Prof Peter Rich

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Personal Profile

Name: Peter Rich Email: prr@ucl.ac.uk
Title: Prof Tel: 2076797746
Department: Structural & Molecular Biology Fax: 2076797096
Position: Professor of Bioenergetics Address: ISMB UCL, Gower Street, London, WC1E 6BT
Research Domain: Basic Life Sciences, Biomedical Imaging (Frontier Disciplines), Cancer, Personalised Medicine Web Page: Personal Web Page

Profile

Research Description

Research expertise is centred around UV/visible and vibrational mid-infrared spectroscopies, together with a range of biochemical, biophysical and electrochemical methods with both basic and translational applications.
Basic research in centred upon biochemical and biophysical studies of biological electron transfer processes, particularly those of the mitochondrial respiratory chain with particular attention to the basic factors that are important for coupled electron and proton transfer within proteins. Our major focus is cytochrome c oxidase, and we have developed as a model system a His-tagged form of yeast mitochondrial cytochrome c oxidase, a system which allows for the first time the genetic manipulation of both nuclear and mitochondrially-encoded subunits.
Translational projects, in collaborations with clinicians at UCH, Hammersmith and Royal Free Hospitals, are aimed at exploiting the rapid technical advances of mid-infrared spectroscopy to provide new medical diagnostic tools. One major project is screening of urine samples for various kidney diseases that are difficult or expensive to diagnose with current clinical methods.  This has already led to our installing an experimental IR spectrometer in the Urology clinic of RFH for a three year data collection programme. A second major programme is development of methods for rapid, automated screening of biopsy samples for cancer stage diagnoses.


Research Activities

Bioenergetics

Education Description

I am Course Organiser, Lecturer and Tutor on 1st year full unit course BIOC1007 (Principles and Practice of Biochemistry). This represent 25% of the 1st year taught programme of all 1st year Biochemistry and Biotechnology students. I have modernised and revamped it with new lectures/lecturers covering modern biochemical methods, new tutorials, a new practical that I designed and implemented, introduction of workshops, accreditation for tutorials and practicals, a Moodle-based MCQ examination in Term 2 and provision of a comprehensive Moodle site and CourseBook for students. Lecturer on BIOC2005 (Metabolism and its Regulation), BIOC3006 (Biomolecular Structure) and BIOL3017 (Biology of Ageing). Tutor on BIOC2005 (Biomolecular Structure and Function). Personal Tutor to approx. 15 undergraduates.

UCL Collaborators

Prof Tony Segal

External Collaborators

Publications

    2014

    • Ojemyr LN, Maréchal A, Vestin H, Meunier B, Rich PR, Brzezinski P (2014). Reaction of wild-type and Glu243Asp variant yeast cytochrome c oxidase with O2.. Biochim Biophys Acta, , - . doi:10.1016/j.bbabio.2014.03.012

    2013

    • Maréchal A, Iwaki M, Rich PR (2013). Structural changes in cytochrome c oxidase induced by binding of sodium and calcium ions: an ATR-FTIR study.. J Am Chem Soc, 135(15), 5802 - 5807. doi:10.1021/ja4005706
    • Rich PR, Maréchal A (2013). Functions of the hydrophilic channels in protonmotive cytochrome c oxidase.. J R Soc Interface, 10(86), 20130183 - . doi:10.1098/rsif.2013.0183
    • Dodia R, Maréchal A, Bettini S, Iwaki M, Rich PR (2013). IR signatures of the metal centres of bovine cytochrome c oxidase: assignments and redox-linkage.. Biochem Soc Trans, 41(5), 1242 - 1248. doi:10.1042/BST20130087

