Human deoxyhypusine hydroxylase, an enzyme involved in regulating cell growth, activates O2 with a nonheme diiron center

Proceedings of the National Academy of Sciences of the United States of America

Volumn 106, Issue 35, 2009, Pages 14814-14819

  Vu, Van V ^a   Emerson, Joseph P ^a,d   Martinho, Marlène ^b   Yeon, Sook Kim ^c,e   Münck, Eckard ^b   Myung, Hee Park ^c   Que Jr , Lawrence ^a  

^a University of Minnesota   (United States)

^b CARNEGIE MELLON UNIVERSITY   (United States)

^c NATIONAL INSTITUTE OF DENTAL AND CRANIOFACIAL RESEARCH   (United States)

^d MISSISSIPPI STATE UNIVERSITY   (United States)

^e Chongju University   (South Korea)

Author keywords

DOHH; eIF5A; Oxygen activation; Peroxo intermediate

Indexed keywords

(MU 1,2 PEROXO)DIIRON; CARBOXYLIC ACID DERIVATIVE; DEOXYHYPUSINE; FERRIC ION; HISTIDINE; METHANE; NONHEME IRON PROTEIN; OXIDOREDUCTASE; OXYGEN; OXYGENASE; RECOMBINANT ENZYME; RIBONUCLEASE; TOLUENE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

ARTICLE; CELL GROWTH; CHROMATOPHORE; HUMAN; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN STRUCTURE; RAMAN SPECTROMETRY; ULTRAVIOLET SPECTROSCOPY;

CELL PROLIFERATION; ENZYME ACTIVATION; HUMANS; HYDROXYLATION; IRON; MIXED FUNCTION OXYGENASES; OXYGEN; PEPTIDE INITIATION FACTORS; RNA-BINDING PROTEINS; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); EUKARYOTA; MAMMALIA;

EID: 70349266069     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0904553106     Document Type: Article

References (53)

