Electrical circuitry in biology: Emerging principles from protein structure

Current Opinion in Structural Biology

Volumn 14, Issue 6, 2004, Pages 642-647

  Leys, David ^a   Scrutton, Nigel S ^a  

^a UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; FLAVOPROTEIN;

BIOLOGY; BREATHING; CATALYSIS; DIFFUSION; ELECTRIC ACTIVITY; ELECTRICITY; ELECTRON TRANSPORT; KINETICS; MORPHOLOGY; MUTATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN STRUCTURE; REVIEW; THERMODYNAMICS;

ANIMALS; CARRIER PROTEINS; CELL PHYSIOLOGY; CYTOCHROMES C; ELECTRON TRANSPORT; ELECTRON TRANSPORT CHAIN COMPLEX PROTEINS; ELECTROPHYSIOLOGY; FLAVOPROTEINS; HUMANS; MODELS, BIOLOGICAL; MODELS, CHEMICAL; MODELS, MOLECULAR; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 9944241407     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2004.10.002     Document Type: Review

References (41)

1. R.A. Marcus, and N. Sutin Electron transfer in chemistry and biology Biochim Biophys Acta 811 1985 265 316
2. C.C. Moser, J.M. Keske, K. Warncke, R.S. Farid, and P.L. Dutton Nature of biological electron transfer Nature 355 1992 796 802
3. D. Beratan, and S. Skourtis Electron transfer mechanisms Curr Opin Chem Biol 2 1998 235 243
4. C.C. Page, C.C. Moser, X. Chen, and P.L. Dutton Natural engineering principles of electron tunnelling in biological oxidation-reduction Nature 402 1999 47 52
5. T. Kawatsu, T. Kakitani, and T. Yamato Worm model for electron tunnelling in proteins: consolidation of the pathway model and the Dutton plot J Phys Chem B 105 2001 4424 4435
6. M.L. Jones, I.V. Kurnikov, and D.N. Beratan The nature of tunnelling pathway and average packing density models for protein-mediated electron transfer J Phys Chem A 106 2002 2002 2006
7. P.B. Crowley, and M. Ubbink Close encounters of the transient kind: protein interactions in the photosynthetic redox chain investigated by NMR spectroscopy Acc Chem Res 36 2003 723 730
8. P.B. Crowley, and M.A. Carrondo The architecture of the binding site in redox protein complexes: implications for fast dissociation Proteins: Structure, Function and Bioinformatics 55 2004 603 612
9. H. Pelletier, and J. Kraut Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c Science 258 1992 1748 1755
10. 551 Science 264 1994 86 90
11. + reductase Nat Struct Biol 8 2001 117 121
12. 1 complex with its bound substrate cytochrome c Proc Natl Acad Sci USA 99 2002 2800 2805
13. M. Jormakka, S. Tornroth, B. Byrne, and S. Iwata Molecular basis of proton motive force generation: structure of formate dehydrogenase-N Science 295 2002 1863 1868 An excellent example of the 'nano-wire' concept, involving eleven redox centers, including molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters, two haem b groups and a menaquinone analogue, aligned in a single chain and extending ∼90 Å through the protein.
14. 3 reductase can occur via a superexchange mechanism using the haem groups to enhance electronic coupling.
15. Paine M, Scrutton NS, Munro AW, Roberts GCK, Wolf CR: Electron transfer partners of cytochrome P450. In Cytochrome P450: Structure, Mechanism and Biochemistry edn 3. Edited by Ortiz de Montellano P. New York: Kluwer Academic/Plenum Publishers; 2004 in press.
16. 1: a new device for electron transfer in proteins Trends Biochem Sci 26 2001 445 451
17. D. Leys, J. Basran, F. Talfournier, M.J. Sutcliffe, and N.S. Scrutton Extensive conformational sampling in a ternary electron transfer complex Nat Struct Biol 10 2003 219 225 A detailed structural analysis of the concept of 'conformational sampling' by a tethered and highly mobile redox domain within the crystal lattice of a physiological electron transfer complex.
18. H.S. Toogood, A. Van Thiel, J. Basran, M.J. Sutcliffe, N.S. Scrutton, and D. Leys Extensive domain motion and electron transfer in the human ETF-MCAD complex J Biol Chem 279 2004 32904 32912 This second example of 'conformational sampling' in an electron transfer complex involving ETF also demonstrates a common anchor point for ETF on the surface of structurally distinct partner proteins.
19. D. Leys, T.E. Meyer, A.S. Tsapin, K.H. Nealson, M.A. Cusanovich, and J.J. Van Beeumen Crystal structures at atomic resolution reveal the novel concept of 'electron-harvesting' as a role for the small tetraheme cytochrome c J Biol Chem 277 2002 35703 35711 Structural analysis of STC suggests multiple sites for electron transfer and rapid distribution of electrons between the haems, thus providing a good example of an 'electron harvesting' unit.
20. V.L. Davidson What controls the rates of interprotein electron-transfer reactions Acc Chem Res 33 2000 87 93
21. 5 J Am Chem Soc 124 2002 6849 6859
