메뉴 건너뛰기




Volumn 1854, Issue 9, 2015, Pages 1118-1122

Is His54 a gating residue for the ferritin ferroxidase site?

Author keywords

Ferritin; Ferroxidase site; Mutagenesis; Reaction kinetics

Indexed keywords

APOFERRITIN; CERULOPLASMIN; FERRIC OXIDE; FERRITIN; FERRITIN FERROXIDASE; HIS54 FERRITIN; IRON; UNCLASSIFIED DRUG; HISTIDINE;

EID: 84937642423     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2015.02.011     Document Type: Article
Times cited : (16)

References (32)
  • 2
    • 77953812371 scopus 로고    scopus 로고
    • X-ray structures of ferritins and related proteins
    • R.R. Crichton, and J.P. Declercq X-ray structures of ferritins and related proteins Biochim. Biophys. Acta 1800 2010 706 718
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 706-718
    • Crichton, R.R.1    Declercq, J.P.2
  • 3
    • 84888589610 scopus 로고    scopus 로고
    • Solution and solid state NMR approaches to draw iron pathways in the ferritin nanocage
    • D. Lalli, and P. Turano Solution and solid state NMR approaches to draw iron pathways in the ferritin nanocage Acc. Chem. Res. 46 2013 2676 2685
    • (2013) Acc. Chem. Res. , vol.46 , pp. 2676-2685
    • Lalli, D.1    Turano, P.2
  • 4
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • F.M. Torti, and S.V. Torti Regulation of ferritin genes and protein Blood 99 2002 3505 3516
    • (2002) Blood , vol.99 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 5
    • 67349100157 scopus 로고    scopus 로고
    • Ferritins: a family of molecules for iron storage, antioxidation and more
    • P. Arosio, R. Ingrassia, and P. Cavadini Ferritins: a family of molecules for iron storage, antioxidation and more Biochim. Biophys. Acta 1790 2009 589 599
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 589-599
    • Arosio, P.1    Ingrassia, R.2    Cavadini, P.3
  • 6
    • 47749097596 scopus 로고    scopus 로고
    • Spectroscopic definition of the ferroxidase site in M ferritin: comparison of binuclear substrate vs cofactor active sites
    • J.K. Schwartz, X.S. Liu, T. Tosha, E.C. Theil, and E.I. Solomon Spectroscopic definition of the ferroxidase site in M ferritin: comparison of binuclear substrate vs cofactor active sites J. Am. Chem. Soc. 130 2008 9441 9450
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 9441-9450
    • Schwartz, J.K.1    Liu, X.S.2    Tosha, T.3    Theil, E.C.4    Solomon, E.I.5
  • 7
    • 0034614666 scopus 로고    scopus 로고
    • A short Fe-Fe distance in peroxodiferric ferritin: control of Fe substrate versus cofactor decay?
    • J. Hwang, C. Krebs, B.H. Huynh, D.E. Edmondson, E.C. Theil, and J.E. Penner-Hahn A short Fe-Fe distance in peroxodiferric ferritin: control of Fe substrate versus cofactor decay? Science 287 2000 122 125
    • (2000) Science , vol.287 , pp. 122-125
    • Hwang, J.1    Krebs, C.2    Huynh, B.H.3    Edmondson, D.E.4    Theil, E.C.5    Penner-Hahn, J.E.6
  • 9
    • 77958076541 scopus 로고    scopus 로고
    • Moving metal ions through ferritin-protein nanocages from three-fold pores to catalytic sites
    • T. Tosha, H.L. Ng, O. Bhattasali, T. Alber, and E.C. Theil Moving metal ions through ferritin-protein nanocages from three-fold pores to catalytic sites J. Am. Chem. Soc. 132 2010 14562 14569
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 14562-14569
    • Tosha, T.1    Ng, H.L.2    Bhattasali, O.3    Alber, T.4    Theil, E.C.5
  • 10
    • 33751517409 scopus 로고    scopus 로고
    • High-resolution structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites X-ray
    • L. Toussaint, L. Bertrand, L. Hue, R.R. Crichton, and J.P. Declercq High-resolution structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites X-ray J. Mol. Biol. 365 2007 440 452
    • (2007) J. Mol. Biol. , vol.365 , pp. 440-452
    • Toussaint, L.1    Bertrand, L.2    Hue, L.3    Crichton, R.R.4    Declercq, J.P.5
  • 11
    • 84901840195 scopus 로고    scopus 로고
    • Moving Fe2 + from ferritin ion channels to catalytic OH centers depends on conserved protein cage carboxylates
