Visiting Professors

Professor Peter Nicholls

Staff positionVisiting Professor
Telephone01206 872121

Curriculum Vitae
Date and Place of Birth: July 13, 1935; Southampton, England.

Citizenship: United Kingdom (Canadian Landed Immigrant).

Marital Status: Married (Freda Johnson, 1961)

Education and Degrees:
1956, B.A., St. John's College, University of Cambridge, U.K.

1959, Ph.D., St. John's College and Molteno Institute, University of Cambridge, U. K.

Reactions of Haemoproteins with Peroxides & Hydrogen Donors (Supervisor: David Keilin).

1976, Sc.D., Sidney Sussex College & Univ. Cambridge, U.K.

Academic positions held:
1959 - 1960, Research Associate: Oregon State College, Corvallis, Oregon, USA.

1960 - 1961, Research Fellow: University of Pennsylvania, Philadelphia, PA, USA.

1961 - 1963, Fellow: St. John's College, Cambridge, England.

1963 - 1969, Instructor, Assistant and Associate Professor, Dept. Biochemistry, State Univ. New York at Buffalo, NY, USA.

1970, Senior Research Fellow, Dept. Biochemistry, University of Bristol, England.

1971 - 1973, Senior Fellow in Medical Science, Sidney Sussex College, Cambridge, England.

1973 - 1975, Lektor in biochemistry, Odense University, Denmark.

1975 - 1997, Professor of Biological Sciences, Brock University, St. Catharines, ON, Canada.

1998 - present, Visiting Professor of Biological Sciences, University of Essex, UK.

Research interests
  • My research involves the haem proteins catalase especially the E. coli and beef liver enzymes, together with catalase-peroxidases;
  • as well as the mammalian and bacterial and cytochrome c oxidase
  • and also the fungal flavohaemoprotein cellobiose dehydrogenase.

The major interest of this laboratory is in oxidative enzymes and the bioenergetics of membrane systems. Together with Prof. Mike Wilson and Dr. Chris Cooper and their coworkers, I am studying catalase and cytochrome c oxidase, the latter both in detergent solution and in artificial (proteoliposomal) membrane systems. Like other large membrane enzymes of this kind, the oxidase lies at the interface between the molecular and microscopic worlds; therein lies the more general interest in pursuing its mechanisms of action - electron and proton transfer, and its mechanisms of control - by local and global gradients of pH and potential across the membrane. The determination of its structure by X-ray crystallography is now stimulating new and better focused work on function. Fatty acid and pH effects on the behaviour of oxidase proteoliposomes were the subject of a thesis by M. Sc. student Ivano Perin at Brock University.

Our other area of study is the comparative biology of catalases, especially the E. coli and beef liver enzymes - closely homologous evolutionarily, but showing substantial differences in reaction mechanism. Ligand reactions of the E. coli HPII enzyme were the subject of a thesis by Brock M. Sc. student Mary Maj.

I have a number of co-workers in these areas and collaborative relationships with laboratories in Italy, Austria and North America, and I would be pleased to receive applications from prospective students or visiting researchers on any of these subjects.

Other Interests
For the period 1995-1997 I was Vice-President of the Canadian Biophysical Society. The society has annual meetings devoted to biophysical topics, usually held in association with the Canadian Federation of Biological Societies (CFBS), but sometimes independently.

I am also immediate Past President of Science for Peace, the Canadian organization concerned with the responsibilities of science and scientists to ensure that scientific ideas and technology are used in humane and life-enhancing ways. Science for Peace engages in research, education and action for peace in a scientific context. The organization was founded by concerned Canadian academics in 1981 at the height of the Cold War. Despite the end or transformation of that War the development, the testing, and in some cases the actual use of a wide range of weapons whose existence is a result of science and technology has continued. Meanwhile some nations and groups remain in poverty and the global economy is under threat. Addressing these concerns may be more important than pursuing purely technical scientific ideas.

Teaching responsibilities

My teaching in biochemistry previously included courses in 'Bioenergetics' and 'Proteins and Enzymes'. I now contribute to the "Issues in Cell & Molecular Biology" courses (BS304 & BS305) recently focussing on the social problems of vaccination programmes.

I am interested in the history of science. I previously examined William Walwyn's contributions to politics and medicine in the 17th. century; I am fascinated by the social and scientific ideas of Alfred Russel Wallace, including his thoughts on vaccination; and a formal study of the development of the idea of a respiratory chain (cf. abstract 132 and paper 186) is planned.


Millar, F. A., Wrigglesworth, J. M., and Nicholls, P. (1981). Ligand binding to catalase and metmyoglobin: involvement of protons. Eur. J. Biochem. 117, 13-17.

Wrigglesworth, J. M. and Nicholls, P. (1982). Proton production by antimycin-inhibited mitochondria. Biochem. J. 204, 743-748.

Nicholls, P. and Kim, J.-K. (1982). Sulphide as an inhibitor and electron donor for the cytochrome c oxidase system. Canad. J. Biochem. 60, 613-623.

Brooks, S. P. J. and Nicholls, P. (1982). Anion and ionic strength effects upon the oxidation of cytochrome c by cytochrome c oxidase. Biochim. Biophys. Acta 680, 33-43.

Nicholls, P. and Chanady, G. A. (1982). Titration and steady state behaviour of the 830 nm chromophore in cytochrome c oxidase. Biochem. J. 203, 541-549.

