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Bhagi-Damodaran A, Petrik I, Lu Y. Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities. Isr J Chem. 2016;56:773-790doi: 10.1002/ijch.201600033.
Bhagi-Damodaran, A., Petrik, I., & Lu, Y. (2016). Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities. Israel journal of chemistry, 56773-790. https://doi.org/10.1002/ijch.201600033
Bhagi-Damodaran, Ambika, et al. "Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities." Israel journal of chemistry vol. 56 (2016): 773-790. doi: https://doi.org/10.1002/ijch.201600033
Bhagi-Damodaran A, Petrik I, Lu Y. Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities. Isr J Chem. 2016 Oct;56:773-790. doi: 10.1002/ijch.201600033. Epub 2016 Sep 16. PMID: 27994254; PMCID: PMC5161413.
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Isr J Chem. 2016 Oct;56:773-790. doi: 10.1002/ijch.201600033. Epub 2016 Sep 16.

Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities.

Israel journal of chemistry

Ambika Bhagi-Damodaran, Igor Petrik, Yi Lu

Affiliations

  1. Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL. 61801.

PMID: 27994254 PMCID: PMC5161413 DOI: 10.1002/ijch.201600033

Abstract

In biology, a heme-Cu center in heme-copper oxidases (HCOs) is used to catalyze the four-electron reduction of oxygen to water, while a heme-nonheme diiron center in nitric oxide reductases (NORs) is employed to catalyze the two-electron reduction of nitric oxide to nitrous oxide. Although much progress has been made in biochemical and biophysical studies of HCOs and NORs, structural features responsible for similarities and differences within the two enzymatic systems remain to be understood. Here, we discuss the progress made in the design and characterization of myoglobin-based enzyme models of HCOs and NORs. In particular, we focus on use of these models to understand the structure-function relations between HCOs and NORs, including the role of nonheme metals, conserved amino acids in the active site, heme types and hydrogen-bonding network in tuning enzymatic activities and total turnovers. Insights gained from these studies are summarized and future directions are proposed.