1. Park MH (2006) The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor5A(eIF5A). J Biochem 139:161-169.
2. Wolff EC, Kang KR, Kim YS, Park MH (2007) Posttranslational synthesis of hypusine: Evolutionary progression and specificity of the hypusine modification. Amino Acids 33:341-350.
3. Byers TL, Lakanen JR, Coward JK, Pegg AE (1994) The role of hypusine depletion in cytostasis induced by S-adenosyl-L-methionine dercarboxylase inhibition: New evidence provided by 1-methylspermidine and 1,12- dimethylspermidine. Biochem J 303:363-368.
4. Park MH, Wolff EC, Leea YB, Folk JE (1994) Antiproliferative effects of inhibitors of deoxyhypusine synthase: Inhibition of growth of Chinese hamster ovary cells by guanul diamines. J Biol Chem 269:27827-27832. (Pubitemid 24982988)
5. Hanauske-Abel HM, et al. (1994) Inhibition of the G1-S transition of the cell cycle by inhibitors of deoxyhypusine hydroxylation. Biochim Biophys Acta 1221:115-124.
6. Clement PMJ, Hanauske-Abel HM, Wolff EC, Kleinman HK, Park MH (2002) The antifungal drug ciclopirox inhibits deoxyhypusine and proline hydroxylation, endothelial cell growth and angiogenesis in vitro. Int J Cancer 100:491-498.
7. Andrus L, et al. (1998) Antiretroviral effects of deoxyhypusyl hydroxylase Inhibitors: A hypusine-dependent host cell mechanism for replication of human immunodeficiency virus type 1 (HIV-1). Biochem Pharmacol 55:1807-1818. (Pubitemid 28305263)
8. Kim YS, et al. (2006) Deoxyhypusine hydroxylase is a Fe(II)-dependent, HEAT-repeat enzyme. Identification of amino acid residues critical for Fe(II) binding catalysis. J Biol Chem 281:13217-13225.
9. Park J-H, et al. (2006) Molecular cloning, expression, and structural prediction of deoxyhypusine hydroxylase: A HEAT-repeat-containing metalloenzyme. Proc Natl Acad Sci USA 103:51-56.
10. Notomista E, Lahm A, Di Donato A, Tramontano A (2003) Evolution of bacterial and archaeal multicomponent monooxygenases. J Mol Evol 56:435-445. (Pubitemid 36390774)
11. Leahy JG, Batchelor PJ, Morcomb SM (2003) Evolution of the soluble diiron monooxygenases. FEMS Microbiol Rev 27:449-479.
12. Wallar BJ, Lipscomb JD (1996) Dioxygen activation by enzymes containing binuclear non-heme iron clusters. Chem Rev 96:2625-2657. (Pubitemid 126641115)
13. 9 desaturase: Oxidase reactivity during single turnover and implications for the mechanism of desaturation. Biochemistry 37:14664-14671.
14. Broadwater JA, Achim C, Münck E, Fox BG (1999) Mössbauer studies of the formation and reactivity of a quasi-stable peroxo intermediate of stearoyl-acyl carrier protein Δ9-desaturase. Biochemistry 38:12197-12204. (Pubitemid 29453279)
15. peroxo, the putative peroxodiiron(III) complex from the methane monooxygenase catalytic cycle. J Am Chem Soc 120:1094-1095.
16. Baldwin J, et al. (2003) Structural characterization of the peroxodiiron(III) intermediate generated during oxygen activation by the W48A/D84E variant of ribonucleotide reductase protein R2 from Escherichia coli. Biochemistry 42:13269-13279. (Pubitemid 37420680)
17. Moenne-Loccoz P, Baldwin J, Ley BA, Loehr TM, Bollinger JM, Jr (1998)O2 activation by non-heme diiron proteins: Identification of a symmetric μ-1,2-peroxide in amutant of ribonucleotide reductase. Biochemistry 37:14659-14663.
18. 2 activation by binuclear non-heme iron enzymes. J Am Chem Soc 126:8842-8855.
19. Yun D, et al. (2007) (μ-1,2-peroxo)diiron(III/III) complex as a precursor to the diiron(III/IV) intermediate X in the assembly of the iron-radical cofactor of ribonucleotide reductase from mouse. Biochemistry 46:1925-1932. (Pubitemid 46272956)
20. 2-activating non-heme diiron proteins. Biochemistry 38:5290-5295.
21. Hwang J, et al. (2000) A short Fe-Fe distance in peroxodiferric ferritin: Control of Fe substrate versus cofactor decay? Science 287:122-125.
22. Kurtz DM, Jr, Shriver DF, Klotz IM (1976) Resonance Raman spectroscopy with unsymmetrically isotopica ligands. Differentiation of possible structures of hemerythrin complexes. J Am Chem Soc 98:5033-5035.
23. Liu KE, et al. (1995) Characterization of a diiron(III) peroxide intermediate in the reaction cycle of methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath). J Am Chem Soc 117:4997-4998.
24. Krebs C, Bollinger JM, Jr, Theil EC, Huynh BH (2002) Exchange coupling constant J of peroxodiferric reaction intermediates determined by Mössbauer spectroscopy. J Biol Inorg Chem 7:863-869. (Pubitemid 36056370)
