Deactivation of hemeperoxidases by hydrogen peroxide: Focus on compound III

Biocatalysis Based on Heme Peroxidases: Peroxidases as Potential Industrial Biocatalysts

Volumn , Issue , 2010, Pages 291-304

  Valderrama, Brenda ^a  

^a INSTITUTO DE BIOTECNOLOGÍA   (Mexico)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84895263475     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-3-642-12627-7_11     Document Type: Chapter

References (149)

1. DeSimone LD, Popoff F (1997) The business link to sustainable development. MIT, Cambridge, MA
2. Anastas PT, Warner JC (1998) Green chemistry: theory and practice. Oxford University Press, New York, NY
3. Ramos MC, Torrijas MC, Diaz AN (2001) Enhanced chemiluminiscence biosensor for the determination of phenolic compounds and hydrogen peroxide. Sens Actuators 73:71-75
4. Iwuoha EI, Joseph S, Zhang Z et al (1998) Drug metabolism biosensors: electrochemical reactivities of cytochrome P450cam immobilized in synthetic vesicular systems. J Pharm Biomed Anal 17:1101-1110
5. Ingram DT, Lamichhane CM, Rollins DM et al (1998) Development of a colony lift immunoassay to facilitate rapid detection and quantification of Escherichia coli O157:H7 from agar plates and filter monitor membranes. Clin Diagn Lab Immunol 5:567-573
6. Paice MG, Jurasek KL (1984) Peroxidase catalyzed color removal from bleach plant effluent. Biotechnol Bioeng 26:477-480
7. Michel FC, Dass SB, Grulke EA et al (1991) Role of manganese peroxidase and lignin peroxidase of Phanerochaete chrysosporium in the decolorization of Kraft bleach plant effluent. Appl Environ Microbiol 57:2368-2375
8. Ferrer I, Dezotti M, Duran N (1991) Decolorization of Kraft effluent by free and immobilized lignin peroxidases and horseradish peroxidase. Biotechnol Lett 13:577-582
9. Husain Q (2006) Potential applications of the oxidoreductive enzymes in the decolorization and detoxification of textile and other synthetic dyes from polluted water: a review. Crit Rev Biotechnol 26:201-221
10. Xu F (2005) Applications of oxidoreductases: recent progress. Ind Biotechnol 1:38-50
11. Lipovs?ek D, Antipov E, Armstrong KA et al (2007) Selection of horseradish peroxidase variants with enhanced enantioselectivity by yeast surface display. Chem Biol 14:1176-1185
12. van Rantwijk F, Sheldon RA (2000) Selective oxygen transfer catalyzed by heme perox-idases: synthetic and mechanistic aspects. Curr Opin Biotechnol 11:554-564
13. van Deurzen MPJ, van Rantwijk F, Sheldon RA (1997) Selective oxidations catalyzed by peroxidases. Tetrahedron 53:13183-13220
14. Hammel KE, Kayanaraman B, Kirk TK (1986) Oxidation of polycyclic aromatic hydrocarbons and dibenzo(p)dioxins by Phanerochaete chrysosporium ligninase. J Biol Chem 36:16948-16952
15. Hammel KE, Tradone PJ (1988) The oxidative 4-dechlorination of polychlorinated phenols is catalyzed by extracellular fungal lignin peroxidase. Biochemistry 27:6563-6568
16. Field JA, de Jong E, Feijoo-Costa G et al (1993) Screening for ligninolytic fungi applicable to the biodegradation of xenobiotics. Trends Biotechnol 11:44-49
17. Klibanov AM, Tu T-M, Scott KL (1983) Peroxidase catalyzed removal from coal-conversion waste waters. Science 221:259-261
18. Patel M, Day BJ (1999) Metalloporphyrin class of therapeutic catalytic antioxidants. Trends Pharm Sci 20:359-364
19. Gaspar S, Popescu IC, Gazaryan IG et al (2000) Biosensors based on novel plant peroxi-dases: a comparative study. Electrochim Acta 46:255-264
