Bovine carbonyl lactoperoxidase structure at 2.0Å resolution and infrared spectra as a function of pH

Protein Journal

Volumn 31, Issue 7, 2012, Pages 598-608

  Singh, Amit K ^a   Smith, Michael L ^b   Yamini, Shavait ^a   Ohlsson, Per Ingvar ^d   Sinha, Mau ^a   Kaur, Punit ^a   Sharma, Sujata ^a   Paul, Jan A K ^c   Singh, Tej P ^a   Paul, K G ^d  

^a ALL INDIA INSTITUTE OF MEDICAL SCIENCES   (India)

^b Jannek Fuel Inc   (United States)

^c Jannek Fuel Inc   (Sweden)

^d UMEÅ UNIVERSITY   (Sweden)

Author keywords

Antimicrobial activity; Carbon monoxide; Heme; Lactoperoxidase; Peroxidase; Protein structure

Indexed keywords

CARBONYL LACTOPEROXIDASE; FERRIC ION; FERROUS ION; HYDROGEN; IMIDAZOLE; LACTOPEROXIDASE; NITROGEN; UNCLASSIFIED DRUG;

ARTICLE; CRYSTALLOGRAPHY; ENZYME STRUCTURE; HYDROGEN BOND; INFRARED RADIATION; PH; PROTEIN BINDING;

ANIMALS; CARBON MONOXIDE; CATTLE; CRYSTALLOGRAPHY, X-RAY; HEME; HYDROGEN-ION CONCENTRATION; LACTOPEROXIDASE; MILK; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PROTEIN CONFORMATION; SPECTROPHOTOMETRY, INFRARED;

BACTERIA (MICROORGANISMS); BOVINAE; MAMMALIA;

EID: 84865626285     PISSN: 15723887     EISSN: 15734943     Source Type: Journal    
DOI: 10.1007/s10930-012-9436-3     Document Type: Article

References (60)