Proteau, G., Wrigglesworth, J., and Nicholls, P. (1983). Proton-motive functions of cytochrome oxidase in reconstituted vesicles: influence of turnover rate on proton translocation. Biochem. J. 210, 199-205.

Brooks, S. P. J., Chanady, G. A. and Nicholls, P. (1982). Effect of Citrate on the reactions of cytochrome c with reductants and cyanide. Canad. J. Biochem. 60, 763-770.

Nicholls, P. (1983). Absorbance Spectroscopy, in Biochemical Research Techniques (ed. J. M. Wrigglesworth), pp. 1-47, John Wiley & Sons Ltd.

Nicholls, P. (1983). The Proteoliposome - is it a defective enzyme test bed? in Liposome Letters (ed. A. D. Bangham), pp. 215-229 , Academic Press, UK.

Hill, B. C., Brittain, T., Eglinton, D. G., Gadsby, P. M. A., Greenwood, C.,Nicholls, P., Peterson, J., Thomson, A. J. & Woon, T. C. (1983). Low spin ferric forms of cyt. a3 in mixed-ligand and partially reduced cyanide-bound derivatives of cytochrome c oxidase. Biochem. J. 215, 57-66.

Nicholls, P. (1983). The site of respiratory inhibition by cyanide.(Textbook errors ) TIBS 8, 353.

Singh, A. P. & Nicholls, P. (1984).Energized transport of potassium ions in the absence of valinomycin by cytochrome c oxidase-reconstituted vesicles. Biochim. Biophys.Acta 777, 194-200.

Sone, N. & Nicholls, P. (1984). Effect of heat treatment on oxidase activity and proton pumping capability of proteoliposome-incorporated beef heart cytochrome aa3. Biochemistry 23, 6550-6554.

Sone, N. & Nicholls, P. (1985). Complexes of cytochrome caa3 from the thermophilic bacterium PS3 with ligands and during catalytic activity. Canad. J. Biochem. Cell Biol. 63, 153-161.

Nicholls, P. & Sone, N. (1984). Kinetics of cytochrome c and TMPD oxidation by PS3 (thermophilic bacterium) cytochrome c oxidase. Biochim. Biophys. Acta 767, 240-247.

Hill,B. C., Woon,T.-C., Nicholls, P., Peterson, J., Greenwood, C., &Thomson, A. J. (1984). Interactions of sulphide and other ligands with cytochrome c oxidase: an electron paramagnetic resonance study. Biochem. J. 224, 591-600.

Grover, A. K., Singh, A. P., Rangachari, P. K. & Nicholls, P. (1985). Rat myometrium plasma membrane ion permeability: a method for studying H+, cation and anion movements in isolated plasma membrane vesicles. Am. J. Physiol. 248, C372-C378.

Singh, A. P., Chanady, G. A. & Nicholls, P. (1985). Interactions of the cyanine dye diSC3-(5) with cytochrome c and liposomes: their implications for estimation of delta psi in cytochrome c oxidase proteoliposomes. J. Memb. Biol. 84, 183-190.

Singh, A. P. & Nicholls, P. (1985). Cyanine and safranine dyes as membrane potential probes in cytochrome c oxidase reconstituted proteoliposomes. J. Biochem. Biophys. Methods. 11, 95-108.

Nicholls, P. & Shaughnessy, S. (1985). Effects of detergents and cytochromec binding on scalar and vectorial proton ejection by cytochrome oxidase-containing proteoliposomes. Biochem. J. 228, 201-210.

Shaughnessy, S. & Nicholls, P. (1985). Control of respiration in sonicated cytochrome oxidase proteoliposomes by gated and ungated ionophores. Biochem. Biophys. Res. Comm. 128, 1025-1030.

Thomson, A.J., Greenwood, C., Gadsby, P.M.A., Peterson, J., Eglinton, D.G., Hill, B.C. & Nicholls, P. (1985). The structure of the cytochrome a3-CuB site of mammalian cytochrome c oxidase as probed by MCD and EPR spectroscopy. J. Inorg. Biochem. 23, 187-197.

Singh, A.P. & Nicholls, P. (1986). Membrane potentials in reconstituted cytochrome c oxidase proteoliposomes determined by butyltriphenyl phosphonium cation distribution. Arch. Biochem. Biophys. 245, 436-445.

Singh, A.P. & Nicholls, P. (1986). Effect of triorganotin-mediated anion-hydroxide exchange upon reconstituted cytochrome c oxidase proteoliposomes. Biochem. Cell Biol. (Canada) 64, 647-655.

Hill, B.C., Greenwood, C. & Nicholls, P. (1986). Intermediate steps in the reaction of cytochrome oxidase with molecular oxygen. Biochim. Biophys. Acta. 853, 91-113.

Nicholls, P. (1987). Reconstitution as a research programme: T. E. King, 1956-1986,in Advances in Membrane Biochemistry and Bioenergetics (ed. C.H. Kim, H.Tedeschi, J.J.Diwan & J.C.Salerno),pp. 13-20, Plenum Press, N.Y.

Nicholls, P., Cooper, C.E., & Kjarsgaard, J. (1987). Control of proteoliposomal cytochrome oxidase: normal and inverted orientations, in Advances in Membrane Biochemistry and Bioenergetics (ed. C.H. Kim, H.Tedeschi,J.J.Diwan & J.C.Salerno), pp. 311-321, Plenum Press, N.Y.