22. H. Mei, K. Wang, N. Peffer, G. Weatherly, D.S. Cohen, M. Miller, G. Pielak, B. Durham, and F. Millett Role of configurational gating in intracomplex electron transfer from cytochrome c to the radical cation in cytochrome c peroxidase Biochemistry 38 1999 6846 6854
23. I.M. van Amsterdam, M. Ubbink, O. Einsle, A. Messerschmidt, A. Merli, D. Cavazzini, G.L. Rossi, and G.W. Canters Dramatic modulation of electron transfer in protein complexes by crosslinking Nat Struct Biol 9 2002 48 52 A demonstration of the importance of conformational freedom for electron exchange reactions between two soluble electron transfer proteins.
24. D. Leys, A.S. Tsapin, K.H. Nealson, T.E. Meyer, M.A. Cusanovich, and J.J. Van Beeumen Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1 Nat Struct Biol 6 1999 1113 1117
25. P. Taylor, S.L. Pealing, G.A. Reid, S.K. Chapman, and M.D. Walkinshaw Structural and mechanistic mapping of a unique fumarate reductase Nat Struct Biol 6 1999 1108 1112
26. O. Einsle, A. Messerschmidt, P. Stach, G.P. Bourenkov, H.D. Bartunik, R. Huber, and P.M. Kroneck Structure of cytochrome c nitrite reductase Nature 400 1999 476 480
27. C.C. Page, C.C. Moser, and P.L. Dutton Mechanism for electron transfer within and between proteins Curr Opin Chem Biol 7 2003 551 556 An excellent survey of 'robust' design features for electron transfer in proteins, with emphasis on the tunnelling reaction and properties of the protein medium.
28. I. Schroder, E. Johnson, and S. de Vries Microbial ferric iron reductases FEMS Microbiol Rev 27 2003 427 447
29. K.E. Pitts, P.S. Dobbin, F. Reyes-Ramirez, A.J. Thomson, D.J. Richardson, and H.E. Seward Characterization of the Shewanella oneidensis MR-1 decaheme cytochrome MtrA: expression in Escherichia coli confers the ability to reduce soluble Fe(III) chelates J Biol Chem 278 2003 27758 27765
30. C. Thorpe Electron-transferring flavoproteins F. Muller Chemistry and Biochemistry of Flavoenzymes vol 2 1991 CRC Press Boca Raton 471 486
31. A. Gruez, D. Pignol, M. Zeghouf, J. Coves, M. Fontecave, J.L. Ferrer, and J.C. Fontecilla-Camps Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module J Mol Biol 299 2000 199 212
32. A. Gutierrez, M. Paine, C.R. Wolf, N.S. Scrutton, and G.C. Roberts Relaxation kinetics of cytochrome P450 reductase: internal electron transfer is limited by conformational change and regulated by coenzyme binding Biochemistry 41 2002 4626 4637 A nice example of the use of equilibrium perturbation kinetic methods to study intraprotein electron transfer in cytochrome P450 reductase. Demonstration of rate limitation through conformational change is also provided.
33. P.A. Hubbard, Shen Al, R. Paschke, C.B. Kasper, and J.J. Kim NADPH cytochrome P450 oxidoreductase: structural basis for hydride and electron transfer J Biol Chem 276 2001 29163 29170
34. C. Feng, R.V. Kedia, J.T. Hazzard, J.K. Hurley, G. Tollin, and J.H. Enemark Effect of solution viscosity on intramolecular electron transfer in sulfite oxidase Biochemistry 41 2002 5816 5821 Electron transfer between the haem and molybdenum centres of sulfite oxidase is shown to be sensitive to solution viscosity in laser flash studies, demonstrating rate limitation through conformational change.
35. S.J. Elliott, A.E. McElhaney, C. Feng, J.H. Enemark, and F.A. Armstrong A voltammetric study of interdomain electron transfer within sulfite oxidase J Am Chem Soc 124 2002 11612 11613 A nice application of voltammetry to demonstrate that motion of the haem domain in sulfite oxidase is a limitation for enzyme activity.
36. 2 intraprotein electron transfer via an interdomain hinge region Biochem J 316 1996 507 513
37. 1 and its implications for energy conversion Proc Natl Acad Sci USA 97 2000 4567 4572
38. Mowat CG, Rothery E, Miles CS, McIver L, Doherty MK, Drewette K, Taylor P, Walkinshaw MD, Chapman SK, Reid GA: Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation. Nat Struct Biol 2004, doi:10.1038/nsmb827. This paper presents a brief structural description of a novel multihaem cytochrome c from metal-reducing Shewanella oneidensis MR1 with tetrathionate reductase activity.
39. P.R. Pokkuluri, Y.Y. Londer, N.E. Duke, W.C. Long, and M. Schiffer Family of cytochrome c7-type proteins from Geobacter sulfurreducens: structure of one cytochrome c7 at 1.45 Å resolution Biochemistry 43 2004 849 859
40. E.D. Garcin, C.M. Bruns, S.J. Lloyd, D.J. Hosfield, M. Tiso, R. Gachhui, D.J. Stuehr, J.A. Tainer, and E.D. Getzoff Structural basis for isozyme-specific regulation of electron transfer in nitric-oxide synthase J Biol Chem 279 2004 37918 37927 An excellent paper describing the effects of calmodulin binding or phosphorylation on the position and conformational freedom of the FMN domain and therefore on the production of nitric oxide.
41. 6f complex Biochemistry 43 2004 5921 5929