    2012

    • Maréchal A, Meunier B, Lee D, Orengo C, Rich PR (2012). Yeast cytochrome c oxidase: a model system to study mitochondrial forms of the haem-copper oxidase superfamily.. Biochim Biophys Acta, 1817(4), 620 - 628. doi:10.1016/j.bbabio.2011.08.011
    • Liu L-N, Bryan SJ, Huang F, Yu J, Nixon PJ, Rich PR, Mullineaux CW (2012). Control of electron transport routes through redox-regulated redistribution of respiratory complexes. Proceeding of the National Academy of Sciences USA, 109(28), 11431 - 11436.
    • Meunier B, Marechal A, Rich PR (2012). Construction of histidine-tagged yeast mitochondrial cytochrome c oxidase for facile purification of mutant forms. BIOCHEMICAL JOURNAL, 444, 199 - 204. doi:10.1042/BJ20120116
    • Rich PR , Marechal A (2012). Electron transfer chains: structures, mechanisms and energy coupling. In Egelman E (Ed.), Comprehensive Biophysics (pp. - ). : Academic Press.
    • Liu L-N, Bryan SJ, Huang F, Yu J, Nixon PJ, Rich PR, Mullineaux CW (2012). Control of electron transport routes through redox-regulated redistribution of respiratory complexes. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1817, S139 - S139. doi:10.1016/j.bbabio.2012.06.366
    • Marechal A, Meunier B, Dodia R, Rich PR (2012). Yeast mitochondrial cytochrome c oxidase: Effect of mutations in the hydrophilic channels within Cox1 and the adjacent supernumerary subunit Cox5A/B. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1817, S109 - S110. doi:10.1016/j.bbabio.2012.06.295
    • Maréchal A, Meunier B, Rich PR (2012). Assignment of the CO-sensitive carboxyl group in mitochondrial forms of cytochrome c oxidase using yeast mutants.. Biochim Biophys Acta, 1817(10), 1921 - 1924. doi:10.1016/j.bbabio.2012.03.036
    • Rich PR, Marechal A, Meunier B, Dodia R (2012). Functions of the hydrophilic channels of mitochondrial forms of cytochrome oxidase from studies of yeast mutants. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1817, S102 - S102. doi:10.1016/j.bbabio.2012.06.276
    • Mullineaux CW, Liu LN, Bryan SJ, Leake MC, Nixon PJ, Rich PR (2012). Sub-micron scale distribution of electron transport compelxes in bacterial membranes, and its influence on electron transfer pathways. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1817, S149 - S150. doi:10.1016/j.bbabio.2012.06.394

    2011

    • Rich PR (2011). Special Section: Peter Mitchell-50th anniversary of the chemiosmotic theory. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1807(12), 1505 - 1506. doi:10.1016/j.bbabio.2011.09.019
    • Maréchal A, Rich PR (2011). Water molecule reorganization in cytochrome c oxidase revealed by FTIR spectroscopy.. Proc Natl Acad Sci U S A, 108(21), 8634 - 8638. doi:10.1073/pnas.1019419108

    2010

    • Murphy EJ, Maréchal A, Segal AW, Rich PR (2010). CO binding and ligand discrimination in human myeloperoxidase.. Biochemistry, 49(10), 2150 - 2158. doi:10.1021/bi9021507
    • Marechal A, Rich PR (2010). Fourier transform infrared spectroscopy reveals water molecules reorganization in cytochrome c oxidases. doi:10.1016/j.bbabio.2010.04.293
    • Rich PR, Maréchal A (2010). The mitochondrial respiratory chain. Essays in Biochemistry, 47, 1 - 23.
    • Rich PR, Marechal A (2010). Roles of amino acids and waters in the protonmotive mechanism of cytochrome oxidase. doi:10.1016/j.bbabio.2010.04.280

    2009

    • Whitehead SJ, Iwaki M, Cotton NPJ, Rich PR, Jackson JB (2009). Inhibition of proton transfer steps in transhydrogenase by metal ions. Biochim. Biophys. Acta, 1787, 1276 - 1288. doi:10.1016/j.bbabio.2009.06.001
    • Marshall D, Rich PR (2009). Studies of complex I by Fourier transform infrared spectroscopy. Methods in Enzymology, 456, 53 - 74. doi:10.1016/S0076-6879(08)04403-0
    • Maréchal A, Kido Y, Kita K, Moore AL, Rich PR (2009). Three redox states of Trypanosoma brucei alternative oxidase identified by infrared spectroscopy and electrochemistry. Journal of Biological Chemistry, 284, 31827 - 31833. doi:10.1074/jbc.M109.059980