Nicholls, P., Shaughnessy, S. & Singh, A. P. (1987). Control of cytochrome oxidase: flux and stoichiometry, in Cytochrome Systems: Molecular Biology and Bioenergetics (ed. S. Papa, B.Chance & L.Ernster), pp.391-398, Plenum Press, N. Y.

Cooper, C. E. & Nicholls, P. (1987). Activity of proteoliposomes containing cytochrome oxidase in the submitochondrial orientation. FEBS letts.223, 155-160.

Nicholls, P., Cooper, C. E., Leece, B., Freedman, J. A. & Chan, S.H.P. (1987). Antibodies as probes of cytochrome oxidase structure and function, in Oxidases and Related Redox Systems IV, ed. M.Morrison, T.E.King & H. S. Mason (Proc. 4th Intern. Symp.) pp.637-651, Alan Liss, N.Y.

Nicholls, P. (1987). 'Integrity of structure' and 'latent life' - the respiratory chain, Claude Bernard and David Keilin, in Oxidases and Related Redox Systems IV , ed. M.Morrison, H. S. Mason and T.E. King (Proceedings of the 4th.Inter. Symp.) pp. 65-78, Alan Liss, New York.

Freedman, J. A., Leece, B., Cooper, C. E., Nicholls, P. & Chan, S.H.P. (1988). Effects of subunit V antibodies on the topology of the subunit and the activity of beef heart cytochrome c oxidase. Biochem.Cell Biol. 66,1210-1217.

Freedman, J. A., Chan, S.H.P. & Nicholls, P. (1988). Topographical changes in cytochrome c oxidase in the soluble and membrane-bound enzyme as probed by antibodies to subunit V and the whole enzyme, in Integration of Mitochondrial Function (ed. J. J. LeMasters, C.R. Hackenbrock, R.G.Thurman, & H.V. Westerhoff), pp.71-77, Plenum Publishing Corp., New York.

Nicholls, P., Cooper, C. E., Freedman, J. A. & Leece, B. D. (1988). Effects of antibodies to intact cytochrome oxidase and its subunit V on the enzymatic activity. Biochem. Cell Biol. 66,1218-1225.

Nicholls, P. & Singh, A. P. (1988). Effect of zinc on proteoliposomal cytochrome oxidase. Life Science Advances (Agra, India) 7, 321-326.

Nicholls, P. & Wrigglesworth, J. M. (1988). Routes of cytochrome a3 reduction:the neoclassical model revisited. Ann. N.Y. Acad.Sci. 550, 59-67.

Wrigglesworth, J. M., Ioannidis, N. & Nicholls, P. (1988). Spectrophotometric characterization of intermediate redox states of cytochrome oxidase. Ann. N. Y. Acad. Sci. 550, 150 -160.

Nicholls, P. & Cooper, C. E. (1989). Modulation of cytochrome oxidase kinetics by indirect antibody action. FEBS letters 250, 453-456.

Wrigglesworth, J.M., Cooper, C.E., Sharpe, M., & Nicholls, P.(1990).The proteoliposomal steady state: effects of size, capacitance and membrane permeability on cytochrome oxidase-induced ion gradients. Biochem.J., 270,109-118.

Cooper, C. E. & Nicholls, P. (1990) . Structure and vectorial properties of proteoliposomes containing cytochrome oxidase in the submitochondrial orientation. Biochemistry 29, 3865-3871.

Cooper, C. E., Bruce, D. H. & Nicholls, P. (1990). Oxonol V as a probe of membrane potential in proteoliposomes containing cytochrome oxidase in the submitochondrial orientation. Biochemistry 29, 3859-3865.

Nicholls, P., Cooper, C. E. & Wrigglesworth, J. M. (1990). Control of proteoliposomal cytochrome c oxidase: the overall reaction. Biochem. Cell Biol., 68, 1128-1134.

Nicholls, P. (1990). Control of proteoliposomal cytochrome c oxidase: the partial reactions. Biochem. Cell Biol., 68, 1135-1141.

Nicholls, P. (1990) Book Review - Membrane Proteins:Structure, Function Assembly (Nobel Symp. #66, J. Rydstrsm, Ed.). Cell Biophysics 16, 99-103.

Zamudio, I., Kornblatt, J.A., Nicholls, P., Li, Y., & Cygler, M. (1990) Preliminary studies on the crystallization of beef heart cytochrome c oxidase by vapor diffusion. Biochem. Biophys. Res. Comm.,169, 1105-1110.

Cooper, C.E., Wrigglesworth, J.M., & Nicholls, P. (1991). The mechanism of potassium movement across the liposomal membrane. Biochem. Biophys. Res. Comm., 173, 1008-1012.

Cooper, C. E., Nicholls, P., & Freedman, J. A. (1991). Cytochrome c oxidase: structure, function and membrane topology of the polypeptide subunits. Biochem. Cell. Biol., 69, 586-607.

Nicholls, P. (1992) Control of proteoliposomal cytochrome c oxidase: models and mechanisms. in in Biothermokinetics, 1990 (ed. H. V. Westerhoff), Chap. 11, pp. 95-104, Intercept Press, Andover, U.K.

Nicholls, P., Obinger, C., Niederhauser, H. & Peschek, G. A. (1991). Cytochrome oxidase in Anacystis nidulans : stoichiometries and possible functions in the cytoplasmic and thylakoid membranes. Biochim. Biophys. Acta, 1098, 184-190.

Moser, D., Nicholls, P., Wastyn, M., & Peschek, G.A.(1991) Acidic cytochrome c6 of unicellular bacteria is an indispensable and kinetically competent electron donor to cytochrome oxidase in plasma and thylakoid membranes. Biochemistry International, 24, 757-768.