    • R.K. Behera, and E.C. Theil Moving Fe2 + from ferritin ion channels to catalytic OH centers depends on conserved protein cage carboxylates Proc. Natl. Acad. Sci. U. S. A. 111 2014 7925 7930
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 7925-7930
    • Behera, R.K.1    Theil, E.C.2
  • 12
    • 84927661468 scopus 로고    scopus 로고
    • Time lapse, anomalous X-ray diffraction shows how Fe2+ substrate ions move through ferritin protein nanocages to oxidoreductase sites
    • in press
    • C. Pozzi, F. Di Pisa, D. Lalli, C. Rosa, E.C. Theil, P. Turano, and S. Mangani Time lapse, anomalous X-ray diffraction shows how Fe2+ substrate ions move through ferritin protein nanocages to oxidoreductase sites Acta Crystallogr. D 2015 10.1107/S1399004715002333 (in press)
    • (2015) Acta Crystallogr. D
    • Pozzi, C.1    Di Pisa, F.2    Lalli, D.3    Rosa, C.4    Theil, E.C.5    Turano, P.6    Mangani, S.7
  • 13
    • 34748853168 scopus 로고    scopus 로고
    • 13C-13C NOESY spectra of a 480 kDa protein: solution NMR of ferritin
    • M. Matzapetakis, P. Turano, E.C. Theil, and I. Bertini 13C-13C NOESY spectra of a 480 kDa protein: solution NMR of ferritin J. Biomol. NMR 38 2007 237 242
    • (2007) J. Biomol. NMR , vol.38 , pp. 237-242
    • Matzapetakis, M.1    Turano, P.2    Theil, E.C.3    Bertini, I.4
  • 14
    • 84901912875 scopus 로고    scopus 로고
    • Coordinating subdomains of ferritin protein cages with catalysis and biomineralization viewed from the C4 cage axes
    • E.C. Theil, P. Turano, V. Ghini, M. Allegrozzi, and C. Bernacchioni Coordinating subdomains of ferritin protein cages with catalysis and biomineralization viewed from the C4 cage axes J. Biol. Inorg. Chem. 19 2014 615 622
    • (2014) J. Biol. Inorg. Chem. , vol.19 , pp. 615-622
    • Theil, E.C.1    Turano, P.2    Ghini, V.3    Allegrozzi, M.4    Bernacchioni, C.5
  • 15
    • 84868349861 scopus 로고    scopus 로고
    • Ferritin ion channel disorder inhibits Fe(II)/O2 reactivity at distant sites
    • T. Tosha, R.K. Behera, and E.C. Theil Ferritin ion channel disorder inhibits Fe(II)/O2 reactivity at distant sites Inorg. Chem. 51 2012 11406 11411
    • (2012) Inorg. Chem. , vol.51 , pp. 11406-11411
    • Tosha, T.1    Behera, R.K.2    Theil, E.C.3
  • 17
    • 2942558543 scopus 로고    scopus 로고
    • Ferritin reactions: direct identification of the site for the diferric peroxide reaction intermediate
    • X. Liu, and E.C. Theil Ferritin reactions: direct identification of the site for the diferric peroxide reaction intermediate Proc. Natl. Acad. Sci. U. S. A. 101 2004 8557 8562
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 8557-8562
    • Liu, X.1    Theil, E.C.2
  • 18
    • 84867672506 scopus 로고    scopus 로고
    • The catalytic center of ferritin regulates iron storage via Fe(II)-Fe(III) displacement
    • K.H. Ebrahimi, E. Bill, P.L. Hagedoorn, and W.R. Hagen The catalytic center of ferritin regulates iron storage via Fe(II)-Fe(III) displacement Nat. Chem. Biol. 8 2012 941 948
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 941-948
    • Ebrahimi, K.H.1    Bill, E.2    Hagedoorn, P.L.3    Hagen, W.R.4
  • 20
    • 0037386550 scopus 로고    scopus 로고
    • Opening protein pores with chaotropes enhances Fe reduction and chelation of Fe from the ferritin biomineral
    • X. Liu, W. Jin, and E.C. Theil Opening protein pores with chaotropes enhances Fe reduction and chelation of Fe from the ferritin biomineral Proc. Natl. Acad. Sci. U. S. A. 100 2003 3653 3658
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 3653-3658
    • Liu, X.1    Jin, W.2    Theil, E.C.3
  • 21
    • 0035954391 scopus 로고    scopus 로고
    • "Opening" the ferritin pore for iron release by mutation of conserved amino acids at interhelix and loop sites
    • W. Jin, H. Takagi, B. Pancorbo, and E.C. Theil "Opening" the ferritin pore for iron release by mutation of conserved amino acids at interhelix and loop sites Biochemistry 40 2001 7525 7532
