EXAFS investigation of the active site of iron superoxide dismutase of Escherichia coli and Propionibacterium shermanii

European Biophysics Journal

Volumn 24, Issue 4, 1996, Pages 243-250

  Scherk, C ^a   Schmidt, M ^a   Nolting, H F ^c   Meier, B ^b   Parak, F ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b UNIVERSITY OF VETERINARY MEDICINE HANNOVER   (Germany)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

E. coli; EXAFS; extended X ray absorption fine structure; iron superoxide dismutase; metalloproteins; P. shermanii; SOD; X ray absorption; XAS

Indexed keywords

METALLOPROTEIN; SUPEROXIDE DISMUTASE;

ARTICLE; ROENTGEN SPECTROSCOPY; SPECTROSCOPY;

ESCHERICHIA COLI; PROPIONIBACTERIUM; PROPIONIBACTERIUM FREUDENREICHII SUBSP. SHERMANII;

EID: 0029997688     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00205105     Document Type: Article

References (29)

1. Achterhold K (1995) Ph. D. Thesis, Technical University Munich, Germany
2. Binsted N, Campbell JW, Gurman SJ, Stephenson PC (1991) SERC Daresbury Laboratory EXCURV92 Program, using: Gurman SJ, Binsted N, Ross I (1984) J Phys C 17: 143-151; Gurman SJ, Binsted N, Ross I (1986) J Phys C 19: 1845-1861; Gurman SJ (1988) J Phys C 21: 3699-3717; Joyner RW, Martin KJ, Meehan P (1987) J Phys C 20: 4005-4012; Binsted N, Strange RW, Hasnian SS (1992) Biochemistry 31: 12117-12125
3. Binsted N, Campbell JW, Gurman SJ, Stephenson PC (1991) SERC Daresbury Laboratory EXCURV92 Program, using: Gurman SJ, Binsted N, Ross I (1984) J Phys C 17: 143-151; Gurman SJ, Binsted N, Ross I (1986) J Phys C 19: 1845-1861; Gurman SJ (1988) J Phys C 21: 3699-3717; Joyner RW, Martin KJ, Meehan P (1987) J Phys C 20: 4005-4012; Binsted N, Strange RW, Hasnian SS (1992) Biochemistry 31: 12117-12125
4. Binsted N, Campbell JW, Gurman SJ, Stephenson PC (1991) SERC Daresbury Laboratory EXCURV92 Program, using: Gurman SJ, Binsted N, Ross I (1984) J Phys C 17: 143-151; Gurman SJ, Binsted N, Ross I (1986) J Phys C 19: 1845-1861; Gurman SJ (1988) J Phys C 21: 3699-3717; Joyner RW, Martin KJ, Meehan P (1987) J Phys C 20: 4005-4012; Binsted N, Strange RW, Hasnian SS (1992) Biochemistry 31: 12117-12125
5. Binsted N, Campbell JW, Gurman SJ, Stephenson PC (1991) SERC Daresbury Laboratory EXCURV92 Program, using: Gurman SJ, Binsted N, Ross I (1984) J Phys C 17: 143-151; Gurman SJ, Binsted N, Ross I (1986) J Phys C 19: 1845-1861; Gurman SJ (1988) J Phys C 21: 3699-3717; Joyner RW, Martin KJ, Meehan P (1987) J Phys C 20: 4005-4012; Binsted N, Strange RW, Hasnian SS (1992) Biochemistry 31: 12117-12125
6. Binsted N, Campbell JW, Gurman SJ, Stephenson PC (1991) SERC Daresbury Laboratory EXCURV92 Program, using: Gurman SJ, Binsted N, Ross I (1984) J Phys C 17: 143-151; Gurman SJ, Binsted N, Ross I (1986) J Phys C 19: 1845-1861; Gurman SJ (1988) J Phys C 21: 3699-3717; Joyner RW, Martin KJ, Meehan P (1987) J Phys C 20: 4005-4012; Binsted N, Strange RW, Hasnian SS (1992) Biochemistry 31: 12117-12125
7. Binsted N, Campbell JW, Gurman SJ, Stephenson PC (1991) SERC Daresbury Laboratory EXCURV92 Program, using: Gurman SJ, Binsted N, Ross I (1984) J Phys C 17: 143-151; Gurman SJ, Binsted N, Ross I (1986) J Phys C 19: 1845-1861; Gurman SJ (1988) J Phys C 21: 3699-3717; Joyner RW, Martin KJ, Meehan P (1987) J Phys C 20: 4005-4012; Binsted N, Strange RW, Hasnian SS (1992) Biochemistry 31: 12117-12125
8. Binsted N, Strange RW, Hasnain SS (1992) Constrained and restrained refinement in EXAFS data analysis with curved wave theory. Biochemistry 31: 12117-12125
9. Di Pace A, Cupane A, Leone M, Vitorano E, Cordone L (1992) Vibrational coupling, spectral broading mechanisms and anharmonicity effects in carbonmonoxy heme proteins studied by the temperature dependence of the Soret band line shape. Biophys J 63: 475-484
