메뉴 건너뛰기




Volumn 86, Issue 6, 2004, Pages 3882-3892

Unusual heme iron-lipid acyl chain coordination in Escherichia coli flavohemoglobin

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; COORDINATION COMPOUND; FATTY ACID; FATTY ACID BINDING PROTEIN; FLAVOHEMOGLOBIN; FLAVOPROTEIN; HEME; HEMOGLOBIN; IRON; LEUCINE; LINOLEIC ACID; LIPID; LIPID ACYL CHAIN; LIPID FREE PROTEIN; PHOSPHOLIPID; PROTEIN; UNCLASSIFIED DRUG;

EID: 2942696586     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.103.034876     Document Type: Article
Times cited : (42)

References (42)
  • 1
    • 0035406449 scopus 로고    scopus 로고
    • Geometrical fitting of experimental XANES spectra by a full multiple scattering procedure
    • Benfatto, M., and S. Della Longa. 2001. Geometrical fitting of experimental XANES spectra by a full multiple scattering procedure. J. Synchr. Rad. 8:1087-1094.
    • (2001) J. Synchr. Rad. , vol.8 , pp. 1087-1094
    • Benfatto, M.1    Della Longa, S.2
  • 2
    • 0032815529 scopus 로고    scopus 로고
    • Pentacoordinate hemin derivatives in sodium dodecyl sulfate micelles: Model systems for the assignment of the fifth ligand in ferric heme proteins
    • Boffi, A., T. K. Das, S. Della Longa, C. Spagnuolo, and D. L. Rousseau. 1999. Pentacoordinate hemin derivatives in sodium dodecyl sulfate micelles: model systems for the assignment of the fifth ligand in ferric heme proteins. Biophys. J. 77:1143-1149.
    • (1999) Biophys. J. , vol.77 , pp. 1143-1149
    • Boffi, A.1    Das, T.K.2    Della Longa, S.3    Spagnuolo, C.4    Rousseau, D.L.5
  • 3
    • 0038629108 scopus 로고    scopus 로고
    • Interaction with membrane lipids and heme ligand binding properties of Escherichia coli flavohemoglobin
    • Bonamore, A., A. Farina, M. Gattoni, M. E. Schininà, A. Bellelli, and A. Boffi. 2003a. Interaction with membrane lipids and heme ligand binding properties of Escherichia coli flavohemoglobin. Biochemistry. 42:5792-5801.
    • (2003) Biochemistry , vol.42 , pp. 5792-5801
    • Bonamore, A.1    Farina, A.2    Gattoni, M.3    Schininà, M.E.4    Bellelli, A.5    Boffi, A.6
  • 4
    • 0037929111 scopus 로고    scopus 로고
    • The flavohemoglobin from Escherichia coli is an efficient alkylhydroperoxide reductase
    • Bonamore, A., P. Gentili, M. E. Schininà, A. Ilari, and A. Boffi. 2003b. The flavohemoglobin from Escherichia coli is an efficient alkylhydroperoxide reductase. J. Biol. Chem. 278:22272-22277.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22272-22277
    • Bonamore, A.1    Gentili, P.2    Schininà, M.E.3    Ilari, A.4    Boffi, A.5
  • 5
    • 2842546487 scopus 로고
    • Structural correlations and vinyl influences in resonance Raman spectra of protoheme complexes in proteins
    • Choi, S., T. G. Spiro, K. C. Langry, K. M. Smith, D. L. Budd, and G. N. La Mar. 1982. Structural correlations and vinyl influences in resonance Raman spectra of protoheme complexes in proteins. J. Am. Chem. Soc. 104:4345-4351.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4345-4351
    • Choi, S.1    Spiro, T.G.2    Langry, K.C.3    Smith, K.M.4    Budd, D.L.5    La Mar, G.N.6
  • 7
    • 42749100563 scopus 로고    scopus 로고
    • Quantitative analysis of x-ray absorption near edge structure data by a full multiple scattering procedure: The Fe-CO geometry in photolyzed carbonmonoxy-myoglobin single crystal
    • Della Longa, S., A. Arcovito, M. Girasole, J. L. Hazemann, and M. Benfatto. 2001. Quantitative analysis of x-ray absorption near edge structure data by a full multiple scattering procedure: the Fe-CO geometry in photolyzed carbonmonoxy-myoglobin single crystal. Phys. Rev. Lett. 87:155501/1-4.
    • (2001) Phys. Rev. Lett. , vol.87
    • Della Longa, S.1    Arcovito, A.2    Girasole, M.3    Hazemann, J.L.4    Benfatto, M.5
  • 10
    • 0029610660 scopus 로고
    • Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 Å resolution
    • Ermler, U., R. A. Siddiqui, R. Cramm, and B. Friedrich. 1995. Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 Å resolution. EMBO J. 14:6067-6077.