Crinson, M., & Nicholls, P. (1992) Routes of electron transfer in beef heart cytochrome c oxidase: is there a unique pathway used by all reductants? Biochem. Cell. Biol., 70, 301-308.

Nicholls, P., Rand, R. P., Fuller, N. & Butko, P. (1992) Water, ions and membrane proteins: how would Darwin look at cytochromes and channels? Biochem. Soc. Trans. (UK) 20, 583-589.

Nicholls, P. & Butko, P. (1993) Protons, pumps and potentials: control of cytochrome c oxidase. J. Bioenerg. Biomemb. 25, 137-143.

Tihova, M., Tattrie, B., & Nicholls, P. (1993) Electron microscopy of cytochrome c oxidase-containing proteoliposomes: imaging analysis of protein orientation and monomer-dimer behaviour. Biochem. J. 292, 933-946.

Nicholls, P. (1992) What form of cytochrome c oxidase reacts with oxygen in vivo? Biochem. J. 288, 1070-1072.

Nicholls, P. & He, J. (1993) Direct and indirect effects of valinomycin upon cytochrome c oxidase. Arch. Biochem. Biophys., 301, 305-310.

Freedman, J. A., Dyer, B., Tattrie, B. & Nicholls, P. (1993) The effect of antibodies to subunit V of cytochrome oxidase on cyanide inhibition of electron transfer. Biochim. Biophys. Acta 1164, 138-142.

He, J., & Nicholls, P. (1993) Dibucaine interacts differently with membrane and protein in cytochrome c oxidase systems. Biochem. Cell. Biol., 71, 14-21.

Nicholls, P. (1993) Control of cytochrome c oxidase: kinetic, thermodynamic or allosteric? in Modern Trends in Biothermokinetics (eds. S. Schuster, J.-P. Mazat & M. Rigoulet), pp. 11-16, Plenum Press, New York.
Hillar, A. & Nicholls, P. (1992) The mechanism of inhibition of catalase compound II formation by NADPH. FEBS letters 314, 179-182.

Butko, P., He, J., & Nicholls, P. (1992) Protein phosphorescence as a probe of conformation change in cytochrome oxidase due to valinomycin binding. Biochem. Biophys. Res. Comm. 189, 1477-1483.

Berka, V., Vygodina, T., Musatov, A., Nicholls, P., & Konstantinov, A.A. (1993) A New Spectral Intermediate in cyanide binding with oxidized cytochrome c oxidase. FEBS Letts 315, 237-241.

Loewen, P. C., Switala, J., von Ossowski, I., Hillar, A., Christie, A., Tattrie, B., & Nicholls, P. (1993) Catalase HPII of Escherichia coli. catalyses the conversion of protohaem to cis-Heme d. Biochemistry 32, 10159-10164.

Rand, R. P., Fuller, N., Butko, P., Francis, G. & Nicholls, P. (1993) Measured change in protein solvation with substrate binding and turnover. Biochemistry 32, 5925-5929.

Nicholls, P. (1993) The steady state of cytochrome c oxidase in proteoliposomes. FEBS Letters 327, 194-198.
Tihova, M., Tattrie, B., & Nicholls, P. (1994) Cytochrome c oxidase in proteoliposomes visualised by platinum-carbon and by tungsten-tantalum shadowing: image analysis. Biochem. Biophys. Res. Comm. 203, 331-337.

Hillar, A. P.,Nicholls, P.,Switala, J.,& Loewen, P. C.(1994) NADPH binding and control of compound II formation: comparison of bovine, yeast, and E. coli catalases. Biochem. J. 300, 531-539.

Nicholls, P. (1994) A Darwinian View Of Cytochromes And Channels. in Principles of Medical Biology (ed. E. E. Bittar), Vol. 1B, Chap. 9, pp. 233-249 (JAI Press, Inc., New York).

Tarba, C., Tattrie, B., & Nicholls, P. (1993) Use of fluorescent probes for a new evaluation of delta psi and delta pH in cytochrome oxidase vesicles. Studia Univ. Babes-Bolyai, Biologia, XXXVIII (1-2), 81-92.

Nicholls, P., Butko, P., & Tattrie, B. (1995) Topology of cytochrome c oxidase-containing proteoliposomes: probes, proteins and pH gradients. J. Liposome Res., 5, 371-398.

Sharpe, M. A., Wrigglesworth, J. M., Loewen, J., & Nicholls, P. (1995) Small pH gradients inhibit cytochrome c oxidase: implications for proton entry to the binuclear centre. Biochem. Biophys. Res. Comm., 216, 931-938.

Sharpe, M., Perin, I., Tattrie, B., & Nicholls, P. (1997) Ligation, inhibition and activation of cytochrome c oxidase by fatty acids. Biochem. Cell. Biol., 75, 71-79.

Sharpe, M. A., Perin, I., Wrigglesworth, J. M. & Nicholls, P. (1996) Fatty acids as modulators of cytochrome c oxidase activity in proteoliposomes. Biochem. J., 320, 557-561.

Sharpe, M. A., Perin, I. & Nicholls, P. (1996) Action of bovine serum albumin on cytochrome c oxidase activity and proton pumping: a role for fatty acids in enzyme function? FEBS letts., 391, 134-138.

