 1998–2011
    • VU University Amsterdam
      • • Department of Physics and Astronomy
      • • Faculty of Sciences
      • • Division of Theoretical Chemistry
      Amsterdam, North Holland, Netherlands
    • University of Glasgow
      • School of Chemistry
      Glasgow, Scotland, United Kingdom
  • 1994–2011
    • University of Amsterdam
      • • Faculty of Science
      • • Department of Physics and Astronomy
      • • Department of Biophysics
      Amsterdam, North Holland, Netherlands
  • 2004–2010
    • Universiteit Twente
      • Group of Biomechanical Engineering
      Enschede, Overijssel, Netherlands
  • 2009
    • Aix-Marseille Université
      • Laboratoire d'Ingénierie des Systèmes Macromoléculaires (UMR 7255 LISM)
      Marseille, Provence-Alpes-Cote d'Azur, France
  • 2008
    • Leiden University
      Leyden, South Holland, Netherlands
  • 1999–2008
    • Rutgers, The State University of New Jersey
      • • Department of Chemical Biology
      • • Institute of Marine and Coastal Sciences
      • • Department of Molecular Biology and Biochemistry
      New Brunswick, NJ, United States
    • Tokyo University of Agriculture and Technology
      Edo, Tōkyō, Japan
  • 2002–2003
    • Ludwig-Maximilian-University of Munich
      • Division of Botany
      München, Bavaria, Germany
  • 1996–2002
    • Lund University
      • Department of Physical Chemistry
      Lund, Skane, Sweden
  • 2001
    • University Hospital München
      München, Bavaria, Germany
  • 1997
    • French National Centre for Scientific Research
      Lutetia Parisorum, Île-de-France, France
  • 1989–1994
    • Umeå University
      Umeå, Västerbotten, Sweden
  • 1988–1993
    • Imperial Valley College
      Imperial, California, United States
  • 1992
    • Queen Mary, University of London
      Londinium, England, United Kingdom
  • 1986–1989
    • Imperial College London
      Londinium, England, United Kingdom
  • 1979–1985
    • University of Bristol
      • Medical School
      Bristol, ENG, United Kingdom