10. Jones A (1994) O-Program, Version 5.10.2, Uppsala University, Sweden
11. Lah MS, Dixon MM, Pattridge KA, Stallings WC, Fee JA, Ludwig ML (1995) Structure - Function in Escherichia coli Iron Superoxide Dismutase: Comparisons with Manganese Enzyme from Thermus thermophilus. Biochemistry 34: 1646-1660
12. Lee PA, Beni G (1977) New method for the calculation of atomic phase shifts: Application to extended X-ray absorption fine structure (EXAFS) in molecules and crystals. Phys Rev B 15: 2862-2883
13. Ludwig ML, Metzger AL, Pattridge KA, Stallings WC (1991) Manganese superoxide dismutase from Thermus thermophilus: A structural model refined at 1.8 Å resolution. J Mol Biol 219: 335-358
14. Meier B, Barra D, Bossa F, Calabrese L, Rotilio G (1982) Synthesis of either Fe- or Mn-superoxide dismutase with an apparently identical protein moiety by an anaerobic bacterium dependent on the metal supplied. J Biol Chem 257: 13977-13980
15. Meier B, Michel C, Saran M, Huettermann J, Parak F, Rotilio G (1995) Kinetic and spectroscopic studies on a superoxide dismutase from Propionibacterium shermanii which is active with iron or manganese: pH dependence. Biochem J 310:945-950
16. Parak F, Frauenfelder H (1993) Protein dynamics. Physica A 201: 332-345
17. Pettifer RF, Hermes C (1985) Absolute Energy Calibration of X-ray Radiation from Synchrotron Sources. J Appl Crystallogr 18: 404-412
18. Ringe D, Petsko GA, Yamakura F, Suzuki K, Ohmori D (1983) Structure of iron Superoxide dismutase from Pseudomonas ovalis at 2.9 Å resolution. Proc Natl Acad Sci USA 80: 3879-3883
19. Roe AL, Schneider DJ, Mayer RJ, Pyrz JW, Widom J, Que Jr L (1984) X-ray absorption spectroscopy of iron-tyrosinate proteins. J Am Chem Soc 106: 1676-1681
20. Shadle SE, Penner-Hahn JE, Schugar HJ, Hedman B, Hodgson KO, Solomon EI (1993) X-ray Absorption Spectroscopic Studies of Blue Copper Site: Metal and Ligand K-Edge Studies to Probe the Origin of the EPR Hyperfine Splitting in Plastocyanin. J Am Chem Soc 115: 767-776
21. Shulman RG, Yafet Y, Eisenberger P, Blumberg WE (1976) Observation and interpretation of X-ray absorption edges in iron compounds and proteins. Proc Natl Acad Sci USA 73: 1384-1388
22. Stallings WC, Powers TB, Pattridge KA, Fee JA, Ludwig ML (1983) Iron Superoxide dismutase from Escherichia coli at 3.1 Å resolution: A structure unlike that of copper/zinc protein at both monomer and dimer levels. Proc Natl Acad Sci USA 80: 3884-3888
23. Stallings WC, Pattridge KA, Strong RK, Ludwig ML (1984) Manganese and Iron Superoxide Dismutase are structural homologues. J Biol Chem 259: 10695-10699
24. Stallings WC, Pattridge KA, Strong RK, Ludwig ML (1985) The structure of manganese Superoxide dismutase from Thermus thermophilus HB 8 at 2.4 Å resolution. J Biol Chem 260: 16424-16432
25. Stoddard BL, Howell PL, Ringe D, Petsko GA (1990) The 2.1 Å resolution structure of iron Superoxide dismutase from Pseudomonas ovalis. Biochemistry 29: 8885-8893
26. Strange RW, Blackburn NJ, Knowles PF, Hasnian SS (1987) X-ray absorption spectroscopy of metal-histidine coordination in metalloproteins. Exact simulation of the EXAFS of Tetrakis(imidazole)copper(II) Nitrate and other Copper-imidazole complexes by use of a multiple-scattering treatment. J Am Chem Soc 109: 7157-7162
27. Tainer JA, Getzoff ED, Beem KM. Richardson JS, Richardson DC (1982) Determination and Analysis of a 2 Å Structure of Copper, Zinc Superoxide Dismutase. J Mol Biol 160: 181-217
28. Teo BK (1986) EXAFS: Basic Principles and Data Analysis. Springer, Berlin Heidelberg New York
29. Tierney DL, Free JA, Ludwig ML, Penner-Hahn JE (1995) X-ray Absorption Spectroscopy of the Iron Site in Escherichia coli Fe(III) Superoxide Dismutase. Biochemistry 34: 1661-1668