25. Pereira AS, et al. (1998) Direct spectroscopic and kinetic evidence for the involvement of a peroxodiferric intermediate during the ferroxidase reaction in fast ferritin mineralization. Biochemistry 37:9871-9876.
26. Murray LJ, Garcia-Serres R, Naik S, Huynh BH, Lippard SJ (2006) Dioxygen activation at non-heme diiron centers: Characterization of intermediates in a mutant form of toluene/o-xylene monooxygenase hydroxylase. J Am Chem Soc 128:7458-7459. (Pubitemid 43877517)
27. Okamura MY, Klotz IM, Johnson CE, Winter MRC, Williams RJP (1969) The state of iron in hemerythrin. A Mössbauer study. Biochemistry 8:1951-1958.
28. Dawson JW, et al. (1972) A magnetic susceptibility study of hemerythrin using an ultrasensitive magnetometer. Biochemistry 11:461-465.
29. Kitajima N, et al. (1994) Monomeric carboxylate ferrous complexes as models for the dioxygen binding sites in non-heme iron proteins. The reversible formation and characterization of μ-peroxo diferric complexes. J Am Chem Soc 116:9071-9085. (Pubitemid 2142702)
30. Kim K, Lippard SJ (1996) Structure and Mössbauer spectrum of a (μ-1,2-peroxo)bis(μ- carboxylato)diiron(III) model for the peroxo intermediate in the methane monooxygenase hydroxylase reaction cycle. J Am Chem Soc 118:4914-4915. (Pubitemid 26186564)
31. 2 adduct: Insight into the mechanism of oxygen activation. Angew Chem Int Ed (Engl) 35:618-620.
32. Fiedler AT, et al. (2008) Spectroscopic and computational studies of (μ-Oxo)(μ-1,2- peroxo)diiron(III) complexes of relevance tononhemediiron oxygenase intermediates. J Phys Chem A 112:13037-13044.
33. Zhang X, et al. (2005) Structural and spectroscopic characterization of (μ-hydroxo or μ-oxo)(μ-peroxo)diiron(III) complexes: Models for peroxo intermediates of non-heme diiron proteins. J Am Chem Soc 127:826-827.
34. Ookubo T, et al. (1996) cis-μ-1,2-peroxo diiron complex: Structure and reversible oxygenation. J Am Chem Soc 118:701-702. (Pubitemid 126532521)
35. DeWitt JG, et al. (1991) X-ray absorption, Mössbauer, and EPR studies of the dinuclear iron center in the hydroxylase component of methane monooxygenase. J Am Chem Soc 113:9219-9235.
36. Roe AL, et al. (1984) X-ray absorption spectroscopy of iron-tyrosinate proteins. J Am Chem Soc 106:1676-1681.
37. Shu L, et al. (1998) EXAFS and Mössbauer characterization of the diiron(III) site in stearoyl-acyl carrier protein Δ9-desaturase. J Biol Inorg Chem 3:392-400. (Pubitemid 28381443)
38. True AE, Scarrow RC, Randall CR, Holz RC, Que L, Jr (1993) EXAFS studies of uteroferrin and its anion complexes. J Am Chem Soc 115:4246-4255.
39. Scarrow RC, et al. (1987) EXAFS studies of binuclear iron proteins: Hemerythrin and ribonucleotide reductase. J Am Chem Soc 109:7857-7864.
40. Kurtz DM, Jr (1997) Structural similarity and functional diversity in diiron-oxo proteins. J Biol Inorg Chem 2:159-167.
41. Kurtz DM, Jr (1990) Oxo- and hydroxo-bridged diiron complexes: A chemical perspective on a biological unit. Chem Rev 90:585-606.
42. 0 transformation in the oxygen-evolving complex in photosynthesis. J Am Chem Soc 112:6387-6388.
43. + active sites of plant-type ferredoxins. J Am Chem Soc 118:8085-8097.
44. 2 activation by non-heme iron enzymes. J Am Chem Soc 120:5674-5690.
45. Liu Y, Nesheim JC, Lee S-K, Lipscomb JD (1995) Gating effects of component B on oxygen activation by the methane monooxygenase hydroxylase component. J Biol Chem 270:24662-24665.
46. Bailey LJ, McCoy JG, Phillips GN, Fox BG (2008) Structural consequences of effector protein complex formation in a diiron hydroxylase. Proc Natl Acad Sci USA 105:19194-19198.
47. Fox BG, Lyle KS, Rogge CE (2004) Reactions of the diiron enzyme stearoyl-acyl carrier protein desaturase. Acc Chem Res 37:421-429.
48. Dixon M (1971) The acceptor specificity of flavins and flavoproteins. I. Techniques for anaerobic spectrophotometry. Biochim Biophys Acta 226:241-258.
49. ε-(4- aminobutyl)lysine). J Biol Chem 259:7217-7222.
50. George GN, Pickering IJ (2000) EXAFSPAK and EDGFIT. (Stanford Synchrotron Radiation Laboratory, Stanford Linear Accelerator Center, Stanford University, Stanford, CA).
51. Rehr JJ, Mustre de Leon J, Zabinsky SI, Albers RC (1991) Theoretical x-ray absorption fine structure standards. J Am Chem Soc 113:5135-5140.
52. Scarrow RC, et al. (1994) X-ray spectroscopy of the iron site in soybean lipoxygenase-1: Changes in coordination upon oxidation or addition of methanol. Biochemistry 33:15023-15035.
53. Ravel B, Newville M (2005) ATHENA, ARTEMIS, HEPHAESTUS: Data analysis for X-ray absorption spectroscopy using IFEFFIT. J Synchrotron Rad 12:537-541. (Pubitemid 41557599)