    2008

    • Maréchal A, Ingledew WJ, Rich PR (2008). Time-resolved FTIR study of CO recombination with horseradish peroxidase. Biochemical Society Transactions, 36, 1165 - 1168. doi:10.1042/BST0361165
    • Amandine M, Rich PR (2008). FTIR detection of carboxyl groups in bovine heart cytochrome c oxidase. doi:10.1016/j.bbabio.2008.05.266
    • Rich PR, Marechal A (2008). Carboxyl group functions in the heme-copper oxidases: Information from mid-ir vibrational spectroscopy. doi:10.1016/j.bbabio.2008.05.258
    • Rich PR, Maréchal A (2008). Rich, P.R. and Maréchal, A. (2008) Carboxyl group functions in the heme-copper oxidases: Information from mid-IR vibrational spectroscopy, Biochim. Biophys. Acta, 1777, 912-918.. Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1777(7-8), 912 - 918. doi:10.1016/j.bbabio.2008.04.035
    • Rich PR (2008). A perspective on Peter Mitchell and the chemiosmotic theory. Journal of Bioenergetics and Biomembranes, 40, 407 - 410. doi:10.1007/s10863-008-9173-7
    • Whitehead SJ, Iwaki M, Rich PR, Jackson JB (2008). Inhibition of H+ transfer in transhydrogenase by Zn2+. doi:10.1016/j.bbabio.2008.05.143

    2007

    • Rich PR, Iwaki M (2007). Probing protein transitions with ATR infrared spectroscopy. Molecular Biosystems, 3, 398 - 407.
    • Rich PR, Iwaki M (2007). Methods to probe protein transitions with ATR infrared spectroscopy.. Mol Biosyst, 3(6), 398 - 407. doi:10.1039/b702328f
    • Iwaki M, Rich PR (2007). An IR Study of Protonation Changes Associated with Heme-Heme Electron Transfer in Bovine Cytochrome c Oxidase. Journal of the American Chemical Society, 129, 2923 - 2929.
    • Rich P, Iwaki M (2007). A Comparison of Catalytic Site Intermediates of Cytochrome c Oxidase and Peroxidases. Biochemistry (Moscow), 72, 1047 - 1055.

    2006

    • Nixon PJ, Rich PR (2006). Chlororespiratory Pathways and Their Physiological Significance. In Wise RR, Hoober JK (Ed.), The Structure and Function of Plastids (pp. 237 - 251). : Springer.
    • Iwaki M, Puustinen A, Wikström M, Rich PR (2006). Structural and Chemical Changes of the PM Intermediate of Paracoccus denitrificans Cytochrome c Oxidase Revealed by IR Spectroscopy With Labelled Tyrosines and Histidine. Biochemistry, 45, 10873 - 10885.
    • Marshall DCA, Fisher N, Grigic L, Zickermann V, Brandt U, Shannon RJ, Hirst J, Lawrence R, Rich PR (2006). ATR-FTIR redox difference spectroscopy of Yarrowia lipolytica and bovine complex I.
    • Iwaki M, Puustinen A, Wikstrom M, Rich PR (2006). ATR-FTIR characterisation of the P-M intermediate of Paracoccus denitrificans cytochrome c oxidase.
    • Marshall D, Fisher N, Grigic L, Zickermann V, Brandt U, Shannon RJ, Hirst J, Lawrence R, Rich PR (2006). ATR-FTIR redox difference spectroscopy of Yarrowia lipolytica and bovine complex I. Biochemistry, 45, 5458 - 5467.
    • Mathe C, Ingledew J, Rich PR (2006). Horseradish peroxidase and myoglobin active site studies by ATR-FTIR spectroscopy.
    • Iwaki M, Cotton , N PJ, Quirk , P G, Rich , P R, Jackson , J B (2006). Molecular recognition between protein and nicotinamide dinucleotide in intact, proton-translocating transhydrogenase studied by ATR-FTIR spectroscopy. Journal of the American Chemical Society, 128, 2621 - 2629.
    • Osyczka A, Zhang H, Mathé C, Rich PR, Moser CC, Dutton PL (2006). Role of the PEWY glutamate in hydroquinone-quinone oxidation-reduction catalysis in the Qo site of cytochrome bc1. Biochemistry, 45, 10492 - 10503.
    • Rich PR, Iwaki M (2006). The protonmotive mechanism of cytochrome c oxidase: Probing the internal charge-compensating protonation by FTIR spectroscopy.

