Imperial College London

Professor Bill Rutherford FRS

Faculty of Natural SciencesDepartment of Life Sciences

Chair in Biochemistry of Solar Energy
 
 
 
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Contact

 

+44 (0)20 7594 5329a.rutherford Website

 
 
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Location

 

702Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Publication Type
Year
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255 results found

BEIJER C, RUTHERFORD AW, 1987, THE IRON-QUINONE ACCEPTOR COMPLEX IN RHODOSPIRILLUM-RUBRUM CHROMATOPHORES STUDIED BY ELECTRON-PARAMAGNETIC-RES, BIOCHIMICA ET BIOPHYSICA ACTA, Vol: 890, Pages: 169-178, ISSN: 0006-3002

Journal article

Mathis P, Rutherford AW, 1987, The Primary Reactions of Photosystems I and II of Algae and Higher Plants, New Comprehensive Biochemistry, Vol: 15, Pages: 63-96, ISSN: 0167-7306

This chapter discusses the primary reactions of photosystems I and II of algae and higher plants. In photosynthetic organisms, the “primary reactions” fulfil the objective of converting the energy of light into a primary form of chemical energy which lasts for a time compatible with ordinary biochemical processes—that is, milliseconds. In these reactions, a rather large fraction, approximately 40%, of the photon energy is stored as chemical free energy. The primary reactions can be viewed from two major perspectives. Firstly, from a photochemical point of view: pigment molecules are excited to their lowest excited singlet state, which reacts in an electron transfer reaction, the first step of a process of charge separation. Secondly, from a biochemical point of view the reactions take place in highly organized complexes, the reaction centres, which are made up of several classes of molecules that cooperate in fulfilling complementary roles, such as: architectural support, light absorption, energy transfer and electron transfer. All oxygenic organisms, ranging from cyanobacteria to algae and higher plants, contain photosystem I (PS I) and PS II reaction centres, with only minor variations in spite of their large taxonomic and ecological diversity. © 1987, Elsevier B.V. All rights reserved.

Journal article

VERMAAS WFJ, WILLIAMS JGK, RUTHERFORD AW, MATHIS P, ARNTZEN CJet al., 1986, GENETICALLY ENGINEERED MUTANT OF THE CYANOBACTERIUM SYNECHOCYSTIS 6803 LACKS THE PHOTOSYSTEM-II CHLOROPHYLL-BINDING PROTEIN CP-47, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 83, Pages: 9474-9477, ISSN: 0027-8424

Journal article

ZIMMERMANN JL, RUTHERFORD AW, 1986, PHOTOREDUCTANT-INDUCED OXIDATION OF FE-2+ IN THE ELECTRON-ACCEPTOR COMPLEX OF PHOTOSYSTEM-II, BIOCHIMICA ET BIOPHYSICA ACTA, Vol: 851, Pages: 416-423, ISSN: 0006-3002

Journal article

VOLKER M, RENGER G, RUTHERFORD AW, 1986, EFFECTS OF TRYPSIN UPON ELECTRON-PARAMAGNETIC-RES SIGNALS ARISING FROM COMPONENTS OF THE DONOR SIDE OF PHOTOSYSTEM-II, BIOCHIMICA ET BIOPHYSICA ACTA, Vol: 851, Pages: 424-430, ISSN: 0006-3002

Journal article

Ono T, Zimmermann JL, Inoue Y, Rutherford AWet al., 1986, EPR evidence for a modified S-state transition in chloride-depleted Photosystem II, BBA - Bioenergetics, Vol: 851, Pages: 193-201, ISSN: 0005-2728

The role of chloride on the S-state transition in spinach Photosystem II (PS II) particles was investigated by EPR spectroscopy at low temperature and the following results were obtained. (1) After excitation by continuous light at 200 K, chloride-depleted particles did not show the EPR multiline signal associated with the S2 state, but only showed the broad signal at g = 4.1. The S2 multiline signal was completely restored upon chloride repletion. (2) In the absence of chloride the S2 multiline signal was not induced by a single flash excitation at 0°C. However, upon addition of chloride after the flash the signal was developed in darkness. (3) The amplitude of the multiline S2 signal thus developed upon chloride addition after flash illumination did not show oscillations dependent upon flash number. These results indicate that the O2-evolving complex in chloride-depleted PS II membranes is able to store at least one oxidizing equivalent, a modified S2 state, which does not give rise to the multiline signal. Addition of chloride converts this oxidizing equivalent to the normal S2 state which gives rise to the multiline signal. The modified S2 state is more stable than the normal S2 state, showing decay kinetics about 20-times slower than those of the normal S2 state, and the formation of higher S states is blocked. © 1986.