Nicholls, P., Sternin, Y., Loewen, J.,Jennings, T., and Tattrie, B. (1996) Hydration as a Control Mechanism in Membrane Proteins: the case of Cytochrome c Oxidase. Faraday Discussions 103, 313-323.

Maj, M., Nicholls, P., Obinger, C., Hillar, A. & Loewen, P. C. (1996) Reaction of E coli catalase HPII with cyanide as ligand and as inhibitor. Biochim. Biophys. Acta, 1298, 241-249.

Fetter, J., Sharpe, M., Qian, J., Mills, D., Ferguson-Miller, S. & Nicholls, P. (1996) Fatty acids stimulate activity and restore respiratory control in a proton channel mutant of cytochrome c oxidase. FEBS letts., 393, 155-160.

Nicholls, P. (1996) Iron enzymes. The Biochemist, 18 (#4, Aug./Sept.), pp.18-22.

Obinger, C., Maj, M., Loewen, P. C. & Nicholls, P. (1997) Activity, peroxide compound formation, and haem d synthesis in E. coli HPII catalase. Arch. Biochem. Biophys., 342, 58-67.

Maj, M., & Nicholls, P. (1997) Reactions of high spin ligands with catalases from E. coli and beef liver. In preparation.

Nicholls, P. (1996) Cytochrome c - a multidisciplinary approach (book review). J. Am Chem. Soc. 118, 9459-9460.

Nicholls, P. (1997) The respiratory chain: from MacMunn and Keilin to the present state of the art. in Modern ideas of oxidative phosphorylation (eds. S. Papa, J. Tager & F. Guerriero) Plenum Press, submitted.

Capitanio, N., Vygodina, T.V., Capitanio, G., Konstantinov, A. A., Nicholls, P., & Papa, S. (1997) Redox-linked protolytic reactions in soluble cytochrome c oxidase from beef heart mitochondria: redox Bohr effects. Biochim. Biophys. Acta, 1318, 255-265.

Nicholls, P. (1997) Water, the one essential reagent? The Biochemist, 19 (#3, June), p. 7.

Old Publications
Keilin, D. and Nicholls, P. (1958). On the supposed catalytic oxidation of thiol groups by catalase. Biochim. Biophys. Acta. 28, 225.

Keilin, D. and Nicholls, P. (1958). Reactions of catalase with hydrogen peroxide and hydrogen donors. Biochim. Biophys. Acta 29, 302-307.

Gibson, J. F., Nicholls, P. and Ingram, D. J. E. (1958). Free radical produced in the reaction of metmyoglobin with hydrogen peroxide. Nature 181, 1398-1399.

Keilin, D. and Nicholls, P. (1959). Effect of azide on free haematins. Biochim. Biophys. Acta 36, 257-259.

Nicholls, P. (1960). Biological organization, Science 132, 1411-1412.

Nicholls, P.(1961). The action of anions on catalase peroxide compounds. Biochem.J.,81,365-374.

Nicholls, P. (1961). The formation and properties of sulphmyoglobin and sulphcatalase, Biochem. J., 81, 374-383.

Nicholls, P. (1962). The reduction of catalase by azide and peroxides. Biochim. Biophys. Acta, 58, 386-388.

Nicholls, P. (1962). The reaction between aminotriazole and catalase. Biochim. Biophys. Acta, 59, 414-420.

Nicholls, P.(1962). The role of the protein in haem enzymes. Biochim. Biophys. Acta 60, 217-225.

Nicholls, P. (1962). Senescence and senility, Nature 194, 506-508.

Nicholls, P. (1962). Peroxidase as an oxygenase; in The Oxygenases (ed.O. Hayaishi), pp. 263-305. Academic Press, New York.

Nicholls, P. (1963). Ferrous complexes in the catalase reaction, Experientia 19, 80-81.
Nicholls, P. (1963). Cytochromes; a survey, in The Enzymes (ed. P. Boyer, H. Lardy & K. Myrback). Vol. VIII (2nd Edn.), pp. 3-40, Academic Press, N. Y.

Nicholls, P. and Schonbaum, G. R. (1963), Catalases, in The Enzymes (ed. P. Boyer, H. Lardy & K. Myrback). Vol. VIII (2nd edn.), pp. 147-225, Academic Press, N. Y.

Nicholls, P. (1963). Reactions of cytochromes a and a3 in the succinate oxidase system. Biochim. Biophys. Acta. 73, 667-670.

Nicholls, P. (1964). The reactions of azide with catalase and their significance. Biochem. J., 90, 331-343.

Nicholls, P. (1964). Kinetics of catalase steady state activity. Trans.Farad. Soc. 60, 137-140.

Nicholls, P. (1964). The formation and catalytic role of catalase compound II, Biochim. Biophys. Acta. 81, 479-495.

Nicholls, P. (1964). Observations on the oxidation of cytochrome c , Arch. Biochem. Biophys. 106, 25-48.

Nicholls, P. (1965). Activity of catalase in the red cell, Biochim.Biophys. Acta. 99, 286-297.

Nicholls, P. (1965). Cytochrome oxidase in situ: concepts and questions, in Oxidases and Related Redox Systems (ed. T. E. King, H. S. Mason and M. Morrison), pp. 764-783. Wiley &Sons, N.Y.

Nicholls, P.(1965). Oxidation and peroxidation. J. Gen. Physiol.49, 131-147.

Nicholls, P. (1966). Horse radish peroxidase: the role of the endogenous donor, in Hemes and Hemoproteins (ed. B. Chance, R. W. Estabrook & T. Yonetani), 307-318. Academic Press, N.Y.

