C Neil Hunter

The University of Sheffield, Sheffield, England, United Kingdom

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Publications (265)1238.07 Total impact

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    Nature Plants 11/2015; DOI:10.1038/NPLANTS.2015.176
  • Amanda A Brindley · Nathan B P Adams · C Neil Hunter · James D Reid ·
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    ABSTRACT: Magnesium chelatase catalyzes the first committed step in chlorophyll biosynthesis by inserting a Mg(2+) ion into proto-porphyrin IX in an ATP-dependent manner. The cyanobacterial (Synechocystis) and higher plant chelatases exhibit a complex cooperative response to free magnesium, while the chelatases from Thermosynechococcus elongatus and photosynthetic bacteria do not. To investigate the basis for this cooperativity we constructed a series of chimeric ChlD proteins using N-terminal, central and C-terminal domains from Synechocystis and Thermosynechococcus. We show that five glutamic acid residues in the C terminal domain play a major role in this process.
    Biochemistry 10/2015; DOI:10.1021/acs.biochem.5b01080 · 3.02 Impact Factor
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    ABSTRACT: In oxygenic phototrophs, chlorophylls, hemes and bilins are synthesized by a common branched pathway. Given the phototoxic nature of tetrapyrroles, this pathway must be tightly regulated and an important regulatory role is attributed to Mg-chelatase enzyme at the branching between the heme and chlorophyll pathway. Gun4 is a porphyrin-binding protein known to stimulate in vitro the Mg-chelatase activity but how the Gun4-porphyrin complex acts in the cell was unknown. To address this issue we first performed simulations to determine the porphyrin-docking mechanism to the cyanobacterial Gun4 structure. After correcting crystallographic loop contacts, we determined the binding site for Mg-protoporphyrin IX. Molecular modeling revealed that the orientation of α6/α7 loop is critical for the binding and the magnesium ion held within the porphyrin is coordinated by Asn211 residue. We also identified the basis for stronger binding in the Gun4-1 variant and for weaker binding in the W192A mutant. The W192A-Gun4 was further characterized in Mg-chelatase assay showing that tight porphyrin-binding in Gun4 facilitates its interaction with the Mg-chelatase ChlH subunit. Finally, we introduced the W192A mutation into cells and show that the Gun4-porphyrin complex is important for the accumulation of ChlH and for channeling metabolites into the chlorophyll biosynthetic pathway.
    Journal of Biological Chemistry 10/2015; DOI:10.1074/jbc.M115.664987 · 4.57 Impact Factor
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    ABSTRACT: The mature architecture of the photosynthetic membrane of the purple phototroph Rhodobacter sphaeroides has been characterised to a level where an atomic-level membrane model is available, but the roles of the putative assembly proteins LhaA and PucC in establishing this architecture are unknown. Here we investigate the assembly of light-harvesting LH2 and reaction centre-light-harvesting1-PufX (RC-LH1-PufX) photosystem complexes using spectroscopy, pull-downs, native gel electrophoresis, quantitative mass spectrometry and fluorescence lifetime microscopy to characterise a series of lhaA and pucC mutants. LhaA and PucC are important for specific assembly of LH1 or LH2 complexes, respectively, but they are not essential; the few LH1 subunits found in ΔlhaA mutants assemble to form normal RC-LH1-PufX core complexes showing that, once initiated, LH1 assembly round the RC is cooperative and proceeds to completion. LhaA and PucC form oligomers at sites of initiation of membrane invagination; LhaA associates with RCs, bacteriochlorophyll synthase (BchG), the protein translocase subunit YajC, and the YidC membrane protein insertase. These associations within membrane nanodomains likely maximise interactions between pigments newly arriving from BchG and nascent proteins within the SecYEG-SecDF-YajC-YidC assembly machinery, thereby coordinating pigment delivery, the co-translational insertion of LH polypeptides and their folding and assembly to form photosynthetic complexes.
    Molecular Microbiology 09/2015; DOI:10.1111/mmi.13235 · 4.42 Impact Factor
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    ABSTRACT: The photosynthetic membranes of the filamentous anoxygenic phototroph Roseiflexus castenholzii have been studied with electron microscopy, atomic force microscopy, and biochemistry. Electron microscopy of the light-harvesting reaction center complex produced a 3D model that aligns with the solved crystal structure of the RC-LH1 from Thermochromatium tepidum with the H subunit removed. Atomic force microscopy of the whole membranes yielded a picture of the supramolecular organization of the major proteins in the photosynthetic electron transport chain. The results point to a loosely packed membrane without accessory antenna proteins or higher order structure.
    Photosynthesis Research 07/2015; DOI:10.1007/s11120-015-0179-9 · 3.50 Impact Factor
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    ABSTRACT: The photocatalytic self-cleaning characteristics of titania facilitate the fabrication of re-useable templates for protein nanopatterning. Titania nanostructures were fabricated over square centimeter areas by interferometric lithography (IL) and nanoimprint lithography (NIL). Using a Lloyd's mirror two-beam interferometer, self-assembled monolayers of alkylphosphonates adsorbed on the native oxide of a Ti film were patterned by photocatalytic nanolithography. In regions exposed to a maximum in the interferogram, the monolayer was removed by photocatalytic oxidation. In regions exposed to an intensity minimum, the monolayer remained intact. After exposure, the sample was etched in piranha solution to yield Ti nanostructures with widths as small as 30 nm. NIL was performed by using a silicon stamp to imprint a spin-cast film of titanium dioxide resin; after calcination and reactive ion etching, TiO2 nanopillars were formed. For both fabrication techniques, subsequent adsorption of an oligo(ethylene glycol) functionalized trichlorosilane yielded an entirely passive, protein-resistant surface. Near-UV exposure caused removal of this protein-resistant film from the titania regions by photocatalytic degradation, leaving the passivating silane film intact on the silicon dioxide regions. Proteins labeled with fluorescent dyes were adsorbed to the titanium dioxide regions, yielding nanopatterns with bright fluorescence. Subsequent near-UV irradiation of the samples removed the protein from the titanium dioxide nanostructures by photocatalytic degradation facilitating the adsorption of a different protein. The process was repeated multiple times. These simple methods appear to yield durable, re-useable samples that may be of value to laboratories that require nanostructured biological interfaces but do not have access to the infrastructure required for nanofabrication.