Journal article

ONO T, ZIMMERMANN JL, INOUE Y, RUTHERFORD AWet al., 1986, ELECTRON-PARAMAGNETIC-RES EVIDENCE FOR A MODIFIED S-STATE TRANSITION IN CHLORIDE-DEPLETED PHOTOSYSTEM-II, BIOCHIMICA ET BIOPHYSICA ACTA, Vol: 851, Pages: 193-201, ISSN: 0006-3002

Journal article

ZIMMERMANN JL, RUTHERFORD AW, 1986, ELECTRON-PARAMAGNETIC RESONANCE PROPERTIES OF THE S-2 STATE OF THE OXYGEN-EVOLVING COMPLEX OF PHOTOSYSTEM-II, BIOCHEMISTRY, Vol: 25, Pages: 4609-4615, ISSN: 0006-2960

Journal article

RUTHERFORD AW, 1986, HOW CLOSE IS THE ANALOGY BETWEEN THE REACTION CENTER OF PHOTOSYSTEM-II AND THAT OF PURPLE BACTERIA, BIOCHEMICAL SOCIETY TRANSACTIONS, Vol: 14, Pages: 15-17, ISSN: 0300-5127

Journal article

RUTHERFORD AW, ACKER S, 1986, ORIENTATION OF THE PRIMARY DONOR IN ISOLATED PHOTOSYSTEM-II REACTION CENTERS STUDIED BY ELECTRON-PARAMAGNETIC RESONANCE, BIOPHYSICAL JOURNAL, Vol: 49, Pages: 101-102, ISSN: 0006-3495

Journal article

Rutherford AW, 1985, Orientation of EPR signals arising from components in Photosystem II membranes, BBA - Bioenergetics, Vol: 807, Pages: 189-201, ISSN: 0005-2728

EPR signals arising from components in oriented multilayers of Photosystem II (PS II) membranes have been studied and the following results have been obtained. (1) The EPR signals arising from the primary semiquinone-iron complex (Q-AFe) were highly oriented, with features at g = 1.90, g = 1.82 and g = 1.66 showing maxima when the membranes were perpendicular to the magnetic field. (2) The EPR signal, arising from the reduced pheophytin acceptor interacting with Q-AFe, showed an orientation-dependent splitting, ranging from 39 G when the membranes were parallel to the magnetic field to 27 G when the membranes were perpendicular to the magnetic field. (3) The S2 multiline signal associated with the O2-evolving enzyme showed an orientation dependence. This was most marked as position shifts in the low-field wings of the spectrum. These effects indicate that the component is oriented within the membrane and has some magnetically anisotropic character. (4) The component at g {reversed tilde equals} 4, though to be due to an oxidized charge carrier close to S2, showed a slight orientation dependence in its amplitude, but a significant orientation-dependent field-position shift was present, indicating that this is a magnetically anisotropic centre with a fixed geometry in the membrane. (5) Cytochrome b-559 in its oxidized form showed large highly oriented signals. The gz 2.97 feature was maximum when the membranes were oriented parallel to the magnetic field, while the gy 2.22 was maximum when the membrane plane was perpendicular to the magnetic field. This indicates that the haem plane is perpendicular to the plane of the membrane, in agreement with previous reports using chloroplasts. Ageing of the sample brings about a change from low- to high-spin state accompanied by a change in orientation of the haem relative to the membrane (from perpendicular to approximately 45°). (6) Signal II slow, which is present in the dark and which arises from a component which acts a

Journal article

ZIMMERMANN JL, RUTHERFORD AW, 1985, THE O2-EVOLVING OF PHOTOSYSTEM .2. RECENT ADVANCES, PHYSIOLOGIE VEGETALE, Vol: 23, Pages: 425-434, ISSN: 0031-9368

Journal article

RUTHERFORD AW, 1985, ORIENTATION OF ELECTRON-PARAMAGNETIC-RES SIGNALS ARISING FROM COMPONENTS IN PHOTOSYSTEM-II MEMBRANES, BIOCHIMICA ET BIOPHYSICA ACTA, Vol: 807, Pages: 189-201, ISSN: 0006-3002

Journal article

RUTHERFORD AW, AGALIDIS I, REISSHUSSON F, 1985, MANGANESE-QUINONE INTERACTIONS IN THE ELECTRON-ACCEPTOR REGION OF BACTERIAL PHOTOSYNTHETIC REACTION CENTERS, FEBS LETTERS, Vol: 182, Pages: 151-157, ISSN: 0014-5793