20. Liu W, Kumar J, Tripathy S et al (1999) Enzymatically synthesized conducting polyaniline. J Am Chem Soc 121:71-78
21. Park JB, Clark DS (2006) Deactivation mechanisms of chloroperoxidase during biotransfor-mations. Biotechnol Bioeng 93:1190-1195
22. Valderrama B, Ayala M, Vazquez-Duhalt R (2002) Suicide inactivaction of peroxidases and the challenge of engineering more robust enzymes. Chem Biol 9:555-565
23. Valderrama B, Vazquez-Duhalt R (2005) Electron-balance during the oxidative self-inacti-vation of cytochrome c. J Mol Cat B Enz 35:41-44
24. Valderrama B, Garćia-Arellano H, Giansanti S et al (2006) Oxidative stabilization of iso-1-cytochrome c by redox-inspired protein engineering. FASEB J 20:1233-1235
25. 2. FEBS J 274:3013-3020
26. Ryan BJ, O'Fágáin C (2007) Effects of single mutations on the stability of horseradish peroxidase to hydrogen peroxide. Biochimie 89:1029-1032
27. Mahmoudi A, Nazari K, Khosraneh M et al (2008) Can amino acids protect horseradish peroxidase against its suicide-peroxide substrate? Enzyme Microb Technol 43:329-335
28. Gil-Rodríguez P, Ferreira-Batista CV, Vazquez-Duhalt R et al (2008) A novel heme peroxi-dase from Raphanus sativus intrinsically resistant to hydrogen peroxide. Eng Life Sci 8:286-296
29. Saab-Rincon G, Valderrama B (2009) Protein engineering of redox-active enzymes. Antioxid Redox Signal 11:167-192
30. Dunford HB (1999) Heme peroxidases. Wiley, New York, NY
31. Keilin D, Hartree EF (1951) Purification of horseradish peroxidase and comparison of its properties with those of catalase and methaemoglobin. Biochem J 49:88-106
32. Patterson WR, Poulos TL, Goodin DB (1995) Identification of a porphyrin p-cation radical in ascorbate peroxidase Compound I. Biochemistry 34:4342-4345
33. Roberts JE, Hoffman BM, Rutter R et al (1981) Electron-nuclear double resonance of horseradish peroxidase compound I. Detection of the porphyrin p-cation radical. J Biol Chem 256:2118-2121
34. Hiner ANP, Hernández-Rúiz J, Williams GA et al (2001) Catalase-like oxygen production by horseradish peroxidase must predominantly be an enzyme-catalyzed reaction. Arch Biochem Biophys 392:295-302
35. Iwamoto H, Kobayashi T, Hasegawa E et al (1987) Reaction of human myeloperoxidase with hydrogen peroxide and its true catalase activity. J Biochem 101:1407-1412
36. Hashimoto S, Nakajima R, Yamazaki I et al (1986) Oxygen-exchange between the Fe(IV)/O-Heme and bulk water for the A2 isozyme of horseradish-peroxidase. FEBS Lett 208:305-307
37. IV/O Heme and bulk water during enzymic catalysis of horseradish peroxidase and its relation with the heme-linked ionization. Proc Natl Acad Sci USA 83:2417-2421
38. Cai DY, Tien M (1989) On the reactions of lignin peroxidase compound III (isozyme H8). Biochem Biophys Res Commun 162:464-469
39. 2. J Biol Chem 267:11149-11155
40. Arnao MB, Acosta M, del Rio JA et al (1990) A kinetic study on the suicide inactivation of peroxidase by hydrogen peroxide. Biochim Biophys Acta 1041:43-47
41. Keilin D, Mann T (1937) On the haematin compound of peroxidase. Proc R Soc Lond Ser B Biol Sci 122:119-133
42. Blumberg WE, Peisach J, Wittenberg BA et al (1968) The electronic structure of protoheme proteins. I. An electron paramagnetic resonance and optical study of horseradish peroxidase and its derivatives. J Biol Chem 243:1854-1862
43. Wittenberg JB, Wittenberg BA, Peisach J et al (1970) On the state of the iron and the nature of the ligand in oxyhemoglobin. Proc Natl Acad Sci USA 67:1846-1853
