Recent developments in dynamic electrochemical studies of adsorbed enzymes and their active sites

Current Opinion in Chemical Biology

Volumn 9, Issue 2, 2005, Pages 110-117

  Armstrong, Fraser A ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; ENZYME; FLAVINE ADENINE NUCLEOTIDE; LACCASE; MOLYBDENUM; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ADSORPTION; CATALYSIS; CATALYST; CYCLIC POTENTIOMETRY; CYTOPLASM; ELECTROCHEMISTRY; ELECTRODE; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INHIBITION; ENZYME SUBSTRATE; ESCHERICHIA COLI; POTENTIOMETRY; PROTEIN ANALYSIS; PROTEIN FUNCTION; QUANTITATIVE ANALYSIS; REDUCTION; REVIEW; RHODOBACTER SPHAEROIDES; SIGNAL TRANSDUCTION;

EID: 16244366777     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2005.02.011     Document Type: Review

References (41)

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2. H.C. Angove, J.A. Cole, D.J. Richardson, and J.N. Butt Protein film voltammetry reveals distinctive fingerprints of nitrite and hydroxylamine reduction by a cytochrome c nitrite reductase J Biol Chem 277 2002 23374 23381 This paper provides an account of the electrocatalytic voltammetry of the six-electron reduction of nitrite by a multi-heme enzyme and examines the differences in behaviour when hydroxylamine (an unreleased intermediate) is the substrate.
3. J.D. Gwyer, H. Angove, D.J. Richardson, and J.N. Butt Redox-triggered events in cytochrome c nitrite reductase Bioelectrochemistry 63 2004 43 47 This paper describes the kinetics and energetics of binding of the inhibitor cyanide to the multi-heme nitrite reductase.
4. •• ] each report, independently, on the unusual potential dependence of catalysis by nitrate reductases, and suggest a special role for Mo(V) in the catalytic cycle.
5. ••].
6. ••].
7. A. Sucheta, B.A.C. Ackrell, B. Cochran, and F.A. Armstrong Diode-like behaviour of a mitochondrial electron-transport enzyme Nature 356 1992 361 362
8. H.R. Pershad, J. Hirst, B. Cochran, B.A.C. Ackrell, and F.A. Armstrong Succinate dehydrogenase: comparison with the enzyme from beef heart mitochondria Biochim Biophys Acta 1412 1999 262
9. S.J. Elliott, C. Léger, H.R. Pershad, J. Hirst, K. Heffron, F. Blasco, R.A. Rothery, J.H. Weiner, and F.A. Armstrong Detection and interpretation of redox potential optima in the catalytic activity of enzymes Biochim Biophys Acta 1555 2002 54 59
10. K. Heffron, C. Léger, R.A. Rothery, J.H. Weiner, and F.A. Armstrong Determination of an optimal potential window for catalysis by E. coli dimethyl sulfoxide reductase and hypothesis on the role of Mo(V) in the reaction pathway Biochemistry 40 2001 3117 3126
11. B. Limoges, and J.-M. Savéant Catalysis by immobilized redox enzymes: diagnosis of inactivation and reactivation effects through odd cyclic voltammetric responses J Electroanal Chem 562 2004 43 52 This paper provides an independent electrochemist's interpretation of the unusual electrocatalytic behaviour of some enzymes at electrodes.
12. A.L. Bradley, S.E. Chobot, D.M. Arciero, A.B. Hooper, and S.J. Elliott A distinctive electrocatalytic response from the cytochrome c peroxidase of Nitrosomonas europaea J Biol Chem 279 2004 13297 13300
13. M.S. Mondal, D.B. Goodin, and F.A. Armstrong Simultaneous voltammetric comparisons of reduction potentials, reactivities, and stabilities of the high-potential catalytic states of wild-type and distal pocket mutant (W51F) yeast cytochrome c peroxidase J Am Chem Soc 120 1998 6270
14. D.L. Johnson, J.L. Thompson, S.M. Brinkmann, K.A. Schuller, and L.L. Martin Electrochemical characterisation of purified Rhus vernicifera laccase: voltammetric evidence for sequential four-electron transfer Biochemistry 42 2003 10229 10237