Nicholls, P. (1966). The azide ferrimyoglobin reaction (discussion comment), in Hemes and Hemoproteins (ed. B. Chance, R. W. Estabrook and T. Yonetani), 205-208. Academic Press, N. Y.

Nicholls, P. and Mochan, E. (1967). Reactivity of cyancytochrome c . Biochem. Biophys. Acta. 131, 397-400.

Nicholls, P. and Malviya, A. N. (1968). Inhibition of non-phosphorylating electron transfer by zinc. The problem of delineating interaction sites. Biochemistry 7, 305-310.

Malviya, A.N., Nicholls,P. and Elliott,W. B.(1968). Steady state changes in loosely coupled sub-mitochondrial particles induced by ADP and uncouplers. Biochim. Biophys. Acta. 153, 920-922.

Nicholls, P. and Kimelberg, H. K. (1968). Cytochromes a and a3: catalytic activity and spectral shifts in situ and in solution. Biochim. Biophys. Acta. 162, 11-21.

Nicholls, P. (1968). Cytochrome oxidase as an allosteric enzyme, in Structure and Function of Cytochromes (ed. K. Okunuki, M. D. Kamen & I. Sekuzu), 76-86, Univ. Park Press, Baltimore.

Brownie, A. C., Skelton, F. R., Gallant, S., Nicholls, P. and Elliott, W. B.(1968). Adrenal cytochrome levels, corticosteroidogenesis and respiratory activity in the rat following MAD treatment. Life Sciences 7, 765-771.

Brodie, J. D. and Nicholls, P. (1968). Enzymatic and metabolic behaviour of fluorosuccinic acids. Biochem. Biophys. Res. Comm. 32, 1071-1077.

Nicholls, P., Mochan, E. and Kimelberg, H. K. (1969). Complex formation by cytochrome c : a clue to the structure and polarity of the inner mitochondrial membrane. FEBS letters 3, 242-246.

Kimelberg, H. K. and Nicholls, P. (1969). Kinetic studies on the interaction of TMPD with cytochrome c and cytochrome c oxidase. Arch. Biochem. Biophys. 133, 327-335.

Brodie, J. D. and Nicholls, P. (1970). Metabolism and enzymology of fluorosuccinic acids. I. Interactions with the succinate oxidase system. Biochim. Biophys. Acta. 198, 423-437.

Tober, C. L., Nicholls, P. and Brodie, J. D. (1970). Metabolism and enzymology of fluorosuccinic acids. II. Substrate and inhibitor effects with soluble succinate dehydrogenase. Arch. Biochem. Biophys. 138, 506-514.

Rothstein, M., Nicholls, F. and Nicholls, P. (1970). Mitochondria from the free-living nematode Turbatrix aceti. Inter. J. Biochem. l, 695-705.

Nicholls, P., Mochan, E. and Kimelberg, H. K. (1971). Endogenous cytochrome c and the structure of the Keilin-Hartree particle in Energy transduction in Respiration and Photosynthesis (ed. G. F. Azzone et al.) pp. 339-352. Adriatica Editrice, Bari.

Nicholls, P. and Mochan, E. (1971). Complex formation between cytochrome c and cyt. c peroxidase. I. Kinetic studies. Biochem. J. 121, 55-67.

Mochan, E. and Nicholls, P. (1971). Complex formation between cytochrome c and cytochrome c peroxidase. II. Titration and equilibrium studies. Biochem. J. 121, 69-82.

Nicholls, P., Kimelberg, H. K., Mochan, E., Mochan, B. S. and Elliott, W. B. (1971). Where is the mitochondrial binding site for cytochrome c ? in Probes of Structure and Function of Macromolecules and Membranes (ed. B. Chance et al.) Vol. I, pp. 431-436. Academic Press, N.Y.

Nicholls, P. and Kimelberg, H. K. (1972). Cytochrome oxidase in the mitochondrial membrane, in Biochemistry and Biophysics of Mitochondrial Membranes (ed. N. Siliprandi et al.) pp. 17-32, Academic Press, N.Y.

Nicholls, P. and Mochan E. (1971). Formation of a stable "active" complex between cytochrome c and yeast peroxidase. Nature New Biology 230, 276-277.

Nicholls, P. (1974). 'Catalase' in USES Chemical Encyclopedia, in Italian, Vol. III, pp. 137-141. (UTET/Sansoni Edizioni Scientifiche, Florence, Italy).

Malviya, A. N., Elliott, W. B., Nicholls, P. and Kimelberg, H. K. (1971). Activation and Inhibition of Respiration in submitochondrial digitonin fragments. Ind. J. Biochem. 8, 121-129.

van Buuren, K. J. H., Nicholls, P. and van Gelder, B. F. (1972). Biochemical and biophysical studies of cytochrome aa3 VI Reaction of cyanide with oxidized and reduced enzyme. Biochim. Biophys. Acta 256, 258-276.

Wilson, D. F., Erecinska, M. and Nicholls, P. (1972). An energy dependent transformation of a ferricytochrome of the mitochondrial respiratory chain. FEBS letters 20, 61-65.

Mochan, E. and Nicholls, P. (1972). Cytochrome c reactivity in its complexes with mammalian cytochrome c oxidase and yeast peroxidase. Biochim. Biophys. Acta 267, 309-319.

Nicholls, P. and Wenner, C. E.(1972). Release of respiratory control by uncouplers:the question of stoichiometry. Arch. Biochem. Biophys.151, 206-215.