44. Barr DP, Mason RP (1995) Mechanism of radical production from the reaction of cyto-chrome c with organic hydroperoxides-an ESR spin-trapping investigation. J Biol Chem 270:12709-12716
45. Peisach J, Blumberg WE, Wittenberg BA et al (1968) The electronic structure of protoheme proteins. III. Configuration of the heme and its ligands. J Biol Chem 243:1871-1880
46. Wariishi H, Gold MH (1990) Lignin peroxidase compound III. Mechanism of formation and decomposition. J Biol Chem 265:2070-2077
47. Lardinois OM (1995) Reactions of bovine liver catalase with superoxide radicals and hydrogen peroxide. Free Radic Res 22:251-274
48. Lardinois OM, Rouxhet PG (1994) Characterization of hydrogen peroxide and superoxide degrading pathways of Aspergillus niger catalase: a steady-state analysis. Free Radic Res 20:29-50
49. Wariishi H, Akileswaran L, Gold MH (1988) Manganese peroxidase from the basidiomycete Phanerochaete chrysosporium: spectral characterization of the oxidized states and the catalytic cycle. Biochemistry 27:5365-5370
50. Hiner AN, Rodŕiguez-López JN, Arnao MB et al (2000) Kinetic study of the inactivation of ascorbate peroxidase by hydrogen peroxide. Biochem J 348:321-328
51. Hiner AN, Hernández-Ruíz J, Garćia-Cánovas F et al (1995) A comparative study of the inactivation of wild-type, recombinant and two mutant horseradish peroxidase isoenzymes C by hydrogen peroxide and m-chloroperoxybenzoic acid. Eur J Biochem 234:506-512
52. Nakajima R, Yamazaki I (1987) The mechanism of oxyperoxidase formation from ferryl peroxidase and hydrogen peroxide. J Biol Chem 262:2576-2581
53. Adediran SA, Lambeir AM (1989) Kinetics of the reaction of compound II of horseradish peroxidase with hydrogen peroxide to form compound III. Eur J Biochem 186:571-576
54. Shimizu N, Kobayashi K, Hayashi K (1989) Kinetics of the reaction of superoxide anion with ferric horseradish peroxidase. Biochim Biophys Acta 995:133-137
55. Edwards J, Ormsby D (2009) Dissociation constants of inorganic acids in aqueous solutions. Institute of Fundamental Sciences Chemistry Resources. http://ifs.massey.ac.nz/resources/chemistry/dissociation/inorgacids.htm
56. Newmyer SL, Ortíz de Montellano PR (1995) Horseradish peroxidase His-42 →Ala, His-42→Val, and Phe-41→Ala mutants. J Biol Chem 270:19430-19438
57. Shikama K (1998) The molecular mechanism of autoxidation for myoglobin and hemoglobin: a venerable puzzle. Chem Rev 98:1357-1374
58. Poulos TL, Freer ST, Alden RA et al (1980) The crystal structure of cytochrome c peroxi-dase. J Biol Chem 255:575-580
59. Tesoriere L, Allegra M, D'Arpa D et al (2001) Reaction of melatonin with hemoglobin-derived oxoferryl radicals and inhibition of the hydroperoxide- induced hemoglobin denatur-ation in red blood cells. J Pineal Res 31:114-119
60. Jantschko W, Furtmuller PG, Zederbauer M et al (2004) Kinetics of oxygen binding to ferrous myeloperoxidase. Arch Biochem Biophys 426:91-97
61. Jantschko W, Furtmuller PG, Zederbauer M et al (2005) Reaction of ferrous lactoperoxidase with hydrogen peroxide and dioxygen: an anaerobic stopped-flow study. Arch Biochem Biophys 434:51-59
62. Rodríguez-López JN, Smith AT, Thorneley RNF (1997) Effect of distal cavity mutations on the binding and activation of oxygen by ferrous horseradish peroxidase. J Biol Chem 272:389-395
63. Sawada Y, Yamazaki I (1973) One-electron transfer reactions in biochemical systems. 8. Kinetic study of superoxide dismutase. Biochim Biophys Acta 327:257-265