    • (1995) EMBO J. , vol.14 , pp. 6067-6077
    • Ermler, U.1    Siddiqui, R.A.2    Cramm, R.3    Friedrich, B.4
  • 11
    • 0001202764 scopus 로고
    • X-ray-absorption spectroscopy and n-body distribution functions in condensed matter. II. Data and applications
    • Filipponi, A., and A. Di Cicco. 1995. X-ray-absorption spectroscopy and n-body distribution functions in condensed matter. II. Data and applications. Phys. Rev. B. 52:15135-15141.
    • (1995) Phys. Rev. B , vol.52 , pp. 15135-15141
    • Filipponi, A.1    Di Cicco, A.2
  • 12
    • 0001202765 scopus 로고
    • X-ray-absorption spectroscopy and n-body distribution functions in condensed matter. I. Theory
    • Filipponi, A., A. Di Cicco, and C. R. Natoli. 1995. X-ray-absorption spectroscopy and n-body distribution functions in condensed matter. I. Theory. Phys. Rev. B. 52:15122-15130.
    • (1995) Phys. Rev. B , vol.52 , pp. 15122-15130
    • Filipponi, A.1    Di Cicco, A.2    Natoli, C.R.3
  • 14
    • 0032564409 scopus 로고    scopus 로고
    • Nitrosative stress: Metabolic pathway involving the flavohemoglobin
    • Hausladen, A., A. J. Gow, and J. S. Stamler. 1998. Nitrosative stress: metabolic pathway involving the flavohemoglobin. Proc. Natl. Acad. Sci. USA. 95:14100-14105.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14100-14105
    • Hausladen, A.1    Gow, A.J.2    Stamler, J.S.3
  • 15
    • 0035964364 scopus 로고    scopus 로고
    • Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl equivalent with molecular oxygen
    • Hausladen, A., A. J. Gow, and J. S. Stamler. 2001. Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl equivalent with molecular oxygen. Proc. Natl. Acad. Sci. USA. 98:10108-10112.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10108-10112
    • Hausladen, A.1    Gow, A.J.2    Stamler, J.S.3
  • 16
    • 0030467166 scopus 로고    scopus 로고
    • Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin
    • Hu, S., K. M. Smith, and T. G. Spiro. 1996. Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin. J. Am. Chem. Soc. 118:12638-12646.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12638-12646
    • Hu, S.1    Smith, K.M.2    Spiro, T.G.3
  • 17
    • 0039667195 scopus 로고
    • Use of one electron theory for the interpretation of near edge structure in K-shell x-ray absorption spectra of transition metal complexes
    • Kutzler, F. W., C. R. Natoli, D. K. Misemer, S. Doniach, and K. O. Hogdson. 1980. Use of one electron theory for the interpretation of near edge structure in K-shell x-ray absorption spectra of transition metal complexes. J. Chem. Phys. 73:3274-3288.
    • (1980) J. Chem. Phys. , vol.73 , pp. 3274-3288
    • Kutzler, F.W.1    Natoli, C.R.2    Misemer, D.K.3    Doniach, S.4    Hogdson, K.O.5
  • 19
    • 0037189541 scopus 로고    scopus 로고
    • The x-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket
    • Ilari, A., A. Bonamore, A. Farina, K. A. Johnson, and A. Boffi. 2002. The x-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket. J. Biol. Chem. 277:23725-23732.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23725-23732
    • Ilari, A.1    Bonamore, A.2    Farina, A.3    Johnson, K.A.4    Boffi, A.5
  • 20
    • 0018345506 scopus 로고
    • X-ray absorption edge fine structure spectroscopy of the active site heme of cytochrome c
    • Labhardt, A., and C. Yven. 1979. X-ray absorption edge fine structure spectroscopy of the active site heme of cytochrome c. Nature. 277:150-151.
    • (1979) Nature , vol.277 , pp. 150-151
    • Labhardt, A.1    Yven, C.2
  • 21
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., M. W. McArthur, D. S. Moss, and J. Thomton. 1993. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thomton, J.4
  • 23
    • 0028906186 scopus 로고
    • X-ray absorption near edge studies of cytochrome P-450-CAM, chloroperoxidase, and myoglobin
    • Liu, H. I., M. Sono, S. Kadkhodayan, L. P. Hager, B. Hedman, K. O. Hodgson, and J. H. Dawson. 1995. X-ray absorption near edge studies of cytochrome P-450-CAM, chloroperoxidase, and myoglobin. J. Biol. Chem. 270:10544-10550.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10544-10550