Nicholls, P., van Buuren, K. J. H. and van Gelder, B. F.(1972). Biochemical and biophysical studies on cytochrome aa3 VIII Effect of cyanide on the catalytic activity. Biochim. Biophys. Acta 275, 279-287.

Nicholls, P., Erecinska, M. and Wilson, D. F. (1973). Low spin ferricytochrome a3: high energy state or intrinsic probe? in Mechanisms in Bioenergetics (ed. E. Quagliariello et al.), pp. 561-570. Academic Press, New York.

Erecinska, M., Wilson, D. F., Sato, N., and Nicholls, P. (1972). The energy dependence of the chemical properties of cytochrome oxidase. Arch. Biochem. Biophys. 151, 188-193.

Nicholls, P. (1972). Contributions of catalase and glutathione peroxidase to red cell peroxide removal. Biochim. Biophys. Acta 279, 306-309.

Mochan, B. S., Elliott, W. B., and Nicholls, P. (1973). Patterns of cytochrome oxidase inhibition by polycations. J. Bioenergetics 4, 329-345.

Nicholls, P. (1973). The CO complex of cytochrome P450. in Oxidases and Related Redox Systems II (ed. T. E. King, H. S. Mason and M. Morrison) pp. 512-513, University Park Press, Baltimore, Md.

Nicholls, P. and Chance, B. (1973). Cytochrome c oxidase, in Molecular Mechanisms of Oxygen Activation (ed. O. Hayaishi) pp. 479-534, Academic Press, New York.

Wrigglesworth, J. M., Baum, H. and Nicholls, P. (1973). Constraints on the mechanism of reduction of molecular oxygen by cytochrome oxidase under coupled conditions. FEBS letts 35, 106-108.

Nicholls, P. (1974). On the nature of cytochrome a3. in Dynamics of Energy-transducing Membranes (ed. L. Ernster, R. W. Estabrook & E. C.Slater), pp. 39-50. Elsevier, Amsterdam.

Nicholls, P. and Elliott, W. B. (1974). The cytochromes. in Iron in Biochemistry and Medicine (ed. A. Jacobs & M. Worwood), pp. 221-277, Academic Press, London, U. K.

Nicholls, P. (1975). Cytochromes and biological oxidation. (Oxford Biology Reader No. 66), Oxford University Press.

Nicholls, P. and Miller, N. G. M. (1974). Chloride diffusion from liposomes. Biochim. Biophys. Acta. 356, 184-198.

Nicholls, P., West, J. and Bangham, A. D. (1974). Chlorophyll b -containing liposomes: effect of temperature on spectrum and catalytic activity. Biochim. Biophys. Acta. 363, 190-201.

Petersen, L. C., Nicholls, P. and Degn, H. (1974). The effect of energization on the apparent Km for oxygen in mitochondrial respiration. Biochem. J. 142, 247-252.

Malviya, A. N. and Nicholls, P. (1974). The reaction of cyanide with cytochrome c and cytochrome oxidase, in Proc. Symp. Bhabha Atomic Research Centre, Bombay, India, pp.509-524.

Nicholls, P. and Petersen, L. C. (1974). Haem-haem interactions in cytochrome aa3 during the anaerobic-aerobic transition. Biochim. Biophys. Acta 357, 462-467.

Nicholls, P. (1974). Cytochrome c binding to enzymes and membranes. Biochim. Biophys. Acta, Bioenergetics Reviews, 346, 261-310.

Nicholls, F., Nicholls, P. and Sand, O. (1976). Phosphofructokinase and related glycolytic enzyme activities in flounder (Platichthys flesus, L.) liver. Comp. Biochem. Physiol. 54B, 461-466.

Nicholls, P. (1975). The effect of sulphide on cytochrome aa3: isosteric and allosteric shifts of the reduced alpha peak. Biochim. Biophys. Acta 396, 24-35.

Nicholls, P. (1975). Electron flux and the steady state of cytochrome c in Electron Transfer Chains and Oxidative Phosphorylation, (ed. E. Quagliariello et al.), pp. 227-232, North Holland Pub. Co., Amsterdam.

Petersen, L. C., Nicholls, P., and Degn, H. (1976). The effect of oxygen concentration on the steady-state kinetics of the solubilized cytochrome c oxidase. Biochim. Biophys. Acta 452, 59-65.

Nicholls, P. (1975). Formate as an inhibitor of cytochrome c oxidase. Biochem. Biophys. Res. Comm. 67, 610-616.

Nicholls, P. (1976). Catalytic activity of cytochromes c and c1 in mitochondria and submitochondrial particles. Biochim. Biophys.Acta 430, 30-45.

Nicholls, P. (1976). The effect of formate on cytochrome aa3 and on electron transport in the intact respiratory chain. Biochim. Biophys. Acta 430, 13-29.

Nicholls, P., Petersen, L.C., Miller, M. and Hansen, F. B.(1976). Ligand-induced spectral changes in cytochrome c oxidase and their possible significance. Biochim. Biophys. Acta 449, 188-196.

Petersen, L. C., Degn, H., and Nicholls, P. (1977). Kinetics of the cytochrome c oxidase and reductase reactions in energized and de-energized mitochondria. Can. Jour. Biochem. 55, 706-713.

Nicholls, P. and Hildebrandt, V. A. (1978). Binding of ligands and spectral shifts in cytochrome c oxidase. Biochem. J. 173, 65-72.