    ACS Nano 06/2015; 9(6). DOI:10.1021/acsnano.5b01636 · 12.88 Impact Factor
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    ABSTRACT: We describe a facile approach for nanopatterning of photosynthetic light-harvesting complexes over macroscopic areas, and use optical spectroscopy to demonstrate retention of native properties by both site-specifically and non-specifically attached photosynthetic membrane proteins. A Lloyd’s mirror dual-beam interferometer was used to expose self-assembled mono-layers of amine-terminated alkylthiolates on gold to laser irradiation. Following exposure, photo-oxidized adsorbates were replaced by oligo(ethy-lene glycol) terminated thiols, and the remaining intact amine-functionalized regions were used for attachment of the major light-harvesting chlorophyll– protein complex from plants, LHCII. These amine patterns could bederivatized with nitrilotriacetic acid (NTA), so that polyhistidine-tagged bacteriochloro-phyll–protein complexes from phototrophic bacteria could be attached with a defined surface orientation. By varying parameters such asthe angle between the interfering beams and the laser irradiation dose, it was possible to vary the period and widths of NTA and amine-functionalized lines on the surfaces; periods varied from 1200 to 240 nm and linewidths as small as 60 nm (l/4) were achieved. This level of control over the surface chemistry was reflected in the surface topology of the protein nanostructures imaged by atomic force microscopy; fluorescence imaging and spectral measurements demonstrated that the surface-attached proteins had retained their native functionality.
    Interface focus: a theme supplement of Journal of the Royal Society interface 05/2015; 5(4):20150005-20150005. DOI:10.1098/rsfs.2015.0005 · 2.63 Impact Factor
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    ABSTRACT: Light-harvesting 2 complexes (LH2) from a genetically modified strain of the purple photosynthetic bacterium Rhodobacter (Rba.) sphaeroides were studied using static and ultrafast optical methods and resonance Raman spectroscopy. Carotenoid synthesis in the Rba. sphaeroides strain was engineered to redirect carotenoid production away from spheroidene into the spirilloxanthin synthesis pathway. The strain assembles LH2 antennas with substantial amounts of spirilloxanthin (total double-bond conjugation length N = 13) if grown anaerobically and of keto-bearing long-chain analogs [2-ketoanhydrorhodovibrin (N = 13), 2-ketospirilloxanthin (N = 14) and 2,2'-diketospirilloxanthin (N = 15)] if grown semi-aerobically (with ratios that depend on growth conditions). We present the photophysical, electronic, and vibrational properties of these carotenoids, both isolated in organic media and assembled within LH2 complexes. Measurements of excited-state energy transfer to the array of excitonically coupled bacteriochlorophyll a molecules (B850) show that the mean lifetime of the first singlet excited state (S1) of the long-chain (N ≥ 13) carotenoids does not change appreciably between organic media and the protein environment. In each case, the S1 state appears to lie lower in energy than that of B850. The energy-transfer yield is ~0.4 in LH2 (from the strain grown aerobically or semi-aerobically), which is less than half that achieved for LH2 that contains short-chain (N ≤ 11) analogues. Collectively, the results suggest that the S1 excited state of the long-chain (N ≥ 13) carotenoids participates little if at all in carotenoid-to-BChl a energy transfer, which occurs predominantly via the carotenoid S2 excited state in these antennas. Copyright © 2015. Published by Elsevier B.V.
    Biochimica et Biophysica Acta 04/2015; 374(6-7). DOI:10.1016/j.bbabio.2015.04.001 · 4.66 Impact Factor
  • Tomoko Horibe · Pu Qian · C. Neil Hunter · Hideki Hashimoto ·
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    ABSTRACT: Stark absorption spectroscopy was applied to clarify the structural differences between carotenoids bound to the B800-820 and B800-850 LH2 complexes from a purple photosynthetic bacterium Phaeospirillum (Phs.) molischianum DSM120. The former complex is produced when the bacteria are grown under stressed conditions of low temperature and dim light. These two LH2 complexes bind carotenoids with similar composition, 10% lycopene and 80% rhodopin, each with the same number of conjugated C=C double bonds (n = 11). Quantitative classical and semi-quantum chemical analyses of Stark absorption spectra recorded in the carotenoid absorption region reveal that the absolute values of the difference dipole moments |Δμ| have substantial differences (2 [D/f]) for carotenoids bound to either B800-820 or B800-850 complexes. The origin of this striking difference in the |Δμ| values was analyzed using the X-ray crystal structure of the B800-850 LH2 complex from Phs. molischianum DSM119. Semi-empirical molecular orbital calculations predict structural deformations of the major carotenoid, rhodopin, bound within the B800-820 complex. We propose that simultaneous rotations around neighboring C=C and C-C bonds account for the differences in the 2 [D/f] of the |Δμ| value. The plausible position of the rotation is postulated to be located around C21-C24 bonds of rhodopin. Copyright © 2014. Published by Elsevier Inc.
    Archives of Biochemistry and Biophysics 12/2014; 572. DOI:10.1016/j.abb.2014.12.015 · 3.02 Impact Factor