1. CH Barlow P-I Ohlsson K-G Paul 1976 Biochemistry 15 2225 2229 10.1021/bi00655a031 1:CAS:528:DyaE28XktFKgsro%3D
2. AT Brunger PD Adams GM Clore WL DeLano P Gros RW Grosse-Kunstleve JS Jiang J Kuszewski M Nilges NS Pannu RJ Read LM Rice T Simonson GL Warren 1998 Acta Crystallogr D 54 905 921 10.1107/S0907444998003254 1:STN:280: DyaK1cvjslKhsw%3D%3D
3. GH Carlsson P Nicholls D Svistunenko GI Berglund J Hajdu 2005 Biochemistry 44 635 642 10.1021/bi0483211 1:CAS:528:DC%2BD2cXhtVyhsrjJ
4. J Carlsson 1983 Biochem Biophys Res Comm 116 568 573 10.1016/0006- 291X(83)90561-2 1:CAS:528:DyaL3sXmtVyktrc%3D
5. C Ciaccio G De Sancis S Marini F Sinibaldi R Santucci A Arcovito A Bellelli E Ghibaudi PF Rose M Coletta 2004 Biophys J 86 448 454 10.1016/S0006-3495(04)74121-1 1:CAS:528:DC%2BD2cXlsV2ltw%3D%3D
6. GE Conner A Salathe R Forteza 2002 Am J Respir Crit Care Med 166 S57 S61 10.1164/rccm.2206018
7. M Davies CL Hawkins DI Pattison MD Rees 2008 Antioxid Redox Signal 10 1199 1234 10.1089/ars.2007.1927 1:CAS:528:DC%2BD1cXlt1aiurY%3D
8. IW Davis A Leaver-Fay VB Chen JN Block GJ Kapral X Wang LW Murray WB Arendall 3rd J Snoeyink JS Richardson DC Richardson 2007 Nucleic Acids Res 35 W375 W383 10.1093/nar/gkm216
9. J Du M Sono JH Dawson 2010 Biochemistry 49 6064 6069 10.1021/bi100741z 1:CAS:528:DC%2BC3cXotVOmu7k%3D
10. SL Edwards TL Poulos 1990 J Biol Chem 265 2588 2595 1:CAS:528: DyaK3cXhsFCgs7s%3D
11. S El-Chemaly M Salathe S Baier GE Conner R Forteza 2003 Am J Respir Crit Care Med 167 425 430 10.1164/rccm.200206-531OC
12. N Gungœr M Knaapen A Munnia M Peluso GR Haenen RK Chiu RWL Godschalk FJ van Schooten 2010 Mutagenesis 25 149 154 10.1093/mutage/gep053
13. I Holzbaur AM English AA Ismail 1996 J Am Chem Soc 118 3354 3359 10.1021/ja953715o 1:CAS:528:DyaK28Xhslagsbg%3D
14. S Hu RW Treat JR Kincaid 1993 Biochemistry 32 10125 10130 10.1021/bi00089a031 1:CAS:528:DyaK3sXlslKmu7c%3D
15. TA Jones JY Zou SW Cowan M Kjeldgaard 1991 Acta Crystallogr A47 110 119 1:CAS:528:DyaK3MXhvVWlur8%3D
16. RD Kidd HM Baker AJ Mathews T Brittain EN Baker 2001 Protein Sci 10 1739 1749 10.1110/ps.11701 1:CAS:528:DC%2BD3MXmsFSgtbw%3D
17. Klebanoff SJ (1991) In: Everse J, Everse KE, Grisham MB (eds) Peroxidases in chemistry and biology, vol 1. CRC Press, Boca Raton, pp 1-35
18. KD Kussendrager AC van Hooijdonk 2000 Br J Nutr 84 Suppl 1 S19 S25 1:CAS:528:DC%2BD3MXivFKitbo%3D
19. RA Laskowski M Macarthur D Moss J Thornton 1993 J Appl Crystallogr 26 283 290 10.1107/S0021889892009944 1:CAS:528:DyaK3sXit12lurY%3D
20. T Li ML Quillin GN Phillips Jr JS Olson 1994 Biochemistry 33 1433 1446 10.1021/bi00172a021 1:CAS:528:DyaK2cXht1yjtbk%3D
21. GN La Mar JS De Ropp VP Chacko JD Satterlee JE Erman 1982 Biochim Biophys Acta 708 317 325 10.1016/0167-4838(82)90443-5 1:CAS:528:DyaL3sXhtVensbc%3D
22. MT McMahon AC de Dios N Godbout R Salzmann DD Kaws H Le RH Havlin E Oldfield 1998 J Am Chem Soc 120 4784 4797 10.1021/ja973272j 1:CAS:528: DyaK1cXis12qsL0%3D
23. EJ Murphy A Marechal AW Sega PR Rich 2010 Biochemistry 49 2150 2158 10.1021/bi9021507 1:CAS:528:DC%2BC3cXitV2gsbc%3D
24. K Nienhaus GU Nienhaus 2008 Methods Enzymol 437 347 378 10.1016/S0076-6879(07)37018-3 1:CAS:528:DC%2BD1cXntF2ht74%3D
25. K Nienhaus GU Nienhaus 2011 Biochim Biophys Acta 1814 1030 1041 10.1016/j.bbapap.2010.07.018 1:CAS:528:DC%2BC3MXnsVCnsLo%3D
26. LG Oberg B Glas SE Swanson C Rappe K-G Paul 1990 Arch Environ Contam Toxicol 19 930 938 10.1007/BF01055064 1:STN:280:DyaK3M%2Fns1Gksw%3D%3D
27. PI Ohlsson K-G Paul 1980 FEBS Lett 110 200 204 10.1016/0014-5793(80) 80072-X
28. PI Ohlsson K-G Paul 1983 Acta Chem Scand B 37 917 921 10.3891/acta.chem.scand.37b-0917 1:STN:280:DyaL2c7pvVyrsA%3D%3D
29. Z Otwinowski W Minor 1997 Methods Enzymol 276 307 326 10.1016/S0076-6879(97)76066-X 1:CAS:528:DyaK2sXivFehsbw%3D
30. SY Park T Yokoyama N Shibayama Y Shiro JR Tame 2006 J Mol Biol 360 690 701 10.1016/j.jmb.2006.05.036 1:CAS:528:DC%2BD28Xms1anu7g%3D