    2005

    • Rich PR, Iwaki M (2005). Infrared Protein Spectroscopy as a Tool to Study Protonation Reactions Within Proteins. In Wikstrom M (Ed.), Biophysical and Structural Aspects of Bioenergetics (pp. 314 - 333). : Royal Society of Chemistry.
    • van Thor JJ, Fisher N, Rich PR (2005). Assignments of the Pfr-Pr FTIR difference spectrum of cyanobacterial phytochrome Cph1 using a 15N and 13C isotopically labelled phycocyanobilin chromophore. The Journal of Physical Chemistry B, B, 20597 - 20604.
    • Iwaki M, Yakovlev G, Hirst J, Osyczka A, Dutton PL, Marshall M, Rich PR (2005). Direct observation of redox-linked histidine protonation changes in the iron sulfur protein of cytochrome bc1 complex by ATR-FTIR spectroscopy. Biochemistry, 44, 4230 - 4237.
    • Ingledew WJ, Rich PR (2005). A study of the horseradish peroxidase catalytic cycle by FTIR spectroscopy. Biochemical Society Transactions, 33, 886 - 889.
    • Ingledew WJ, Smith SME, Gao YT, Jones RJ, Salerno JC, Rich PR (2005). Ligand, co-factor and residue vibrations in the catalytic site of endothelial Nitric Oxide Synthase. Biochemistry, 44, 4238 - 4246.

    2004

    • Rich PR (2004). The quinone chemistry of bc complexes.. Biochim Biophys Acta, 1658(1-2), 165 - 171. doi:10.1016/j.bbabio.2004.04.021
    • Iwaki M, Osyczka A, Moser CC, Dutton PL, Rich PR (2004). ATR-FTIR spectroscopy studies of iron-sulfur protein and cytochrome c1 in Rhodobacter capsulatus cytochrome bc1 complex. Biochemistry, 43, 9477 - 9486. doi:10.1021/bi049211x
    • Iwaki M, Puustinen A, Wikström M, Rich PR (2004). ATR-FTIR Spectroscopy and Isotope-Labelling of the PM Intermediate of Paracoccus denitrificans Cytochrome c Oxidase. Biochemistry, 43, 14370 - 14378.
    • Iwaki M, Puustinen A, Wikstrom M, Rich PR (2004). ATR-FTIR spectroscopy and isotope labelling studies of the PM intermediate of paracoccus denitrificans cytochrome c oxidase.
    • Rich PR (2004). Biochimica et Biophysica Acta Bioenergetics The Quinone Chemistry of bc Complexes. Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1658, 165 - 171.
    • Iwaki M, Rich PR, Bizouarn T, Boxel GI, Cotton NPJ, Jackson JB (2004). The binding of nucleotides to the intact proton-translocating transhydrogenase studied by calorimetry and ftir spectroscopy.
    • Iwaki M, Rich PR (2004). Direct Detection of Formate-Ligation in Cytochrome c Oxidase by ATR-FTIR Spectroscopy. Journal of the American Chemical Society, 126, 2386 - 2389. doi:10.1021/ja039320j
    • Rich PR (2004). The quinone chemistry of BC complexes.

