Electrochemical titrations and reaction time courses monitored in situ by magnetic circular dichroism spectroscopy

Analytical Biochemistry

Volumn 419, Issue 2, 2011, Pages 110-116

  Bradley, Justin M ^a   Butt, Julea N ^a   Cheesman, Myles R ^a  

^a UNIVERSITY OF EAST ANGLIA   (United Kingdom)

Author keywords

Electrochemistry; Magnetic circular dichroism; MCD; Metalloprotein

Indexed keywords

DICHROISM; ELECTROCHEMICAL ELECTRODES; ELECTROCHEMISTRY; INFRARED DEVICES; MAGNETISM; PROTEINS; SOLENOIDS; TITRATION; TRANSITION METALS; VOLTAMMETRY;

ABSORBANCE SPECTROSCOPY; MAGNETIC CIRCULAR DICHROISM SPECTROSCOPY; MAGNETIC CIRCULAR DICHROISMS; METALLOPROTEIN; NEAR-INFRARED WAVELENGTH; POTENTIOMETRIC TITRATIONS; SUPERCONDUCTING SOLENOIDS; TRANSITION METAL SITE;

CIRCULAR DICHROISM SPECTROSCOPY;

METALLOPROTEIN; REAGENT;

ARTICLE; CIRCULAR DICHROISM; ELECTROCHEMICAL ANALYSIS; ELECTRODE; ENVIRONMENTAL TEMPERATURE; HORSE; MAGNETIC CIRCULAR DICHROISM SPECTROSCOPY; NONHUMAN; OXIDATION REDUCTION REACTION; PARACOCCUS PANTOTROPHUS; POTENTIOMETRY; PRIORITY JOURNAL; REACTION TIME; SUPERCONDUCTOR; TITRIMETRY;

SOLENOIDEA;

EID: 80054081208     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2011.07.030     Document Type: Article

References (50)