64. Shimizu N, Kobayashi K, Hayashi K (1984) The reaction of superoxide radical with catalase. Mechanism of the inhibition of catalase by superoxide radical. J Biol Chem 259:4414-4418
65. 2 binds to heme-reasons for rapid binding and spin inversion. J Biol Chem 279:14561-14569
66. Van Wart HE, Zimmer J (1985) Resonance Raman evidence for the activation of dioxygen in horseradish oxyperoxidase. J Biol Chem 260:8372-8377
67. Scheidt WR, Reed CA (1981) Spin-state stereochemical relationships in iron porphyrins-implications for the hemoproteins. Chem Rev 81:543-555
68. Metodiewa D, Dunford HB (1992) Spectral studies of intermediate species formed in one-electron reactions of bovine liver catalase at room and low temperatures. A comparison with peroxidase reactions. Int J Rad Biol 62:543-553
69. Cuperus RA, Muijsers AO, Wever R (1986) The superoxide dismutase activity of myeloper-oxidase; formation of compound III. Biochim Biophys Acta 871:78-84
70. 2*: the forgotten radical. DNA Cell Biol 21:251-257
71. Dordick JS, Klibanov AM, Marletta MA (1986) Horseradish peroxidase catalyzed hydro-xylations: mechanistic studies. Biochemistry 25:2946-2951
72. Grey CE, Hedstrom M, Adlercreutz P (2007) A mass spectrometric investigation of native and oxidatively inactivated chloroperoxidase. ChemBioChem 8:1056-1062
73. Barr DP, Aust SD (1994) Conversion of lignin peroxidase compound III to active enzyme by cation radicals. Arch Biochem Biophys 312:511-515
74. Chung N, Aust SD (1995) Inactivation of lignin peroxidase by hydrogen peroxide during the oxidation of phenols. Arch Biochem Biophys 316:851-855
75. Barr DP, Gunther MR, Deterding LJ et al (1996) ESR spin-trapping of a protein-derived tyrosyl radical from the reaction of cytochrome c with hydrogen peroxide. J Biol Chem 271:15498-15503
76. Gunther MR, Tschirret-Guth RA, Witkowska HE et al (1998) Site-specific spin trapping of tyrosine radicals in the oxidation of metmyoglobin by hydrogen peroxide. Biochem J 330:1293-1299
77. DeGray JA, Lassmann G, Curtis JF et al (1992) Spectral analysis of the protein-derived tyrosyl radicals from prostaglandin H synthase. J Biol Chem 267:23583-23588
78. Shi W, Hoganson CW, Espe M et al (2000) Electron paramagnetic resonance and electron nuclear double resonance spectroscopic identification and characterization of the tyrosyl radicals in prostaglandin H synthase 1. Biochemistry 39:4112-4121
79. Hiner ANP, Mart́inez JI, Arnao MB et al (2001) Detection of a tryptophan radical in the reaction of ascorbate peroxidase with hydrogen peroxide. Eur J Biochem 268: 3091-3098
80. Rúiz-Dueñas FJ, Pogni R, Morales M et al (2009) Protein radicals in fungal versatile peroxidase. J Biol Chem 284:7986-7994
81. Blodig W, Doyle WA, Smith AT et al (1998) Autocatalytic formation of a hydroxy group at C beta of Trp171 in lignin peroxidase. Biochemistry 37:8832-8838
82. Doyle WA, Blodig W, Veitch NC et al (1998) Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis. Biochemistry 37:15097-15105
83. Hawkins CL, Davies MJ (2001) Generation and propagation of radical reactions on proteins. Biochim Biophys Acta 1504:196-219
84. Prutz WA (1990) Free radical transfer involving sulphur peptide functions. In: Chatgilialoglu C, Asmus KD (eds) Sulfur-centered reactive intermediates in chemistry and biology. Plenum, New York
85. 2. J Biol Chem 267:8827-8833
86. Giulivi C, Cadenas E (1998) Heme protein radicals: formation, fate and biological consequences. Free Radic Biol Med 24:269-279