    2003

    • Iwaki M, Puustinen A, Wikström M, Rich PR (2003). ATR-FTIR spectroscopy of the PM and F intermediates of bovine and Paracoccus denitrificans cytochrome c oxidase. Biochemistry, 42, 8809 - 8817. doi:10.1021/bi034522d
    • Rich PR (2003). The molecular machinery of Keilin's respiratory chain. Biochemical Society Transactions, 31, 1095 - 1105.
    • Rich PR (2003). The cost of living. Nature, 421, 583 - .
    • Iwaki M, Giotta L, Akinsiku AO, Schägger H, Fisher N, Breton J, Rich PR (2003). Redox transitions in bovine cytochrome bc1 complex studied by perfusion-induced ATR-FTIR spectroscopy. Biochemistry, 42, 11109 - 11119. doi:10.1021/bi0343020

    2002

    • Iwaki M, Andrianambinintsoa S, Rich PR, Breton J (2002). Attenuated total reflection fourier transform infrared spectroscopy of redox transitions in photosynthetic reaction centres: Comparison of perfusion and light induced difference spectra. Spectroscopica Acta, 58, 1523 - 1533.
    • Ingledew WJ, Smith SME, Salerno JC, Rich PR (2002). Neuronal nitric oxide synthase ligand and protein vibrations at the substrate binding site. A study by FTIR. Biochemistry, 41, 8377 - 8384.
    • Rich PR, Breton J (2002). ATR-FTIR Studies of redox changes in bovine cytochrome c oxidase: Resolution of the redox FTIR difference spectrum of heme a3. Biochemistry, 41, 967 - 973.
    • Iwaki M, Breton J, Rich PR (2002). ATR-FTIR difference spectroscopy of the PM intermediate of bovine cytochrome c oxidase . Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1555, 116 - 121.
    • Rich PR, Rigby SEJ, Heathcote P (2002). Radicals associated with the catalytic intermediates of bovine cytochrome c oxidase. Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1554, 137 - 146.
    • Rich PR, Breton J (2002). Attenuated total reflection Fourier transform infrared studies of redox changes in bovine cytochrome c oxidase: resolution of the redox Fourier transform infrared difference spectrum of heme a(3).. Biochemistry, 41(3), 967 - 973.
    • Tottey S, Rondet SAM, Borrelly GPM, Robinson PJ, Rich PR, Robinson NJ (2002). A copper metallochaperone for photosynthesis and respiration reveals metal-specific targets, interaction with an importer, and alternative sites for copper acquisition. Journal of Biological Chemistry, 277, 5490 - 5497.

    2001

    • Tottey S, Rich PR, Rondet SAM, Robinson NJ (2001). Two Menkes-type ATPases supply copper for photosynthesis in Synechocystis PCC 6803. J BIOL CHEM, 276(23), 19999 - 20004.
    • Tottey S, Rich PR, Rondet SAM, Robinson NJ (2001). Two Menkes-type ATPases that both supply copper for photosynthetic electron transport in Synechocystis PCC6803. Journal of Biological Chemistry, 276, 19999 - 20004.
    • Rich PR, Breton J (2001). FTIR studies of the cyanide and CO adducts of fully reduced bovine cytochrome c oxidase. Biochemistry, 40, 6441 - 6449.
    • Rich PR, Mischis LA, Purton S, Wiskich JT (2001). The sites of interaction of triphenyltetrazolium chloride with mitochondrial respiratory chains.. FEMS Microbiol Lett, 202(2), 181 - 187.
    • Schneider D, Berry S, Rich PR, Seidler A, R gner M (2001). The cytochrome b6f subunit PetM in Synechocystis PCC6803. Journal of Biological Chemistry, 276, 16780 - 16785.
    • Rich PR, Mischis LM, Purton S, Wiskich JT (2001). The sites of interaction of TTC with mitochondrial respiratory chains. FEMS Microbiology Letters, 202(2), 181 - 187.