31. K-G Paul P-I Ohlsson NA Jonsson 1982 Anal Biochem 124 102 107 10.1016/0003-2697(82)90226-3 1:CAS:528:DyaL38XltVGqtL4%3D
32. J Paul ML Smith KG Paul 1985 Biochim Biophysi Acta 832 257 264 10.1016/0167-4838(85)90258-4 1:CAS:528:DyaL28Xks1Shs7c%3D
33. TL Poulos 2010 Arch Biochem Biophys 500 3 12 10.1016/j.abb.2010.02.008 1:CAS:528:DC%2BC3cXosV2itrg%3D
34. GN Ramachandran V Sasisekaran 1968 Adv Protein Chem 23 283 438 10.1016/S0065-3233(08)60402-7 1:CAS:528:DyaE3cXhtFOmsL8%3D
35. MP Roach YP Chen SA Woodin DE Lincoln CR Lovell JH Dawson 1997 Biochemistry 36 2197 2202 10.1021/bi9621371 1:CAS:528:DyaK2sXhvFGgtLs%3D
36. SW Ryter LE Otterbein 2004 Bioessays 26 270 280 10.1002/bies.20005 1:CAS:528:DC%2BD2cXis1Wqsbo%3D
37. MK Safo DJ Abraham 2001 Protein Sci 10 1091 1099 10.1110/ps.48301 1:CAS:528:DC%2BD3MXksFCjsr4%3D
38. Z Salamon JT Hazzard G Tollin 1993 Proc Nat Acad Sci 90 6420 6423 10.1073/pnas.90.14.6420 1:CAS:528:DyaK3sXltlCrsbo%3D
39. JD Satterlee JE Erman 1984 J Am Chem Soc 106 1139 1140 10.1021/ja00316a066 1:CAS:528:DyaL2cXotFyktg%3D%3D
40. IA Sheikh AK Singh N Singh M Sinha SB Singh A Bhushan P Kaur A Srinivasan S Sharma TP Singh 2009 J Biol Chem 284 14849 14856 10.1074/jbc.M807644200 1:CAS:528:DC%2BD1MXmtlChtL4%3D
41. K Shin K Yamauchi S Teraguchi H Hayasawa I Imoto 2002 J Med Miocrobiol 51 231 237 1:CAS:528:DC%2BD38XitFehurk%3D
42. JS Shindler WG Bardsley 1975 Biochem Biophys Res Commun 67 1307 1312 10.1016/0006-291X(75)90169-2 1:CAS:528:DyaE28XlsFyiuw%3D%3D
43. AK Singh RP Kumar N Pandey N Singh M Sinha A Bhushan P Kaur S Sharma TP Singh 2010 J Biol Chem 285 1569 1576 10.1074/jbc.M109.060327 1:CAS:528:DC%2BC3cXkvFCq
44. AK Singh N Pandey M Sinha P Kaur S Sharma TP Singh 2011 Biochem Mol Biol 2 328 339 1:CAS:528:DC%2BC38XlvFWlsQ%3D%3D
45. AK Singh N Singh S Sharma K Shin M Takase P Kaur A Srinivasan TP Singh 2009 Biophys J 96 646 654 10.1016/j.bpj.2008.09.019 1:CAS:528: DC%2BD1MXht12ktrg%3D
46. AK Singh N Singh S Sharma SB Singh P Kaur A Bhushan A Srinivasan TP Singh 2008 J Mol Biol 376 1060 1075 10.1016/j.jmb.2007.12.012 1:CAS:528: DC%2BD1cXhslejurY%3D
47. AK Singh N Singh M Sinha A Bhushan P Kaur A Srinivasan S Sharma TP Singh 2009 J Biol Chem 284 20311 20318 10.1074/jbc.M109.010280 1:CAS:528: DC%2BD1MXos1ensb8%3D
48. AK Singh N Singh A Tiwari M Sinha GS Kushwaha P Kaur A Srinivasan S Sharma TP Singh 2010 J Biol Inorg Chem 15 1099 1107 10.1007/s00775-010-0669-3 1:CAS:528:DC%2BC3cXlvVOmsL8%3D
49. S Singh P Madzelan J Stasser CL Weeks D Becker G Spiro J Penner-Hahn R Banerjee 2009 J Inorgan Biochem 103 689 697 10.1016/j.jinorgbio.2009.01.009 1:CAS:528:DC%2BD1MXkslyisL0%3D
50. ML Smith PI Ohlsson K-G Paul 1983 FEBS Lett 163 303 305 10.1016/0014-5793(83)80840-0 1:CAS:528:DyaL2cXjtFCnsA%3D%3D
51. ML Smith J Paul PI Ohlsson K-G Paul 1984 Biochemistry 23 6776 6785 10.1021/bi00321a076 1:CAS:528:DyaL2MXhvFymsw%3D%3D
52. M Sono JH Dawson M Ikeda-Saito 1986 Biochim Biophys Acta 873 62 72 10.1016/0167-4838(86)90190-1 1:CAS:528:DyaL28Xmt1WltLs%3D
53. TG Spiro PM Kozlowski 2001 Acc Chem Res 34 137 144 10.1021/ar000108j 1:CAS:528:DC%2BD3cXotlKiurc%3D
54. TG Spiro IH Wasbotten 2005 J Inorg Biochem 99 34 44 10.1016/j.jinorgbio. 2004.09.026 1:CAS:528:DC%2BD2cXhtVKksLvI
55. M Tsubaki Y Ichikawa 1985 Biochim Biophys Acta 827 268 274 10.1016/0167-4838(85)90211-0 1:CAS:528:DyaL2MXhsVCqu7o%3D
56. J Vojtechovsky K Chu J Berendzen RM Sweet I Schlichting 1999 Biophys J 77 2153 2174 10.1016/S0006-3495(99)77056-6 1:CAS:528:DyaK1MXmtl2mtrc%3D
57. BA Wagner KA Reszka ML McCormick BE Britigan CB Evig CP Burns 2004 Free Radic Res 38 167 175 10.1080/10715760310001643302 1:CAS:528:DC%2BD2cXhsFKktb0%3D
58. C Xu M Ibrahim TG Spiro 2008 Biochemistry 47 2379 2387 10.1021/bi702254y 1:CAS:528:DC%2BD1cXps1GlsQ%3D%3D
59. ET Yukl BR Goblirsch VL Davidson CM Wilmot 2011 Biochemistry 50 2931 2938 10.1021/bi200023n 1:CAS:528:DC%2BC3MXjtFKqtrk%3D
60. B Zelent T Yano P-I Ohlsson J Paul ML Smith J Vanderkooi 2005 Biochemistry 44 15953 15959 10.1021/bi0513655 1:CAS:528:DC%2BD2MXhtFynurzM