87. Davies MJ, Puppo A (1992) Direct detection of a globin-derived radical in leghaemoglobin treated with peroxides. Biochem J 281:197-201
88. 2-mediated cross-linking of sperm whale myoglobin. J Biol Chem 263:17880-17886
89. Zgoda VG, Karuzina II, Archakov AI (1999) Heme and apoprotein modification of cyto-chrome P450 2B4 during its oxidative inactivation in monooxigenase reconstituted system. Free Radic Biol Med 26:620-632
90. Lardinois OM, Medzihradszky KF, Ortiz de Montellano PR (1999) Spin trapping and protein cross-linking of the lactoperoxidase protein radical. J Biol Chem 274:35441-35448
91. Lardinois OM, Ortiz de Montellano PR (2000) EPR spin-trapping of a myeloperoxidase protein radical. Biochem Biophys Res Commun 270:199-202
92. Ruf RAS, Lutz EA, Zigoneanu IG et al (2008) a-Synuclein conformation affects its tyrosine-dependent oxidative aggregation. Biochemistry 47:13604-13609
93. Nagababu E, Rifkind JM (2000) Heme degradation during autoxidation of oxyhemoglobin. Biochem Biophys Res Commun 273:839-845
94. Catalano CE, Choe YS, Ortiz de Montellano PR (1989) Reactions of the protein radical in peroxide-treated myoglobin. Formation of a heme-protein cross-link. J Biol Chem 264: 10534-10541
95. Nakajima R, Yamazaki I (1980) The conversion of horseradish peroxidase C to a verdohe-moprotein by a hydroperoxide derived enzymatically from indole-3-acetic acid and by m-nitroperoxybenzoic acid. J Biol Chem 255:2067-2071
96. Sector A, Zhou W, Ma WC et al (2000) Investigation of the mechanism of action of microperoxidase-11, (MP-11), a potential anti-cataract agent, with hydrogen peroxide and ascorbate. Exp Eye Res 71:183-194
97. He K, Bornheim LM, Falick AM et al (1998) Identification of the heme-modified peptides from cumene hydroperoxide-inactivated cytochrome P450 3A4. Biochemistry 37:17448-17457
98. Lambeir AM, Dunford HB (1985) Oxygen binding to dithionite-reduced chloroperoxidase. Eur J Biochem 147:93-96
99. Chang HC, Holland RD, Bumpus JA et al (1999) Inactivation of Coprinus cinereus peroxi-dase by 4-chloroaniline during turnover: comparison with horseradish peroxidase and bovine lactoperoxidase. Chem Biol Interact 123:197-217
100. Mahy JP, Gaspard S, Delaforge M et al (1994) Reactions of prostaglandin-H synthase with monosubstituted hydrazines and diazenes-formation of iron(II)-diazene and iron(III)-sigma-alkyl or iron(III)-sigma-aryl complexes. Eur J Biochem 226:445-457
101. Sigman JA, Wang X, Lu Y (2001) Coupled oxidation of heme by myoglobin is mediated by exogenous peroxide. J Am Chem Soc 123:6945-6946
102. O'Carra P (1975) Heme-cleavage: biological systems and chemical analogs. In: Smith K (ed) Porphyrin and metalloporphyrins. Elsevier, The Netherlands
103. Brown SB (1976) A model for the formation of bile-pigments isomers in vivo and in vitro. Biochem J 159:23-27
104. Smith AM, Morrison WL, Milham PJ (1982) Oxidation of indole-3-acetic acid by peroxi-dase: involvement of reduced peroxidase and compound III with superoxide as a product. Biochemistry 21:4414-4419
105. Winterbourn CC, Garcia RC, Segal AW (1985) Production of the superoxide adduct of myeloperoxidase (compound III) by stimulated human neutrophils and its reactivity with hydrogen peroxide and chloride. Biochem J 228:583-592
106. Ximenes VF, Catalani LH, Campa A (2001) Oxidation of melatonin and tryptophan by and HRP cycle involving Compound III. Biochem Biophys Res Commun 287:130-134