    • (2001) Biochemistry , vol.40 , pp. 7525-7532
    • Jin, W.1    Takagi, H.2    Pancorbo, B.3    Theil, E.C.4
  • 22
    • 57649121590 scopus 로고    scopus 로고
    • Ferritin contains less iron (59Fe) in cells when the protein pores are unfolded by mutation
    • M.R. Hasan, T. Tosha, and E.C. Theil Ferritin contains less iron (59Fe) in cells when the protein pores are unfolded by mutation J. Biol. Chem. 283 2008 31394 31400
    • (2008) J. Biol. Chem. , vol.283 , pp. 31394-31400
    • Hasan, M.R.1    Tosha, T.2    Theil, E.C.3
  • 24
    • 0027732697 scopus 로고
    • Defining the roles of the threefold channels in iron uptake, iron oxidation and iron-core formation in ferritin: a study aided by site-directed mutagenesis
    • A. Treffry, E.R. Bauminger, D. Hechel, N.W. Hodson, I. Nowik, S.J. Yewdall, and P.M. Harrison Defining the roles of the threefold channels in iron uptake, iron oxidation and iron-core formation in ferritin: a study aided by site-directed mutagenesis Biochem. J. 296 1993 721 728
    • (1993) Biochem. J. , vol.296 , pp. 721-728
    • Treffry, A.1    Bauminger, E.R.2    Hechel, D.3    Hodson, N.W.4    Nowik, I.5    Yewdall, S.J.6    Harrison, P.M.7
  • 25
    • 0037380857 scopus 로고    scopus 로고
    • Functional properties of threefold and fourfold channels in ferritin deduced from electrostatic calculations
    • T. Takahashi, and S. Kuyucaky Functional properties of threefold and fourfold channels in ferritin deduced from electrostatic calculations Biophys. J. 84 2003 2256 2263
    • (2003) Biophys. J. , vol.84 , pp. 2256-2263
    • Takahashi, T.1    Kuyucaky, S.2
  • 27
    • 84867672506 scopus 로고    scopus 로고
    • The catalytic center of ferritin regulates iron storage via Fe(II)-Fe(III) displacement
    • K.H. Ebrahimi, E. Bill, P.L. Hagedoorn, and W.R. Hagen The catalytic center of ferritin regulates iron storage via Fe(II)-Fe(III) displacement Nat. Chem. Biol. 8 2012 941 948
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 941-948
    • Ebrahimi, K.H.1    Bill, E.2    Hagedoorn, P.L.3    Hagen, W.R.4
  • 29
    • 34249874901 scopus 로고    scopus 로고
    • Crystal structure of the ferritin from the hyperthermophilic archaeal anaerobe Pyrococcus furiosus
    • J. Tatur, W.R. Hagen, and P.M. Matias Crystal structure of the ferritin from the hyperthermophilic archaeal anaerobe Pyrococcus furiosus J. Biol. Inorg. Chem. 12 2007 615 630
    • (2007) J. Biol. Inorg. Chem. , vol.12 , pp. 615-630
    • Tatur, J.1    Hagen, W.R.2    Matias, P.M.3
  • 30
    • 76749113944 scopus 로고    scopus 로고
    • Structural studies of bacterioferritin B from Pseudomonas aeruginosa suggest a gating mechanism for iron uptake via the ferroxidase center
    • S.K. Weeratunga, S. Lovell, H. Yao, K.P. Battaile, C.J. Fischer, C.E. Gee, and M. Rivera Structural studies of bacterioferritin B from Pseudomonas aeruginosa suggest a gating mechanism for iron uptake via the ferroxidase center Biochemistry 49 2010 1160 1175
    • (2010) Biochemistry , vol.49 , pp. 1160-1175
    • Weeratunga, S.K.1    Lovell, S.2    Yao, H.3    Battaile, K.P.4    Fischer, C.J.5    Gee, C.E.6    Rivera, M.7
  • 31
    • 0035852651 scopus 로고    scopus 로고
    • Hypoxia-induced gene expression profiling in the euryoxic fish Gillichthys mirabilis
    • A.Y. Gracey, J.V. Troll, and G.N. Somero Hypoxia-induced gene expression profiling in the euryoxic fish Gillichthys mirabilis Proc. Natl. Acad. Sci. U. S. A. 98 2001 1993 1998
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 1993-1998
    • Gracey, A.Y.1    Troll, J.V.2    Somero, G.N.3
  • 32
    • 84905827092 scopus 로고    scopus 로고
    • Mechanisms of iron mineralization in ferritins: one size does not fit all
    • J.M. Bradley, G.R. Moore, and N.E. Le Brun Mechanisms of iron mineralization in ferritins: one size does not fit all J. Biol. Inorg. Chem. 19 2014 775 785
    • (2014) J. Biol. Inorg. Chem. , vol.19 , pp. 775-785
    • Bradley, J.M.1    Moore, G.R.2    Le Brun, N.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.