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    ABSTRACT: Magnesium chelatase (MgCH) initiates chlorophyll biosynthesis by catalysing the ATP-dependent insertion of Mg2+ into protoporphyrin. This large enzyme complex comprises ChlH, I and D subunits, with I and D involved in ATP hydrolysis, and H the protein that handles the substrate and product. The 148 kDa ChlH subunit has a globular N-terminal domain attached by a narrow linker to a hollow cage-like structure. Following deletion of this ~18 kDa domain from the Thermosynechoccus elongatus ChlH, we used single particle reconstruction to show that the apo- and porphyrin-bound forms of the mutant subunit consist of a hollow globular protein with three connected lobes; superposition of the mutant and native ChlH structures shows that, despite the clear absence of the N-terminal 'head' region, the rest of the protein appears to be correctly folded. Analyses of dissociation constants shows that the ΔN159ChlH mutant retains the ability to bind protoporphyrin and the Gun4 enhancer protein, although the addition of I and D subunits yields an extremely impaired active enzyme complex. Addition of the Gun4 enhancer protein, which stimulates MgCH activity significantly especially at low Mg2+ concentrations, partially reactivates the ΔN159ChlH-I-D mutant enzyme complex, suggesting that the binding site or sites for Gun4 on H do not wholly depend on the N-terminal domain.
    Biochemical Journal 12/2014; 464(3):315-22. DOI:10.1042/BJ20140463 · 4.40 Impact Factor
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    ABSTRACT: Carotenoids protect the photosynthetic apparatus against harmful radicals arising from the presence of both light and oxygen. They also act as accessory pigments for harvesting solar energy, and are required for stable assembly of many light-harvesting complexes. In the phototrophic bacterium Rhodobacter (Rba.) sphaeroides phytoene desaturase (CrtI) catalyses three sequential desaturations of the colourless carotenoid phytoene, extending the number of conjugated carbon-carbon double bonds, N, from three to nine and producing the yellow carotenoid neurosporene; subsequent modifications produce the yellow/red carotenoids spheroidene/spheroidenone (N=10/11). Genomic crtI replacements were used to swap the native three-step Rba. sphaeroides CrtI for the four-step Pantoea agglomerans enzyme, which re-routed carotenoid biosynthesis and culminated in the production of 2,2'-diketo-spirilloxanthin under semi-aerobic conditions. The new carotenoid pathway was elucidated using a combination of HPLC and mass spectrometry. Premature termination of this new pathway by inactivating crtC or crtD produced strains with lycopene or rhodopin as major carotenoids. All of the spirilloxanthin series carotenoids are accepted by the assembly pathways for LH2 and RC-LH1-PufX complexes. The efficiency of carotenoid-to-bacteriochlorophyll energy transfer for 2,2'-diketo-spirilloxanthin (15 conjugated CC bonds; N=15) in LH2 complexes is low, at 35%. High energy transfer efficiencies were obtained for neurosporene (N=9; 94%), spheroidene (N=10; 96%) and spheroidenone (N=11; 95%), whereas intermediate values were measured for lycopene (N=11; 64%), rhodopin (N=11; 62%) and spirilloxanthin (N=13; 39%). The variety and stability of these novel Rba. sphaeroides antenna complexes make them useful experimental models for investigating the energy transfer dynamics of carotenoids in bacterial photosynthesis. Copyright © 2014. Published by Elsevier B.V.
    Biochimica et Biophysica Acta (BBA) - Bioenergetics 10/2014; 1847(2):189-201. DOI:10.1016/j.bbabio.2014.10.004 · 5.35 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 10/2014; 1837(10). DOI:10.1016/j.bbabio.2014.07.011 · 5.35 Impact Factor
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    ABSTRACT: In the purple phototrophic bacterium Rhodobacter sphaeroides, many protein complexes congregate within the membrane to form operational photosynthetic units consisting of arrays of light-harvesting LH2 complexes and monomeric and dimeric reaction center (RC)-light-harvesting 1 (LH1)-PufX “core” complexes. Each half of a dimer complex consists of a RC surrounded by 14 LH1 αβ subunits, with two bacteriochlorophylls (Bchls) sandwiched between each αβ pair of transmembrane helices. We used atomic force microscopy (AFM) to investigate the assembly of single molecules of the RC-LH1-PufX complex using membranes prepared from LH2-minus mutants. When the RC and PufX components were also absent, AFM revealed a series of LH1 variants where the repeating α1β1(Bchl)2 units had formed rings of variable size, ellipses, and spirals and also arcs that could be assembly products. The spiral complexes occur when the LH1 ring has failed to close, and short arcs are suggestive of prematurely terminated LH1 complex assembly. In the absence of RCs, we occasionally observed captive proteins enclosed by the LH1 ring. When production of LH1 units was restricted by lowering the relative levels of the cognate pufBA transcript, we imaged a mixture of complete RC-LH1 core complexes, empty LH1 rings, and isolated RCs, leading us to conclude that once a RC associates with the first α1β1(Bchl)2 subunit, cooperative associations between subsequent subunits and the RC tend to drive LH1 ring assembly to completion.
    Journal of Biological Chemistry 09/2014; 289(43). DOI:10.1074/jbc.M114.596585 · 4.57 Impact Factor
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    Matthew P Johnson · Cvetelin Vasilev · John D Olsen · C Neil Hunter ·
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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; 26(7). DOI:10.1105/tpc.114.127233 · 9.34 Impact Factor
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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; 8(8). DOI:10.1021/nn5014319 · 12.88 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 07/2014; 30(28). DOI:10.1021/la501483s · 4.46 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 07/2014; 1837(10). DOI:10.1016/j.bbabio.2014.02.003 · 4.66 Impact Factor
  • Matthew Johnson · Cvetelin Vasilev · John D. Olsen · C. Neil Hunter ·

