Quantitative interpretation of EPR spectroscopy with applications for iron-sulfur proteins

Iron-Sulfur Clusters in Chemistry and Biology

Volumn , Issue , 2014, Pages 21-48

  Petasis, Doros T ^a   Hendrich, Michael P ^b  

^a ALLEGHENY COLLEGE   (United States)

^b CARNEGIE MELLON UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84979146472     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1515/9783110308426.21     Document Type: Chapter

References (42)

1. Eaton GR, Eaton SS, Salikhov KM. Foundations of modern EPR. Singapore, World Scientific; 1998.
2. Abragam A, Bleaney B. Electron paramagnetic resonance of transition ions. Oxford: Clarendon Press; 1970.
3. Carrington A, McLachlan AD. Introduction to magnetic resonance with applications to chemistry and chemical physics. New York: Harper & Row; 1967.
4. Pake GE, Estle TL. In: Benjamin WA, ed. The physical principles of electron paramagnetic resonance. 2nd ed. Reading (MA); 1973.
5. Pilbrow JR. Transition ion electromagnetic resonance. New York: Oxford University Press; 1990.
6. Weil JA, Bolton JR, Wertz JE. Electron paramagnetic resonance: elementary theory and practical applications. New York: Wiley; 1994.
7. Palmer G. Electron paramagnetic resonance of metalloproteins. In: Que L Jr, ed. Physical methods in bioinorganic chemistry. University Science Books; 2000:121-185.
8. Gaffney BJ. EPR of Mononuclear non-heme iron proteins. In: Hanson G, Berliner L, eds. Biological magnetic resononance. New York: Springer; 2009:233-268.
9. Brudvig GW. Electron paramagnetic resonance spectroscopy. In: Sauer K, ed. Methods in enzymology. New York: Academic Press; 1995:536-554.
10. Hagen WR. Practical approaches to biological inorganic chemistry. In: Crichton RR, Louro RO, eds. EPR spectroscopy. Oxford: Elsevier; 2013:53-75.
11. Cammack R, MacMillan F. Electron magnetic resonance of iron-sulfur proteins in electron-transfer chains: resolving complexity. In: Hanson G, Berliner L, eds. Metals in biology. New York: Springer; 2010:11-44.
12. Guigliarelli B, Bertrand P. Application of EPR spectroscopy to the structural and functional study of iron-sulfur proteins. Adv Inorg Chem 1999;47:421-497.
13. Hagen WR. Probing the iron/sulfur domain with EPR: Pandora's box ajar. ACS Conference Proceedings 1987;459-466.
14. n: n-side electron and proton transfer reactions. In: Fromme P, ed. Photosynthetic protein complexes: a structural approach. Weinheim: Wiley-VCH; 2008:155-179.
15. Golombek AP, Hendrich MP. Quantitative analysis of dinuclear manganese(II) EPR spectra. J Magn Reson 2003;165:33-48.
16. Gunderson WA, Zatsman AI, Emerson JP, Farquhar ER, Que L Jr., Lipscomb JD, Hendrich MP. Electron paramagnetic resonance detection of intermediates in the enzymatic cycle of an extradiol dioxygenase. J Am Chem Soc 2008;130:14465-14467.
17. Gupta R, Fu R, Liu A, Hendrich MP. EPR and Mossbauer spectroscopy show inequivalent hemes in tryptophan dioxygenase. J Am Chem Soc 2010;132:1098-1109.
18. Hendrich MP, Debrunner PG. Integer-spin electron paramagnetic resonance of iron proteins. Biophys J 1989;56:489-506.
19. Hendrich MP, Gunderson W, Behan RK, Green MT, Mehn MP, Betley TA, Lu CC, Peters JC. On the feasibility of N2 fixation via a single-site FeI/FeIV cycle: spectroscopic studies of FeI(N2)FeI, FeIV[triple bond]N, and related species. Proc Natl Acad Sci USA 2006;103:17107-17112.
20. Hendrich MP, Munck E, Fox BG, Lipscomb JD. Integer-spin EPR studies of the fully reduced methane monooxygenase hydroxylase component. J Am Chem Soc 1990;112:5861-5865.
21. Hendrich MP, Petasis D, Arciero DM, Hooper AB. Correlations of structure and electronic properties from EPR spectroscopy of hydroxylamine oxidoreductase. J Am Chem Soc 2001;123:2997-3005.
22. Hudder BN, Morales JG, Stubna A, Munck E, Hendrich MP, Lindahl PA. Electron paramagnetic resonance and Mossbauer spectroscopy of intact mitochondria from respiring Saccharomyces cerevisiae. J Biol Inorg Chem 2007;12:1029-1053.