15. B. Haghighi, L. Gorton, T. Ruzgas, and L.J. Jönsson Characterization of graphite electrodes modified with laccase from Trametes versicolor and their use for bioelectrochemical monitoring of phenolic compounds in flow injection analysis Anal Chim Acta 487 2003 3 14
16. + by the catalytic (1λ) subcomplex of mitochondrial NADH:ubiquinone oxidoreductase (Complex I) J Am Chem Soc 125 2003 6020 6021 This paper demonstrates how PFV can be used to determine the catalytic properties of a large and extremely complex enzyme. Here, the 1λ subcomplex of Complex I, which catalyses the oxidation of NADH by quinone (but which lacks the membrane-intrinsic subdomain across which protons are pumped) is seen to possess a bias in favour of the reverse reaction, NAD reduction.
17. H.A. Heering, J.H. Weiner, and F.A. Armstrong Direct detection and measurement of electron relays in a multicentered enzyme: voltammetry of electrode-surface films of E. coli fumarate reductase, an iron-sulfur flavoprotein J Am Chem Soc 119 1997 11628
18. A.K. Jones, E. Sillery, S.P.J. Albracht, and F.A. Armstrong Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst Chem Commun 2002 866 867
19. C. Léger, A.K. Jones, W. Roseboom, S.P.J. Albracht, and F.A. Armstrong Enzyme electrokinetics: hydrogen evolution and oxidation by Allochromatium vinosum [NiFe]-hydrogenase Biochemistry 41 2002 15736 15746
20. C. Léger, A.K. Jones, S.P.J. Albracht, and F.A. Armstrong Effect of a dispersion of interfacial electron transfer rates on steady state catalytic electron transport in [NiFe]-hydrogenase and other enzymes J Phys Chem B 106 2002 13058 13063
21. S.E. Lamle, K.A. Vincent, L.M. Halliwell, S.P.J. Albracht, and F.A. Armstrong Hydrogenase on an electrode: a remarkable heterogeneous catalyst Dalton Transactions 21 2003 4152 4157
22. A.K. Jones, S.E. Lamle, H.R. Pershad, K.A. Vincent, S.P.J. Albracht, and F.A. Armstrong Enzyme electrokinetics: Electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase J Am Chem Soc 125 2003 8505 8514 This paper describes studies that illuminate the complicated anaerobic transformations leading to and from the so-called 'Ready' inactive state of [NiFe]-hydrogenases.
23. C. Léger, S. Dementin, P. Bertrand, M. Rousset, and B. Guigliarelli Inhibition and aerobic inactivation kinetics of Desulfovibrio fructosovorans hydrogenase studied by protein film voltammetry J Am Chem Soc 126 2004 12162 12172 This paper demonstrates a novel way to study reactions of an adsorbed enzyme with gaseous substrates.
24. 2.
25. F.A. Armstrong Insights from protein film voltammetry into mechanisms of complex biological electron-transfer reactions J Chem Soc Dalton Transactions 2002 661
26. K.S. Chen, J. Hirst, R. Camba, C.A. Bonagura, C.D. Stout, B.K. Burgess, and F.A. Armstrong Atomically defined mechanism for proton transfer to a buried redox centre in a protein Nature 405 2000 814 817
27. M. Meuwly, and M. Karplus Theoretical investigations of ferredoxin I: the possible role of internal water molecules on the coupled electron proton transfer reaction Faraday Discuss 124 2003 297 313
28. R. Camba, Y.-S. Jung, L. Hunsicker-Wang, B.K. Burgess, C.D. Stout, H. Hirst, and F.A. Armstrong Mechanisms of redox-coupled proton transfer in proteins: role of the proximal proline in reactions of the [3Fe-4S] cluster in Azotobacter vinelandii ferredoxin I Biochemistry 42 2003 10589 10599 This study follows on from the earlier paper [25] and demonstrates that a mutation that allows a water molecule to occupy a position close to a buried Fe-S cluster does not assist proton transfer.