107. Adediran SA (1996) Kinetics of the formation of p-670 and of the decay of Compound III of horseradish peroxidase. Arch Biochem Biophys 327:279-284
108. Ximenes VF, Silva SO, Rodrigues MR et al (2005) Superoxide-dependent oxidation of melatonin by myeloperoxidase. J Biol Chem 280:38160-38169
109. Ximenes VF, Pessoa AS, Padovan CZ et al (2009) Oxidation of melatonin by AAPH-derived peroxyl radicals: Evidence of a pro-oxidant effect of melatonin. Biochim Biophys Acta 1790:787-792
110. Berglund GI, Carlsson GH, Smith AT et al (2002) The catalytic pathway of horseradish peroxidase at high resolution. Nature 417:463-468
111. Poulos TL, Schuller DJ, Ban N et al (1996) The crystal structure of peanut peroxidase. Structure 4:311-321
112. Nielsen KL, Indiani C, Henriksen A et al (2001) Differential activity and structure of highly similar peroxidases. Spectroscopic, crystallographic, and enzymatic analyses of lignifying Arabidopsis thaliana peroxidase A2 and horseradish peroxidase A2. Biochemistry 40:1103-11021
113. Choinowski T, Blodig W, Winterhalter KH et al (1999) The crystal structure of lignin peroxidase at 1.70 angstrom resolution reveals a hydroxy group on the C-beta of tryptophan 171: A novel radical site formed during the redox cycle. J Mol Biol 286:809-827
114. Sundaramoorthy M, Terner J, Poulos TL (1995) The crystal structure of chloroperoxidase: a heme peroxidase-cytochrome P450 functional hybrid. Structure 3:1367-1378
115. Pecyna MJ, Ullrich R, Bittner B et al (2009) Molecular characterization of aromatic peroxygenase from Agrocybe aegerita. Appl Microbiol Biotechnol 84:885-897
116. Sono M, Roach MP, Coulter ED et al (1996) Heme-containing oxygenases. Chem Rev 96:2841-2888
117. Poulos TL (1996) The role of the proximal ligand in heme enzymes. J Biol Inorg Chem 1:356-359
118. Hsu MC, Woody RW (1971) The origin of the heme Cotton effects in myoglobin and hemoglobin. J Am Chem Soc 93:3515-3525
119. Sugita Y, Nagai M, Yoneyama Y (1971) Circular dichroism of hemoglobin in relation to the structure surrounding the heme. J Biol Chem 246:383-388
120. Nicola NA, Minasian E, Appleby CA et al (1975) Circular dichroism studies of myoglobin and leghemoglobin. Biochemistry 14:5141-5149
121. Strickland EH, Kay E, Shannon LM et al (1968) Peroxidase isoenzymes from horseradish roots. J Biol Chem 243:3560-3565
122. Myer YP, Pande A (1978) Circular dichroism studies of hemoproteins and heme models. The porphyrins 3:271-322
123. Das TK, Mazumdar S, Mitra S (1995) Heme CD as a probe for monitoring local structural changes in hemeproteins: alkaline transition in hemeproteins. J Chem Sci 107:497-503
124. Nozawa T, Kobayashi N, Hatano M et al (1980) Magnetic circular-dichroism on oxygen complexes of hemoproteins-correlation between magnetic circular-dichroism magnitude and electronic-structures of oxygen complexes. Biochim Biophys Acta 626:282-290
125. Vickery L, Nozawa T, Sauer K (1976) Magnetic circular dichroism studies of myoglobin complexes. Correlations with heme spin state and axial ligation. J Am Chem Soc 98:343-350
126. Andersson KK, Barra A-L (2002) The use of high field/frequency EPR in studies of radical and metal sites in proteins and small inorganic models. Spectrochim Acta A 58: 1101-1112
127. Hagen WR (2006) EPR spectroscopy as a probe of metal centres in biological systems. Dalton Trans 2006:4415-4434
128. Ubbink M, Worrall JAR, Canters GW et al (2002) Paramagnetic resonance of biological metal centers. Annu Rev Biophys Biomol Struct 31:393-422