Journal article

RUTHERFORD AW, HEATHCOTE P, 1985, PRIMARY PHOTOCHEMISTRY IN PHOTOSYSTEM .1., PHOTOSYNTHESIS RESEARCH, Vol: 6, Pages: 295-316, ISSN: 0166-8595

Journal article

RENGER G, RUTHERFORD AW, VOLKER M, 1985, EVIDENCE FOR RESISTANCE OF THE MICROENVIRONMENT OF THE PRIMARY PLASTOQUINONE ACCEPTOR (QA-.FE-2+) TO MILD TRYPSINIZATION IN PS-II PARTICLES, FEBS LETTERS, Vol: 185, Pages: 243-247, ISSN: 0014-5793

Journal article

Rutherford AW, Zimmermann JL, 1984, A new EPR signal attributed to the primary plastosemiquinone acceptor in Photosystem II, BBA - Bioenergetics, Vol: 767, Pages: 168-175, ISSN: 0005-2728

A study of signals, light-induced at 77 K in O2-evolving Photosystem II (PS II) membranes showed that the EPR signal that has been attributed to the semiquinone-iron form of the primary quinone acceptor, Q-AFe, at g = 1.82 was usually accompanied by a broad signal at g = 1.90. In some preparations, the usual g = 1.82 signal was almost completely absent, while the intensity of the g = 1.90 signal was significantly increased. The g = 1.90 signal is attributed to a second EPR form of the primary semiquinone-iron acceptor of PS II on the basis of the following evidence. (1) The signal is chemically and photochemically induced under the same conditions as the usual g = 1.82 signal. (2) The extent of the signal induced by the addition of chemical reducing agents is the same as that photochemically induced by illumination at 77 K. (3) When the g = 1.82 signal is absent and instead the g = 1.90 signal is present, illumination at 200 K of a sample containing a reducing agent results in formation of the characteristic split pheophytin- signal, which is thought to arise from an interaction between the photoreduced pheophytin acceptor and the semiquinone-iron complex. (4) Both the g = 1.82 and g = 1.90 signals disappear when illumination is given at room temperature in the presence of a reducing agent. This is thought to be due to a reduction of the semiquinone to the nonparamagnetic quinol form. (5) Both the g = 1.90 and g = 1.82 signals are affected by herbicides which block electron transfer between the primary and secondary quinone acceptors. It was found that increasing the pH results in an increase of the g = 1.90 form, while lowering the pH favours the g = 1.82 form. The change from the g = 1.82 form to the g = 1.90 form is accompanied by a splitting change in the split pheophytin- signal from approx. 42 to approx. 50 G. Results using chloroplasts suggest that the g = 1.90 signal could represent the form present in vivo. © 1984.

Journal article

Zimmermann JL, Rutherford AW, 1984, EPR studies of the oxygen-evolving enzyme of Photosystem II, BBA - Bioenergetics, Vol: 767, Pages: 160-167, ISSN: 0005-2728

The light-induced EPR multiline signal is studied in O2-evolving PS II membranes. The following results are reported: (1) Its amplitude is shown to oscillate with a period of 4, with respect to the number of flashes given at room temperature (maxima on the first and fifth flashes). (2) Glycerol enhances the signal intensity. This effect is shown to come from changes in relaxation properties rather than an increase in spin concentration. (3) Deactivation experiments clearly indicate an association with the S2 state of the water-oxidizing enzyme. A signal at g = 4.1 with a linewidth of 360 G is also reported and it is suggested that this arises from an intermediate donor between the S states and the reaction centre. This suggestion is based on the following observations: (1) The g = 4.1 signal is formed by illumination at 200 K and not by flash excitation at room temperature, suggesting that it arises from an intermediate unstable under physiological conditions. (2) The formation of the g = 4.1 signal at 200 K does not occur in the presence of DCMU, indicating that more than one turnover is required for its maximum formation. (3) The g = 4.1 signal decreases in the dark at 220 K probably by recombination with Q-AFe. This recombination occurs before the multiline signal decreases, indicating that the g = 4.1 species is less stable than S2. (4) At short times, the decay of the g = 4.1 signal corresponds with a slight increase in the multiline S2 signal, suggesting that the loss of the g = 4.1 signal results in the disappearance of a magnetic interaction which diminishes the multiline signal intensity. (5) Tris-washed PS II membranes illuminated at 200 K do not exhibit the signal. © 1984.