Hansen, F. B., Miller, M. and Nicholls, P. (1978). Control of respiration in proteoliposomes containing cytochrome aa3: I. Stimulation by valinomycin and uncoupler. Biochim. Biophys. Acta 502, 385-399.

Hansen, F. B. and Nicholls, P. (1978). Control of respiration in proteoliposomes containing cytochrome aa3: II.Inhibition by CO and azide. Biochim. Biophys. Acta 502,400-408.

Wrigglesworth, J. M. and Nicholls, P. (1978). Vectorial properties of cytochrome c oxidase in reconstituted vesicles. Biochim. Biophys. Acta 547, 36-46.

Wrigglesworth, J. M. and Nicholls, P. (1978). Spectroscopic behaviour of cytochrome c oxidase in reconstituted vesicles. FEBS letts. 91, 190-193.

Nicholls, P. (1978). Membrane Proteins (Vol. 45, Proc. 11th FEBS meeting, Copenhagen, 1977), co-editor. Introduction, p. 35 (Pergamon Press).

Nicholls, P. (1978). Cytochromes and biological oxidation (2nd. edition), Carolina Biology Reader No. 66, 16 pp. Carolina Biological Supply Co., Burlington, N. C.

Nicholls, P. (1978). Are cytochromes a and a3 on opposite sides of the energy-conserving membrane? in Frontiers in Biological Energetics (ed. P.L.Dutton, J. S. Leigh, & A. Scarpa), pp. 825-832, Academic Press, N. Y.

Nicholls, P. and Hildebrandt, V. (1978). Redox state of the partially reduced cytochrome aa3-cyanide complex. Biochim. Biophys. Acta 504, 457-460.

Nicholls, P. (1978). A new carbon monoxide-induced complex of cytochrome c oxidase. Biochem. J. 175, 1147-1150.

Nicholls, P. (1979). Is cytochrome c oxidase 'Compound C' another carbon monoxide complex of the enzyme? in Oxygen: Biochemical and Clinical Aspects (ed. W. S. Caughey), Acad. Press, N.Y.

Nicholls, P. and Wrigglesworth, J. M. (1979). Scalar and vectorial pH effects in cytochrome aa3: is there a proton-motive aa3 cycle? in Oxidases and Related Oxidation-Reduction Systems - 3rd. Inter. Symp. (eds.T. E. King, H. S. Mason & M. Morrison), pp. 1149-1160, Pergamon Press.

Nicholls, P. (1979). Carbon monoxide - ancient and modern clue to the reaction mechanism of oxygen with cytochrome oxidase, in Oxidases and Related Oxidation-Reduction Systems - 3rd Inter. Symp. (eds. T. E. King, H. S. Mason & M. Morrison), pp. 1161-1179, Pergamon Press.

Nicholls, P. (1979). Effects of inhibitory ligands upon the aerobic carbon monoxide complex of cytochrome c oxidase. Biochem. J. 183, 519-529.

Miller, M., Petersen, L. Chr., Hansen, F. B. and Nicholls, P. (1979). Effect of ionophores on carrier-mediated electron translocation in ferricyanide -containing liposomes. Biochem. J. 184, 125-131.

Malviya, A. N., Nicholls, P. and Elliott, W. B. (1980). Observations on the oxidoreduction of the two cytochromes b in cyt. c deficient mitochondria and submitochondrial particles. Biochim. Biophys. Acta, 589, 137-149.

Nicholls, P., Hildebrandt, V.and Wrigglesworth, J. M. (1980). Orientation and reactivity of cytochrome aa3 in proteoliposomes. Arch. Biochem. Biophys. 204, 533 - 543.

Hill, B. C. and Nicholls, P. (1980). Reduction and activity of cytochrome c in the cytochrome c - cytochrome aa3 complex. Biochem. J. 187, 809-818.

Hill, B. C. and Nicholls, P. (1980). Cyt. c reduction by cysteine plus copper: a pseudosubstrate system for cyt. c oxidase. Canad. J. Biochem. 58, 499-503.

Nicholls, P., Hildebrandt, V., Hill, B. C., Nicholls, F., and Wrigglesworth, J. M. (1980). Pathways of cytochrome c oxidation by soluble and membrane-bound cytochrome aa3. Canad. J. Biochem. 58, 969-977.

Nicholls, P. and Chanady, G. A. (1981). Interactions of cytochrome aa3 with oxygen and carbon monoxide. The role of the 607 nm complex. Biochim. Biophys. Acta 634, 256-265.

Nicholls, P. (1983). The Biology of Oxygen. Carolina Biology Reader #100.

Nicholls, P. (1981). Liposomes as Artificial Organelles, Topochemical Matrices, and Therapeutic Carrier Systems. Inter. Rev. Cytol. Supplemental Volume 12: Membrane Research; Classic Origins and Current Concepts (ed. A. L. Muggleton-Harris) , pp. 327-388.

Nicholls, P. and Chanady, G. A. (1981). Reactivity of photoreduced cytochrome aa3 complexes with molecular oxygen. Biochem. J. 194, 713-720.

Nicholls, P. and Kim, J.-K. (1981). Oxidation of sulphide by cytochrome aa3. Biochim. Biophys. Acta. 637, 312-320.

Additional information
  • I am sometime Vice-president of the Canadian Biophysical Society.
  • I am a Board member of Science for Peace Canada,
  • A member of Scientists for Global Responsibility and also
  • Current Chair of Abolition 2000 UK

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