1. M.R. Cheesman, C. Greenwood, and A.J. Thomson Magnetic circular dichroism of hemoproteins Adv. Inorg. Chem. 36 1991 201 255
2. 3: MCD and EPR studies J. Am. Chem. Soc. 126 2004 4157 4166
3. 3 J. Biol. Chem. 277 2002 20146 20150
4. E.I. Solomon, E.G. Pavel, K.E. Loeb, and C. Campochiaro Magnetic circular dichroism spectroscopy as a probe of the geometric and electronic structure of non-heme ferrous enzymes Coord. Chem. Rev. 144 1995 369 460
5. K. Rupnik, Y.-L. Hu, A.W. Fay, M.W. Ribbe, and B.J. Hales Variable-temperature variable-field magnetic circular dichroism spectroscopic study of NifEN-bound precursor and FeMoco J. Biol. Inorg. Chem. 16 2011 325 332
6. E.M. Walters, and M.K. Johnson Ferredoxin:thioredoxin Reductase: disulfide reduction catalyzed via novel site-specific [4Fe-4S] cluster chemistry Photosynth. Res. 79 2004 249 264
7. P. Hänzelmann, H.L. Hernández, C. Menzel, R. García-Serres, B.H. Huynh, M.K. Johnson, R.R. Mendel, and H. Schindelin Characterization of MOCS1A an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis J. Biol. Chem. 279 2004 34721 34732
8. G. Mitou, C. Higgins, P. Wittung-Stafshede, R.C. Conover, A.D. Smith, M.K. Johnson, J. Gaillard, A. Stubna, E. Münck, and J. Meyer An Isc-type extremely thermostable [2Fe-2S] ferredoxin from Aquifex aeolicus: biochemical spectroscopic and unfolding studies Biochemistry 42 2003 1354 1364
9. K.S. Hadler, N. Mitić, S. H-C. Yip, L.R. Gahan, D.L. Ollis, G. Schenk, and J.A. Larrabee Electronic structure analysis of the dinuclear metal center in the bioremediator glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes Inorg. Chem. 49 2010 2727 2734
10. J.A. Larrabee, C.M. Alessi, E.T. Asiedu, J.O. Cook, K.R. Hoerning, L.J. Klingler, G.S. Okin, S.G. Santee, and T.L. Volkert Magnetic circular dichroism spectroscopy as a probe of geometric and electronic structure of cobalt(II)-substituted proteins: ground-state zero-field splitting as a coordination number indicator J. Am. Chem. Soc. 119 1997 4182 4196
11. E.C. Duin, L. Signor, R. Piskorski, F. Mahlert, M.D. Clay, M. Goenrich, R.K. Thauer, B. Jaun, and M.K. Johnson Spectroscopic investigation of the nickel-containing porphinoid cofactor F430: comparison of the free cofactor in the +1, +2, and +3 oxidation states with the cofactor bound to methyl-coenzyme M reductase in the silent, red, and ox forms J. Biol. Inorg. Chem. 9 2004 563 576
12. M.K. Johnson, I.C. Zambrano, M.H. Czechowski, H.D. Peck Jr. , D.V. DerVartanian, and J. LeGall Low temperature magnetic circular dichroism spectroscopy as a probe for the optical transitions of paramagnetic nickel in hydrogenase Biochem. Biophys. Res. Commun. 128 1985 220 225
13. J.L. Craft, P.W. Ludden, and T.C. Brunold Spectroscopic studies of nickel-deficient carbon monoxide dehydrogenase from Rhodospirillum rubrum: nature of the iron-sulfur clusters Biochemistry 41 2002 1681 1688
14. Z in the enzyme nitrous oxide reductase from Paracoccus pantotrophus Biochem. J. 364 2002 807 815
15. L. Quintanar, J. Yoon, C.P. Aznar, A.E. Palmer, K.K. Andersson, R.D. Britt, and E.I. Solomon Spectroscopic and electronic structure studies of the trinuclear Cu cluster active site of the multicopper oxidase laccase: nature of its coordination unsaturation J. Am. Chem. Soc. 127 2005 13832 13845
16. A.J. Thomson, M.R. Cheesman, and S.J. George Variable-temperature magnetic circular dichroism Methods Enzymol. 226 1993 199 232
17. 1 ground state which models the spectroscopic properties of heme d J. Am. Chem. Soc. 118 1996 7373 7380
18. M.K. Johnson, A.J. Thomson, A.E. Robinson, K.K. Rao, and D.O. Hall Low-temperature magnetic circular dichroism spectra and magnetization curves of 4Fe clusters in iron-sulfur proteins from Chromatium and Clostridium pasteurianum Biochim. Biophys. Acta 667 1981 433 451
19. A.J. Thomson, A.E. Robinson, M.K. Johnson, J.J.G. Moura, I. Moura, A.V. Xavier, and J. LeGall The 3-iron cluster in a ferredoxin from Desulfovibrio gigas: a low-temperature magnetic circular dichroism study Biochim. Biophys. Acta 670 1981 93 100
20. 4] clusters Adv. Inorg. Chem. 47 1999 1 82
21. P.M.A. Gadsby, and A.J. Thomson Assignment of the axial ligands of ferric ion in low-spin hemoproteins by near-infrared magnetic circular dichroism and electron paramagnetic resonance spectroscopy J. Am. Chem. Soc. 112 1990 5003 5011
22. R.M. Jones, F.E. Inscore, R. Hille, and M.L. Kirk Freeze-quench magnetic circular dichroism spectroscopic study of the "very rapid" intermediate in xanthine oxidase Inorg. Chem. 38 1999 4963 4970