    Biochimica et Biophysica Acta (BBA) - Bioenergetics 07/2014; 1837:e122. DOI:10.1016/j.bbabio.2014.05.326 · 5.35 Impact Factor

Publication Stats

9k Citations
1,238.07 Total Impact Points


  • 1989-2015
    • The University of Sheffield
      • • Department of Molecular Biology and Biotechnology
      • • Centre for Photosynthesis Research (Robert Hill Institute)
      Sheffield, England, United Kingdom
  • 1980-2008
    • Rutgers, The State University of New Jersey
      • Department of Chemical Biology
      New Brunswick, NJ, United States
  • 2007
    • University Hospital München
      München, Bavaria, Germany
  • 2006
    • Jagiellonian University
      Cracovia, Lesser Poland Voivodeship, Poland
  • 2000
    • University of Glasgow
      Glasgow, Scotland, United Kingdom
  • 1998
    • VU University Amsterdam
      • Division of Theoretical Chemistry
      Amsterdam, North Holland, Netherlands
  • 1995
    • University of Amsterdam
      • Department of Physics and Astronomy
      Amsterdam, North Holland, Netherlands
  • 1994
    • University of California, Berkeley
      • Lawrence Berkeley Laboratory
      Berkeley, California, United States
  • 1988-1993
    • Imperial Valley College
      • Department of Pure and Applied Biology
      Imperial, California, United States
  • 1986-1989
    • Imperial College London
      Londinium, England, United Kingdom
  • 1985
    • University of Pennsylvania
      • Department of Biochemistry and Biophysics
      Filadelfia, Pennsylvania, United States
  • 1979-1985
    • University of Bristol
      • Medical School
      Bristol, England, United Kingdom