    2000

    • Rich PR, Breton J, J_nemann S, Heathcote P (2000). Protonation reactions in relation to the coupling mechanism of bovine cytochrome c oxidase. Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1459, 475 - 480.
    • Jünemann S, Heathcote P, Rich PR (2000). The reactions of hydrogen peroxide with bovine cytochrome c oxidase.. Biochim Biophys Acta, 1456(1), 56 - 66.
    • Rigby SEJ, Junemann S, Rich PR, Heathcote P (2000). The reaction of bovine cytochrome c oxidase with hydrogen peroxide produces a tryptophan cation radical and a porphyrin cational radical. Biochemistry, 39, 5921 - 5928.
    • Fisher N, Rich PR (2000). A motif for quinone binding sites in respiratory and photosynthetic systems. Journal of Molecular Biology, 296, 1153 - 1162.

    1999

    • Junemann S, Meunier B, Fisher N, Rich PR (1999). Effects of Mutation of the Conserved Glutamic Acid-286 in Subunit I of Cytochrome c Oxidase from Rhodobacter sphaeroides. Biochemistry, 38, 5248 - 5255.
    • Rich PR, Fisher N (1999). Generic features of quinone binding sites. Biochemical Society Transactions, 27, 561 - 565.

    1998

    • Meunier B, Ortwein C, Brandt U, Rich PR (1998). Effects of mutation of residue I67 in yeast cytochrome c oxidase on redox-linked protonation processes. Biochemical Journal, 330, 1197 - 1200.
    • Br ker S, Meunier B, Rich PR, Gattermann N, Hofhaus G (1998). MtDNA mutations associated with sideroblastic anaemia cause a defect of mitochondrial cytochrome c oxidase. European Journal of Biochemistry, 258, 132 - 138.
    • Meunier B, Rodriguez-Lopez JN, Smith AT, Thorneley RNF, Rich PR (1998). Redox- and Anion-linked protonation sites in horseradish peroxidase. Biochemical Journal, 330, 303 - 309.
    • Meunier B, Rich PR (1998). Can second-site reversion analysis predict tertiary protein structure? An assessment using mutations in yeast cytochrome c oxidase subunits I and II. Journal of Molecular Biology, 283, 727 - 730.
    • Rich PR, J nemann S, Meunier B (1998). Protonmotive mechanism of haem-copper oxidases. Journal of Bioenergetics and Biomembranes, 30, 131 - 138.
    • Rich PR, Hoefnagel MHN, Wiskich JT (1998). Possible chlororespiratory reactions of thylakoid membranes. In Moller IM, Gardstr m P, Glimelius K, Glaser E (Ed.), Plant Mitochondria: From Gene to Function (pp. 17 - 23). : Backhuys Publishers.
    • Rich PR (1998). Mechanism of protonmotive activity of heme-copper oxidases. Frontiers of Cellular Bioengernetics: Molecular Biology, Biochemistry and Physiopathology, , - .
    • Moody AJ, Butler CS, Watmough NJ, Thomson AJ, Rich PR (1998). The reaction of halides with pulsed cytochrome bo from Escherichia coli. Biochemical Journal, 331, 459 - 464.
    • Meunier B, Rich PR (1998). Second-site reversion analysis is not a reliable method to determine distance in membrane proteins: An assessment using mutations in yeast cytochrome c oxidase subunits I and II. Journal of Molecular Biology, 283, 727 - 730.
    • Meunier B, Rich PR (1998). Quantitation and characterisation of cytochrome c oxidase in complex systems. Analytical Biochemistry, 260, 237 - 243.
    • Moody AJ, Butler CS, Watmough NJ, Thomson AJ, Rich PR (1998). The reaction of halides with pulsed cytochrome bo from Escherichia coli. BIOCHEM J, 331, 459 - 464.
    • Meunier B, Ortwein C, Brandt U, Rich PR (1998). Effects of mutation of residue I67 on redox-linked protonation processes in yeast cytochrome c oxidase.. Biochem J, 330 ( Pt 3), 1197 - 1200.
    • J nemann S, Heathcote P, Rich PR (1998). On the mechanism of quinol oxidation in the bc1 complex. Journal of Biological Chemistry, 273, 21603 - 21607.