23. 1 observed by freeze-quench NIR-MCD spectroscopy Biochem. Biophys. Res. Commun. 279 2000 674 677
24. IV dimer J. Am. Chem. Soc. 129 2007 9049 9065
25. S.J. Marritt, J.H. van Wonderen, M.R. Cheesman, and J.N. Butt Magnetic circular dichroism of hemoproteins with in situ control of electrochemical potential: MOTTLE Anal. Biochem. 359 2006 79 83
26. S.J. Marritt, G.L. Kemp, L. Xiaoe, J.R. Durrant, M.R. Cheesman, and J.N. Butt Spectroelectrochemical characterization of a pentaheme cytochrome in solution and as electrocatalytically active films on nanocrystalline metal-oxide electrodes J. Am. Chem. Soc. 130 2008 8588 8589
27. L. Male, S.J. Marritt, B.C. Berks, M.R. Cheesman, J.H. van Wonderen, S.J. George, and J.N. Butt Protein voltammetry and spectroscopy: integrating approaches Theor. Chem. Account. 19 2008 107 111
28. 1-type nitrite reductase from, and the absence of a copper-type nitrite reductase from, the aerobic denitrifier Thiosphaera pantotropha: the role of pseudoazurin as an electron donor Eur. J. Biochem. 212 1993 377 385
29. 1-heme Biochemistry 36 1997 13611 13616
30. B.F. van Gelder, and E.C. Slater The extinction coefficient of cytochrome c Biochim. Biophys. Acta 58 1962 593 595
31. S.R. Pauleta, F. Guerlesquin, C.F. Goodhew, B. Devreese, J. van Beeumen, A.S. Pereira, I. Moura, and G.W. Pettigrew Paracoccus pantotrophus pseudoazurin is an electron donor to cytochrome c peroxidase Biochemistry 43 2004 11214 11225
32. 1, from Pseudomonas stutzeri and Thiosphaera pantotropha Biochemistry 36 1997 16267 16276
33. 1 from Parococcus pantotrophus exhibits kinetically gated, conformationally dependent, highly cooperative two-electron redox behavior Biochemistry 39 2000 4243 4249
34. 1 Cell 81 1995 369 377
35. T. Horio, T. Higashi, K. Okunuki, H. Matsubara, and T. Yamanaka Purification and properties of cytochrome oxidase from Pseudomonas aeruginosa J. Biol. Chem. 236 1961 944 951
36. 1 interaction in Pseudomonas cytochrome oxidase (nitrite reductase): reappraisal of spectroscopic evidence Biochem. Biophys. Res. Commun. 80 1978 458 463
37. 1, reductive activation and kinetic analysis of a multifunctional respiratory enzyme J. Biol. Chem. 277 2002 3093 3100
38. 1 nitrite reductase with nitrite J. Biol. Chem. 275 2000 33231 33237
39. F.A. Armstrong, A.O. Hill, and N.J. Walton Direct electrochemistry of redox proteins Acc. Chem. Res. 21 1988 407 413
40. E.I. Solomon, and R.G. Hadt Recent advances in understanding blue copper proteins Coord. Chem. Rev. 255 2011 744 789
41. E.I. Solomon, J.W. Hare, D.M. Dooley, J.H. Dawson, and P.J. Stephens Spectroscopic studies of stellacyanin, plastocyanin, and azurin: electronic structure of the blue copper sites J. Am. Chem. Soc. 102 1980 168 178
42. J. Abramson, M. Svensson-Ek, B. Byrne, and S. Iwata Structure of cytochrome c oxidase: a comparison of the bacterial and mitochondrial enzymes Biochim. Biophys. Acta 1544 2001 1 9
43. M.J.F. Suharti, J.F. Strampraad, and Schröder S. de Vries A novel copper-A containing menaquinol NO reductase from Bacillus azotoformans Biochemistry 40 2001 2632 2639
44. J. Simon, O. Einsle, P.M.H. Kroneck, and W.G. Zumft The unprecedented nos gene cluster of Wolinella succinogenes encodes a novel respiratory electron transfer pathway to cytochrome c nitrous oxide reductase FEBS Lett. 569 2004 7 12
45. A: a novel mixed-valence dinuclear copper electron-transfer center J. Am. Chem. Soc. 118 1996 11501 11514
46. 2O reductase and in an inactive protein isolated from a mutant deficient in copper-site biosynthesis Inorg. Chem. 30 1991 3006 3011
47. A-type centers: ligand-field control of ground-state properties related to electron transfer J. Am. Chem. Soc. 120 1998 5246 5263
48. P.M. Paes de Sousa, S.R. Pauleta, M.L. Simões Gonalves, G.W. Pettigrew, I. Moura, M.M. Correia dos Santos, and J.J.G. Moura Mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by P. pantotrophus pseudoazurin: kinetics of intermolecular electron transfer J. Biol. Inorg. Chem. 12 2007 691 698
49. 2 electrodes in kinetic and catalytic analyses of redox proteins Biochem. Soc. Trans. 37 2009 368 372
50. A.J. Gates, G.L. Kemp, C.Y. To, J. Mann, S.J. Marritt, A.G. Mayes, D.J. Richardson, and J.N. Butt The relationship between redox enzyme activity and electrochemical potential: cellular and mechanistic implications from protein film electrochemistry Phys. Chem. Chem. Phys. 13 2011 7720 7731