Extensive conformational sampling in a ternary electron transfer complex

Nature Structural Biology

Volumn 10, Issue 3, 2003, Pages 219-225

  Leys, David ^a   Basran, Jaswir ^a   Talfournier, François ^a   Sutcliffe, Michael J ^a   Scrutton, Nigel S ^a  

^a UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

FLAVOPROTEIN; TRIMETHYLAMINE DEHYDROGENASE; UNCLASSIFIED DRUG;

ARTICLE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ELECTRON TRANSPORT; METHYLOPHILUS METHYLOTROPHUS; MOLECULAR DYNAMICS; MOLECULAR MECHANICS; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN INTERACTION; STEADY STATE; TRANSPORT KINETICS;

AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ELECTRON-TRANSFERRING FLAVOPROTEINS; FLAVIN-ADENINE DINUCLEOTIDE; FLAVOPROTEINS; KINETICS; MACROMOLECULAR SUBSTANCES; METHYLOPHILUS METHYLOTROPHUS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXIDOREDUCTASES, N-DEMETHYLATING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

METHYLOPHILUS METHYLOTROPHUS; NEGIBACTERIA;

EID: 0037334897     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb894     Document Type: Article

References (27)

1. Marcus, R.A. & Sutin, N. Electron transfers in chemistry and biology. Biochim. Biophys. Acta 811, 265-316 (1985).
2. Davidson, V. Unraveling the kinetic complexity of interprotein electron transfer reactions. Biochemistry 35, 14035-14039 (1996).
3. 1. Nature 392, 677-84 (1998).
4. Feng, C. et al. Effect of solution viscosity on intramolecular electron transfer in sulfite oxidase. Biochemistry 41, 5816-5821 (2002).
5. Gruez, A. et al. Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module. J. Mol. Biol. 299, 199-212 (2000).
6. Hubbard, P.A., Shen, A.L., Paschke, R., Kasper, C.B. & Kim, J.J. NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer. J. Biol. Chem. 276, 29163-29170 (2001).
7. Gutierrez, A., Paine, M., Wolf, C.R., Scrutton, N.S. & Roberts, G.C. Relaxation kinetics of cytochrome P450 reductase: internal electron transfer is limited by conformational change and regulated by coenzyme binding. Biochemistry 41, 4626-4637 (2002).
8. Chen, L., Durley, R.C., Mathews, F.S. & Davidson, V.L. Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i. Science 264, 86-90 (1994).
9. Pelletier, H. & Kraut, J. Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c. Science 258, 1748-1755 (1992).
10. Jones, M., Basran, J., Sutcliffe, M.J., Grossmann, J.G. & Scrutton, N.S. X-ray scattering studies of Methylophilus methylotrophus (sp. W3A1) electron-transferring flavoprotein. Evidence for multiple conformational states and an induced fit mechanism for assembly with trimethylamine dehydrogenase. J. Biol. Chem. 275, 21349-21354 (2000).
11. Trickey, P. et al. Structural and biochemical characterization of recombinant wild type and a C30A mutant of trimethylamine dehydrogenase from Methylophilus methylotrophus (sp. W3A1). Biochemistry 39, 7678-7688 (2000).
12. Pettigrew, G.W. & Moore, G.R. In Cytochromes c: Biological Aspects. (Springer Verlag, New York; 1987).
13. Roberts, D.L., Frerman, F.E. & Kim, J.J. Three-dimensional structure of human electron transfer flavoprotein to 2.1-Å resolution. Proc. Natl. Acad. Sci. USA 93, 14355-14360 (1996).
14. Roberts, D.L., Salazar, D., Fulmer, J.P., Frerman, F.E. & Kim, J.J. Crystal structure of Paracoccus denitrificans electron transfer flavoprotein: structural and electrostatic analysis of a conserved flavin binding domain. Biochemistry 38, 1977-1989 (1999).
15. Talfournier, F. et al. αArg-237 in Methylophilus methylotrophus (sp. W3A1) electron-transferring flavoprotein affords approximately 200-millivolt stabilization of the FAD anionic semiquinone and a kinetic block on full reduction to the dihydroquinone. J. Biol. Chem. 276, 20190-20196 (2001).
16. Wilson, E.K. et al. An ultracentrifugal approach to quantitative characterization of the molecular assembly of a physiological electron-transfer complex: the interaction of electron-transferring flavoprotein with trimethylamine dehydrogenase. Eur. J. Biochem. 243, 393-399 (1997).
17. Page, C.C., Moser, C.C., Chen, X. & Dutton, P.L. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature 402, 47-52 (1999).
18. Chohan, K.K., Scrutton, N.S. & Sutcliffe, M.J. Major structural reorganisation most likely accompanies the transient formation of a physiological electron transfer complex. Protein Pept. Lett. 5, 231-236 (1998).
19. Chohan, K.K. et al. Protein dynamics enhance electronic coupling in electron transfer complexes. J. Biol. Chem. 276, 34142-34147 (2001).
20. Basran, J., Chohan, K.K., Sutcliffe, M.J. & Scrutton, N.S. Differential coupling through Val-344 and Tyr-442 of trimethylamine dehydrogenase in electron transfer reactions with ferricenium ions and electron transferring flavoprotein. Biochemistry 39, 9188-9200 (2000).
21. Jones, M. et al. Electron transfer and conformational change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein. J. Biol. Chem. 277, 8457-8465 (2002).
22. Thorpe, C. Electron-transferring flavoproteins, in Chemistry and Biochemistry of Flavoenzymes Vol. II. (ed. Muller, F.) 471-486 (CRC Press, Boca Raton; 1991).
23. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276, 307-326 (1997).
24. Cowtan K. DM: an automated procedure for phase improvement by density modification. Joint CCP4 and ESF-EACBM Newslett. Prot. Crystallogr. 31, 34-38 (1994).
25. Murshudov, G.N., Vagin, A.A. & Dodson, E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255 (1997).
26. Elamrani, S., Berry, M.B., Phillips, G.N. & McCammon, J.A. Study of global motions in proteins by weighted masses molecular dynamics: adenylate kinase as a test case. Proteins 25, 79-88 (1996).
27. Brooks, B.R. et al. CHARMM - a program for macromolecular energy, minimization, and dynamics calculations. Comput. Chem. 4, 187-217 (1983).