Journal article

Vermaas WFJ, Rutherford AW, 1984, EPR measurements on the effects of bicarbonate and triazine resistance on the acceptor side of Photosystem II, FEBS Letters, Vol: 175, Pages: 243-248, ISSN: 0014-5793

CO2 depletion leads to an approximately 10-fold increase in the light-induced EPR signal at g = 1.82, attributed to the QA- · Fe2+ complex, in Photosystem II-enriched thylakoid membrane fragments. Upon reconstitution with HCO3-the signal decreases to the size in control samples. The split pheophytin- signal is broader in control or reconstituted than in CO2-depleted samples. It is concluded that HCO2- strongly influences the localization and conformation of the QA- · Fe+ complex. The QA- · Fe2+ and split pheophytirr- EPR signals from triazine-resistant Brassica napus were virtually identical to those from triazine-susceptible samples, indicating that the change in the 32-kDa azidoatrazine-binding protein does not lead to a confonnational change of the Qa- · Fe2+ complex. © 1984.

Journal article

ZIMMERMANN JL, RUTHERFORD AW, 1984, ELECTRON-PARAMAGNETIC-RES STUDIES OF THE OXYGEN-EVOLVING ENZYME OF PHOTOSYSTEM-II, BIOCHIMICA ET BIOPHYSICA ACTA, Vol: 767, Pages: 160-167, ISSN: 0006-3002

Journal article

RUTHERFORD AW, ZIMMERMANN JL, 1984, A NEW ELECTRON-PARAMAGNETIC-RES SIGNAL ATTRIBUTED TO THE PRIMARY PLASTOSEMIQUINONE ACCEPTOR IN PHOTOSYSTEM-II, BIOCHIMICA ET BIOPHYSICA ACTA, Vol: 767, Pages: 168-175, ISSN: 0006-3002

Journal article

GOVINDJEE, NAKATANI HY, RUTHERFORD AW, INOUE Yet al., 1984, EVIDENCE FROM THERMO-LUMINESCENCE FOR BICARBONATE ACTION ON THE RECOMBINATION REACTIONS INVOLVING THE SECONDARY QUINONE ELECTRON-ACCEPTOR OF PHOTOSYSTEM-II, BIOCHIMICA ET BIOPHYSICA ACTA, Vol: 766, Pages: 416-423, ISSN: 0006-3002

Journal article

RUTHERFORD AW, ZIMMERMANN JL, MATHIS P, 1984, THE EFFECT OF HERBICIDES ON COMPONENTS OF THE PS-II REACTION CENTER MEASURED BY ELECTRON-PARAMAGNETIC-RES, FEBS LETTERS, Vol: 165, Pages: 156-162, ISSN: 0014-5793

Journal article

RUTHERFORD AW, INOUE Y, 1984, OSCILLATION OF DELAYED LUMINESCENCE FROM PS-II - RECOMBINATION OF S2QB- AND S3QB-, FEBS LETTERS, Vol: 165, Pages: 163-170, ISSN: 0014-5793

Journal article

MATHIS P, RUTHERFORD AW, 1984, EFFECT OF PHENOLIC HERBICIDES ON THE OXYGEN-EVOLVING SIDE OF PHOTOSYSTEM-II - FORMATION OF THE CAROTENOID CATION, BIOCHIMICA ET BIOPHYSICA ACTA, Vol: 767, Pages: 217-222, ISSN: 0006-3002

Journal article

RUTHERFORD AW, RENGER G, KOIKE H, INOUE Yet al., 1984, THERMO-LUMINESCENCE AS A PROBE OF PHOTOSYSTEM-II - THE REDOX AND PROTONATION STATES OF THE SECONDARY ACCEPTOR QUINONE AND THE O2-EVOLVING ENZYME, BIOCHIMICA ET BIOPHYSICA ACTA, Vol: 767, Pages: 548-556, ISSN: 0006-3002

Journal article

RUTHERFORD AW, GOVINDJEE, INOUE Y, 1984, CHARGE ACCUMULATION AND PHOTOCHEMISTRY IN LEAVES STUDIED BY THERMO-LUMINESCENCE AND DELAYED LIGHT-EMISSION, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, Vol: 81, Pages: 1107-1111, ISSN: 0027-8424

Journal article

VERMAAS WFJ, RUTHERFORD AW, 1984, ELECTRON-PARAMAGNETIC-RES MEASUREMENTS ON THE EFFECTS OF BICARBONATE AND TRIAZINE RESISTANCE ON THE ACCEPTOR SIDE OF PHOTOSYSTEM-II, FEBS LETTERS, Vol: 175, Pages: 243-248, ISSN: 0014-5793

Journal article

METZ JG, MILES D, RUTHERFORD AW, 1983, CHARACTERIZATION OF NUCLEAR MUTANTS OF MAIZE WHICH LACK THE CYTOCHROME-F/B-563 COMPLEX, PLANT PHYSIOLOGY, Vol: 73, Pages: 452-459, ISSN: 0032-0889

Journal article

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