29. K.R. Hoke, N. Cobb, F.A. Armstrong, and R. Hille Electrochemical studies of arsenite oxidase: an unusual example of a highly cooperative two-electron molybdenum icenter Biochemistry 43 2004 1667 1674 This study reports the first observation of a highly cooperative Mo(VI)/(IV) redox couple in an enzyme, in which the Mo(V) state is not detectable by EPR.
30. K.F. Aguey-Zinsou, P.V. Bernhardt, and S. Leimkühler Protein film voltammetry of Rhodobacter capsulatus xanthine dehydrogenase J Am Chem Soc 125 2003 15352 15358 The experiments in this paper suggest that an unidentified redox cofactor is involved in catalytic oxidation of xanthine. The authors propose that activity depends upon an oxidation-linked transformation of the pterin cofactor.
31. 1-type Rieske [2Fe-2S] center of Thermus thermophilus J Am Chem Soc 123 2001 9906 9907
32. 0 core by protonation Proc Natl Acad Sci USA 101 2004 10913 10918 Here, the ability of PFV to explore reactions occurring at extremely low potentials is exploited to produce and characterize an all-Fe(II) state of a Rieske centre.
33. J. Zhang, Q. Chi, A.M. Kuznetsov, A.G. Hansen, H. Wackerbarth, H.E.M. Christensen, J.E.T. Andersen, and J. Ulstrup Electronic properties of functional biomolecules at metal/aqueous solution interfaces J Phys Chem B 106 2002 1131 1152
34. J. Zhang, A.M. Kuznetsov, and J. Ulstrup In situ scanning tunnelling microscopy of redox molecules. Coherent electron transfer at large bias voltages J Electroanal Chem 541 2003 133 146
35. J. Zhang, A.C. Welinder, A.G. Hansen, H.E.M. Christensen, and J. Ulstrup Catalytic monolayer voltammetry and in situ scanning tunnelling microscopy of copper nitrite reductase on cysteamine-modified Au(111) electrodes J Phys Chem B 107 2003 12480 12484 This paper combines catalytic voltammetry with STM studies that reveal the structure of the self-assembled monolayer of cysteamine and the manner of adsorption of enzyme molecules.
36. K. Ataka, and J. Heberle Functional vibrational spectroscopy of a cytochrome c monolayer: SEIDAS probes the interaction with different surface-modified electrodes J Am Chem Soc 126 2004 9445 9457 This study provides detailed information on the way that a protein interacts specifically with different electrode surfaces.
37. K. Ataka, F. Giess, W. Knoll, R. Naumann, S. Haber-Pohlmeier, B. Richter, and J. Heberle Oriented attachment and membrane reconstitution of his-tagged cytochrome c oxidase to a gold electrode: in situ monitoring by surface-enhanced infrared absorption spectroscopy J Am Chem Soc 126 2004 16199 16206
38. F. Baymann, N.L. Barlow, C. Aubert, B. Schoepp-Cothenet, G. Leroy, and F.A. Armstrong Voltammetry of a 'protein on a rope' FEBS Lett 539 2003 91 94 This paper provides evidence for the importance of immobilizing a protein on an electrode so that it retains mobility.
39. H.A. Heering, F.G.M. Wiertz, C. Dekker, and S. de Vries Direct immobilization of native yeast iso-1 cytochrome c on bare gold. Fast electron relay to redox enzymes and zeptomole protein-film voltammetry J Am Chem Soc 126 2004 11103 11112 This study provides an excellent example of how a protein that is covalently attached directly to a gold electrode surface can be stable and exhibit fast electron transfer. The immobilized protein is able to relay electrons to natural enzyme partners.
40. F.A. Armstrong, N.L. Barlow, P.L. Burn, K.R. Hoke, L.J.C. Jeuken, C. Shenton, and G.R. Webster Fast long-range electron-transfer reactions of a 'blue' copper protein coupled non-covalently to an electrode through a stilbenyl thiolate monolayer Chem Comm 2004 316 317
41. C.R. Hess, G.A. Juda, D.M. Dooley, R.N. Amii, M.G. Hill, J.R. Winkler, and H.B. Gray Gold electrodes wired for coupling with the deeply buried active site of Arthrobacter globiformis amine oxidase J Am Chem Soc 125 2003 7156 7157