References

  1. J Am Chem Soc. 2010 Sep 22;132(37):12794-5 - PubMed
  2. J Am Chem Soc. 2005 Nov 2;127(43):15161-7 - PubMed
  3. J Am Chem Soc. 2005 Nov 30;127(47):16541-7 - PubMed
  4. Biochim Biophys Acta. 2004 Apr 12;1655(1-3):298-305 - PubMed
  5. Biochem J. 1998 Apr 15;331 ( Pt 2):459-64 - PubMed
  6. Proc Natl Acad Sci U S A. 1998 Jul 7;95(14):8020-5 - PubMed
  7. Proc Natl Acad Sci U S A. 2009 Jun 30;106(26):10528-33 - PubMed
  8. J Am Chem Soc. 2006 May 31;128(21):6766-7 - PubMed
  9. J Am Chem Soc. 2009 Oct 14;131(40):14493-507 - PubMed
  10. Biochemistry. 1997 Oct 21;36(42):13034-42 - PubMed
  11. J Am Chem Soc. 2014 Feb 12;136(6):2420-31 - PubMed
  12. Proc Natl Acad Sci U S A. 2008 Oct 14;105(41):15660-5 - PubMed
  13. Proc Natl Acad Sci U S A. 2006 Oct 31;103(44):16135-40 - PubMed
  14. Proteins. 2014 Jul;82(7):1258-71 - PubMed
  15. Chem Rev. 1996 Nov 7;96(7):2951-2964 - PubMed
  16. IUBMB Life. 2013 Mar;65(3):217-26 - PubMed
  17. J Am Chem Soc. 2015 Sep 16;137(36):11570-3 - PubMed
  18. Philos Trans R Soc Lond B Biol Sci. 2012 May 5;367(1593):1195-203 - PubMed
  19. Biochemistry. 2005 Aug 16;44(32):10766-75 - PubMed
  20. J Bioenerg Biomembr. 1993 Apr;25(2):121-36 - PubMed
  21. J Am Chem Soc. 2016 Feb 3;138(4):1134-7 - PubMed
  22. J Am Chem Soc. 2001 Feb 21;123(7):1403-15 - PubMed
  23. Science. 1998 Jun 12;280(5370):1723-9 - PubMed
  24. Eur J Biochem. 2001 Dec;268(24):6486-91 - PubMed
  25. J Am Chem Soc. 2014 Aug 27;136(34):11882-5 - PubMed
  26. Science. 2010 Jul 16;329(5989):327-30 - PubMed
  27. Proc Natl Acad Sci U S A. 2010 May 11;107(19):8581-6 - PubMed
  28. Biochim Biophys Acta. 2001 Mar 1;1504(1):46-57 - PubMed
  29. Science. 1989 Jan 6;243(4887):69-72 - PubMed
  30. Biochim Biophys Acta. 2007 May;1767(5):387-92 - PubMed
  31. EMBO J. 2000 Apr 17;19(8):1766-76 - PubMed
  32. Biochemistry. 2011 Jul 5;50(26):5939-47 - PubMed
  33. Curr Opin Chem Biol. 1999 Apr;3(2):207-19 - PubMed
  34. Nature. 1992 Mar 26;356(6367):301-9 - PubMed
  35. Biochemistry. 2005 May 3;44(17):6559-64 - PubMed
  36. Biochim Biophys Acta. 1997 Aug 22;1321(2):107-27 - PubMed
  37. Biochim Biophys Acta. 2013 Jul;1827(7):826-33 - PubMed
  38. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10733-7 - PubMed
  39. Biochemistry. 1986 Jan 14;25(1):161-7 - PubMed
  40. Nature. 2009 Dec 24;462(7276):1079-82 - PubMed
  41. Biochemistry. 2002 Oct 29;41(43):13046-52 - PubMed
  42. J Bioenerg Biomembr. 2008 Oct;40(5):521-31 - PubMed
  43. Biochemistry. 1998 Oct 13;37(41):14471-6 - PubMed
  44. Biochemistry. 2004 May 25;43(20):6330-8 - PubMed
  45. J Biol Chem. 1998 Dec 4;273(49):32475-8 - PubMed
  46. Biochem J. 2007 Jan 1;401(1):111-9 - PubMed
  47. Biochem J. 2013 May 1;451(3):389-94 - PubMed
  48. Biochem Biophys Res Commun. 2007 Apr 6;355(2):587-91 - PubMed
  49. Appl Environ Microbiol. 2008 Feb;74(4):1145-56 - PubMed
  50. J Inorg Biochem. 2000 Nov;82(1-4):1-7 - PubMed
  51. Chem Rev. 2004 Feb;104(2):1077-133 - PubMed
  52. J Biol Chem. 2003 Aug 22;278(34):31473-8 - PubMed
  53. Proc R Soc Lond B Biol Sci. 1978 May 16;201(1144):285-300 - PubMed
  54. Biochemistry. 2006 Dec 26;45(51):15405-10 - PubMed
  55. J Am Chem Soc. 2002 Feb 27;124(8):1798-808 - PubMed
  56. J Am Chem Soc. 2010 Jul 28;132(29):9970-2 - PubMed
  57. Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):3629-34 - PubMed
  58. Nature. 2009 Nov 5;462(7269):113-6 - PubMed
  59. Inorg Chem. 2010 Apr 19;49(8):3567-72 - PubMed
  60. Biochemistry. 1998 Nov 10;37(45):15896-907 - PubMed
  61. Biofizika. 1980 Mar-Apr;25(2):203-7 - PubMed
  62. Proc Natl Acad Sci U S A. 1997 Sep 30;94(20):10547-53 - PubMed
  63. Nat Commun. 2015 Oct 12;6:8467 - PubMed
  64. Protein Sci. 1999 May;8(5):985-90 - PubMed
  65. Angew Chem Int Ed Engl. 2012 Apr 27;51(18):4312-6 - PubMed
  66. Chem Rev. 1996 Nov 7;96(7):2889-2908 - PubMed
  67. J Bacteriol. 2001 Jan;183(1):189-99 - PubMed
  68. Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14718-23 - PubMed
  69. J Org Chem. 2004 May 14;69(10):3546-9 - PubMed
  70. Biochemistry. 1999 Oct 19;38(42):13780-6 - PubMed
  71. Chem Biodivers. 2008 Aug;5(8):1437-48 - PubMed
  72. J Am Chem Soc. 2015 Apr 15;137(14):4594-7 - PubMed
  73. Biochem Biophys Res Commun. 1995 Jul 26;212(3):1054-60 - PubMed
  74. Proc Natl Acad Sci U S A. 2012 May 8;109(19):7286-91 - PubMed
  75. J Bioenerg Biomembr. 1998 Feb;30(1):55-62 - PubMed
  76. J Biol Chem. 2009 Apr 24;284(17):11301-8 - PubMed
  77. Biochemistry. 2014 Aug 5;53(30):4894-903 - PubMed
  78. Biochemistry. 2016 Apr 12;55(14 ):2091-9 - PubMed
  79. Science. 2010 Nov 19;330(6007):1075-8 - PubMed
  80. Biochim Biophys Acta. 1997 Jan 16;1318(1-2):202-16 - PubMed
  81. Biochim Biophys Acta. 2012 Apr;1817(4):629-37 - PubMed
  82. J Inorg Biochem. 2009 May;103(5):845-50 - PubMed
  83. Chem Rev. 2010 Dec 8;110(12):7062-81 - PubMed
  84. Angew Chem Int Ed Engl. 2012 Jun 4;51(23):5589-92 - PubMed
  85. Arch Biochem Biophys. 2011 Mar 1;507(1):36-43 - PubMed
  86. FEBS Lett. 2004 Jun 1;567(1):103-10 - PubMed

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