129. Ivancich A, Jakopitsch C, Auer M et al (2003) Protein-based radicals in the catalase-peroxidase of Synechocystis PCC6803: a multifrequency EPR investigation of wild-type and variants on the environment of the heme active site. J Am Chem Soc 125:14093-14102
130. Zucchi MR, Nascimento OR, Faljoni-Alario A et al (2003) Modulation of cytochrome c spin states by lipid acyl chains: a continuous-wave electron paramagnetic resonance (CW-EPR) study of haem iron. Biochem J 370:671-678
131. Wang Y, Van Wart HE (1993) Raman and resonance Raman spectroscopy. Methods Enzymol 226:319-373
132. Spiro TG (1975) Biological applications of resonance Raman-spectroscopy- Heme proteins. Proc R Soc Lond Ser A Math Phys Eng 345:89-105
133. Spiro TG (1988) Biological applications of Raman spectroscopy, vol 3. Resonance Raman spectra of heme proteins and other metalloproteins. Wiley, New York, NY
134. Smulevich G, Feis A, Howes BD (2005) Fifteen years of Raman spectroscopy of engineered heme containing peroxidases: what have we learned? Acc Chem Res 38:433-440
135. 2 stretching modes in oxyhemoglobins. Proc Natl Acad Sci USA 98:479-484
136. Sitter AJ, Reczek CM, Terner J (1986) Comparison of the heme structures of horseradish peroxidase compounds X and II by resonance Raman spectroscopy. J Biol Chem 261: 8638-8642
137. Sitter AJ, Reczek CM, Terner J (1985) Heme-linked ionization of horseradish peroxidase compound II monitored by the resonance Raman Fe (IV)/O stretching vibration. J Biol Chem 260:7515-7522
138. Franzen S, Bohn B, Poyart C et al (1995) Evidence for sub-picosecond heme doming in hemoglobin and myoglobin: a time-resolved resonance Raman comparison of carbon monoxy and deoxy species. Biochemistry 34:1224-1237
139. Zimmer J, Van Wart HE (1982) Resonance Raman spectrum of horseradish peroxidase compound III: comparison with oxyhemoglobin. Biochem Biophys Res Commun 108:977-981
140. 2-binding to heme: electronic structure and spectrum of oxyheme, studied by multiconfigurational methods. J Inorg Biochem 99:45-54
141. Maseras F (2000) The IMOMM method opens the way for the accurate calculation of "real" transition metal complexes. Chem Commun 2000:1821-1827
142. Torrens F (2003) Nature of Fe-III-O-2, Fe-II-CO and Fe-III-CN complexes of hemoprotein models. Polyhedron 22:1091-1098
143. Rovira C, Kunc K, Hutter J et al (1997) Equilibrium geometries and electronic structure of iron-porphyrin complexes: a density functional study. J Phys Chem A 101:8914-8925
144. Tsai TE, Groves JL, Wu CS (1981) Electronic structure of iron-dioxygen bond in oxy Hb A and its isolated oxy and oxy chains. J Chem Phys 74:4306-4314
145. Maeda Y, Morita Y (1967) Mossbauer effect in peroxidase-hydrogen peroxide compounds. Biochem Biophys Res Commun 29:680-685
146. Schulz CE, Rutter R, Sage JT et al (1984) Mossbauer and electron paramagnetic resonance studies of horseradish peroxidase and its catalytic intermediates. Biochemistry 23: 4743-4754
147. Henriksen A, Welinder KG, Gajhede M (1998) Structure of barley grain peroxidase refined at 1.9-A resolution. A plant peroxidase reversibly inactivated at neutral pH. J Biol Chem 273:2241-2248
148. Henriksen A, Mirza O, Indiana C et al (2001) Structure of soybean seed coat peroxidase: a plant peroxidase with unusual stability and haem-apoprotein interactions. Protein Sci 10:108-115
149. Miller MA, Shaw A, Kraut J (1994) 2.2 A structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex. Nat Struct Mol Biol 1:524-531