23. Lacy DC, Gupta R, Stone KL, Greaves J, Ziller JW, Hendrich MP, Borovik AS. Formation, structure, and EPR detection of a high spin Fe(IV)-oxo species derived from either an Fe(III)-oxo or Fe(III)-OH complex. J Am Chem Soc 2010;132:12188-12190.
24. Lee D, Du Bois J, Petasis D, Hendrich MP, Krebs C, Huynh BH, Lippard SJ. Formation of Fe(III) Fe(IV) species from the reaction between a Diiron(II) complex and dioxygen: relevance to ribonucleotide reductase intermediate X. J Am Chem Soc 1999;121:9893-9894.
25. Mbughuni MM, Chakrabarti M, Hayden JA, Bominaar EL, Hendrich MP, Munck E, Lipscomb JD. Trapping and spectroscopic characterization of an FeIII-superoxo intermediate from a nonheme mononuclear iron-containing enzyme. Proc Natl Acad Sci USA 2010;107:16788-16793.
26. Parsell TH, Behan RK, Green MT, Hendrich MP, Borovik AS. Preparation and properties of a monomeric Mn(IV)-oxo complex. J Am Chem Soc 2006;128:8728-8729.
27. Petasis DT, Hendrich MP. A new Q-band EPR probe for quantitative studies of even electron metalloproteins. J Magn Reson 1999;136:200-206.
28. Pierce BS, Elgren TE, Hendrich MP. Mechanistic implications for the formation of the Diiron cluster in ribonucleotide reductase provided by quantitative EPR spectroscopy. J Am Chem Soc 2003;125:8748-8759.
29. Sanakis Y, Petasis D, Petrouleas V, Hendrich M. Simultaneous binding of fluoride and NO to the nonheme iron of photosystem II: quantitative EPR evidence for a weak exchange interaction between the semiquinone QA- and the iron-nitrosyl complex. J Am Chem Soc 1999;121: 9155-9164.
30. Upadhyay AK, Petasis DT, Arciero DM, Hooper AB, Hendrich MP. Spectroscopic characterization and assignment of reduction potentials in the tetraheme cytochrome c554 from nitrosomonas europaea. J Am Chem Soc 2003;125:1738-1747.
31. Zatsman AI, Zhang H, Gunderson WA, Cramer WA, Hendrich MP. Heme-heme interactions in the cytochrome b6f complex: EPR spectroscopy and correlation with structure. J Am Chem Soc 2006;128:14246-14247.
32. Orton JW. Electron paramagnetic resonance: an introduction to transition group ions in crystals. Iliffe; 1968.
33. Bencini A, Gatteschi D. Electron paramagnetic resonance of exchange coupled systems. Berlin, New York: Springer-Verlag; 1990.
34. Poole CP. Electron Spin Resonance: A comprehensive treatise on experimental techniques. 2nd ed. New York: Wiley; 1983.
35. Fox BG, Hendrich MP, Surerus KK, Andersson KK, Froland WA, Lipscomb JD, Munck E. Moessbauer, EPR, and ENDOR studies of the hydroxylase and reductase components of methane monooxygenase from Methylosinus trichosporium OB3b. J Am Chem Soc 1993;115:3688-3701.
36. Aasa R, Vanngard T. EPR signal intensity and powder shapes. Reexamination. J Magn Reson 1975;19:308-315.
37. Schulz C, Debrunner PG. Rubredoxin, a simple iron-sulfur protein: its spin Hamiltonian and hyperfine parameters. J Phy Colloq 1976;153-158.
38. Yoo SJ, Meyer J, Achim C, Peterson J, Hendrich MP, Munck E. Mossbauer, EPR, and MCD studies of the C9S and C42S variants of Clostridium pasteurianum rubredoxin and MCD studies of the wild-type protein. J Biol Inorg Chem 2000;5:475-487.
39. Hendrich MP, Debrunner PG. EPR of non-Kramers systems in biology. In: Eaton E, Salikhov ed. Foundations of modern EPR. London: World Scientific; 1998:530-547.
40. Muenck E, Surerus KK, Hendrich MP. Combining Moessbauer spectroscopy with integer spin electron paramagnetic resonance. Methods Enzymol 1993;227:463-479.
41. Yoo SJ, Angove HC, Burgess BK, Hendrich MP, Muenck E. Moessbauer and integer-spin EPR studies and spin-coupling analysis of the [4Fe-4S]0 cluster of the Fe protein from azotobacter vinelandii nitrogenase. J Am Chem Soc 1999;121:2534-2545.
42. Surerus KK, Hendrich MP, Christie PD, Rottgardt D, Orme-Johnson WH, Munck E. Moessbauer and integer-spin EPR of the oxidized P-clusters of nitrogenase: POX is a non-Kramers system with a nearly degenerate ground doublet. J Am Chem Soc 1992;114:8579-8590.