    1997

    • Hoefnagel MHN, Rich PR, Zhang QS, Wiskich JT (1997). Substrate kinetics of the plant mitochondrial alternative oxidase and the effects of pyruvate. PLANT PHYSIOL, 115(3), 1145 - 1153.
    • Rich PR, Meunier B, Junnmann S (1997). Coupling of Ion and Charge Movement: from Peroxidase to Protonmotive Oxidases. Oxygen Homeostasis and Its Dynamics, , 40 - 46.
    • Hoefnagel MHN, Millar AH, Rich PR, Zhang QS, Wiskich JT (1997). The substrate kinetics of the alternative oxidase of plant mitochondria: Are they simple or complex?. PLANT PHYSIOL, 114(3), 61004 - 61004.
    • Hoefnagel MHN, Rich PR, Zhang Q, Wiskich JT (1997). The substrate affinity of the alternative oxidase of plant mitochondria is not increased by pyruvate.. PLANT PHYSIOL, 114(3), 287 - 287.
    • Ortwein C, Link TA, Meunier B, Colson A, Rich PR, Brandt U (1997). Structural and Functional Analysis of Deficient Mutants in Subunit I of Cytochrome c Oxidase from Saccharomyces cerevisiae. BIOCHIM BIOPHYS ACTA, 1321, 79 - 92.
    • Hoefnagel MHN, Rich PR, Zhang Q, Wiskich JT (1997). Substrate kinetics of the alternative oxidase of plant mitochondria: Pyruvate does not increase the substrate affinity. PLANT PHYSIOL, 115, 1145 - 1153.
    • Meunier B, Rich PR (1997). Coupling of protons transfer to oxygen chemistry in cytochrome oxidase; the roles of residues 167 and E243. Oxygen Homeostasis and Its Dynamics, , 106 - 111.
    • Meunier B, Rich PR (1997). Photolysis of the cyanide adduct of the ferrous horseradish peroxide. BIOCHIM BIOPHYS ACTA, 1318, 235 - 245.
    • Junnmann S, Wrigglesworth JM, Rich PR (1997). Effects of decyl-aurachin D and reversed electron transfer in cytochrome bd. Biochemistry, 36, 9323 - 9331.
    • Hunter DJB, Moody AJ, Rich PR, Ingledew WJ (1997). EPR spectroscopy of Escherichia coli cytochrome bo which lacks CuB. FEBS LETT, 412, 43 - 47.
    • Rich PR, Moody AJ (1997). Cytochrome c Oxidase. In Graber P, Milazzo G (Ed.), Bioenergetics (pp. 418 - 456). : Birkhauser.
    • Moody AJ, Mitchell R, Jeal AJ, Rich PR (1997). Comparison of the ligand-binding properties of native and copper-less cytochrome bo from Escherichia coli. BIOCHEM J, 324, 743 - 752.
    • Vener AV, van Kan PJM, Rich PR, Ohad I, Anderson B (1997). Plastoquinol at the quinol oxidation site of reduced cytochrome bf medicates signal transduction between light and protein phosphorylation: Thylakoid protein kinase deactivation by a single-turnover flash. PROC NATL ACAD SCI USA, 94, 1585 - 1590.
    • Junnmann S, Meunier B, Gennis RB, Rich PR (1997). Effects of mutation of the conserved lysine-362 in cytochrome c oxidase from Rhodobacter sphaeoides. Biochemistry, 36, 14456 - 14464.

    1995

    • MOODY AJ, COOPER CE, GENNIS RB, RUMBLEY JN, RICH PR (1995). INTERCONVERSION OF FAST AND SLOW FORMS OF CYTOCHROME BO FROM ESCHERICHIA-COLI. BIOCHEMISTRY-US, 34(20), 6838 - 6846.