    • Liu, H.I.1    Sono, M.2    Kadkhodayan, S.3    Hager, L.P.4    Hedman, B.5    Hodgson, K.O.6    Dawson, J.H.7
  • 25
    • 0035831479 scopus 로고    scopus 로고
    • Flavohemoglobin, a globin with a peroxidase-like catalytic site
    • Mukai, M., C. E. Mills, R. K. Poole, and S. R. Yeh. 2001. Flavohemoglobin, a globin with a peroxidase-like catalytic site. J. Biol. Chem. 276:7272-7277.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7272-7277
    • Mukai, M.1    Mills, C.E.2    Poole, R.K.3    Yeh, S.R.4
  • 27
    • 35949024002 scopus 로고
    • Use of general potentials in multiple scattering theory
    • Natoli, C. R., M. Benfatto, and S. Doniach. 1986. Use of general potentials in multiple scattering theory. Phys. Rev. A. 34:4682-4694.
    • (1986) Phys. Rev. A , vol.34 , pp. 4682-4694
    • Natoli, C.R.1    Benfatto, M.2    Doniach, S.3
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Ottwinowski, Z., and W. Minor. 1997. Processing of x-ray diffraction data collected in oscillation mode. Meth. Enzymol. 276:307-326
    • (1997) Meth. Enzymol. , vol.276 , pp. 307-326
    • Ottwinowski, Z.1    Minor, W.2
  • 32
    • 0029831326 scopus 로고    scopus 로고
    • Nitric oxide, nitrite and FNR regulation of HMP (flavohemoglobin) gene expression in Escherichia coli
    • Poole, R. K., M. F. Anjum, J. Membrillo-Hemandez, S. O. Kim, M. N. Hughes, and V. Stuart. 1996. Nitric oxide, nitrite and FNR regulation of HMP (flavohemoglobin) gene expression in Escherichia coli. J. Bacteriol. 178:5487-5492.
    • (1996) J. Bacteriol. , vol.178 , pp. 5487-5492
    • Poole, R.K.1    Anjum, M.F.2    Membrillo-Hemandez, J.3    Kim, S.O.4    Hughes, M.N.5    Stuart, V.6
  • 33
    • 33751390964 scopus 로고
    • XANES spectra of copper II complexes: Correlation of the intensity of the 1s-3d transition
    • Sano, M., S. Komorita, and H. Yamatera. 1992. XANES spectra of copper II complexes: correlation of the intensity of the 1s-3d transition. Inorg. Chem. 31:459-463.
    • (1992) Inorg. Chem. , vol.31 , pp. 459-463
    • Sano, M.1    Komorita, S.2    Yamatera, H.3
  • 34
    • 0025090930 scopus 로고
    • X-ray absorption spectral study of ferric high spin hemeproteins: XANES evidence for coordination structure of the heme iron
    • Shiro, Y., F. Sato, T. Suzuki, T. Izuka, T. Matsushita, and H. Oyanagi. 1990. X-ray absorption spectral study of ferric high spin hemeproteins: XANES evidence for coordination structure of the heme iron. J. Am. Chem. Soc. 112:2921-2924.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 2921-2924
    • Shiro, Y.1    Sato, F.2    Suzuki, T.3    Izuka, T.4    Matsushita, T.5    Oyanagi, H.6
  • 35
    • 0032949323 scopus 로고    scopus 로고
    • Peroxidase-benzhydroxamic acid complexes: Spectroscopic evidence that a Fe-H2O distance of 2.6 Å can correspond to hexa-coordinated high-spin heme
    • Smulevich, G., A. Feis, C. Indiani, M. Becucci, and M. P. Marzocchi. 1999. Peroxidase-benzhydroxamic acid complexes: spectroscopic evidence that a Fe-H2O distance of 2.6 Å can correspond to hexa-coordinated high-spin heme. J. Biol. Inorg. Chem. 4:39-47.
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 39-47
    • Smulevich, G.1    Feis, A.2    Indiani, C.3    Becucci, M.4    Marzocchi, M.P.5
  • 36
    • 0001314340 scopus 로고    scopus 로고
    • Heme-protein interactions in cytochrome c peroxidase revealed by site directed mutagenesis and resonance Raman spectra of isotopically labelled hemes
    • Smulevich, G., S. Hu, K. R. Rodgers, D. B. Goodin, K. M. Smith, and T. G. Spiro. 1996. Heme-protein interactions in cytochrome c peroxidase revealed by site directed mutagenesis and resonance Raman spectra of isotopically labelled hemes. Biospectroscopy. 2:365-376.
    • (1996) Biospectroscopy , vol.2 , pp. 365-376
    • Smulevich, G.1    Hu, S.2    Rodgers, K.R.3    Goodin, D.B.4    Smith, K.M.5    Spiro, T.G.6
  • 37
    • 0031569849 scopus 로고    scopus 로고
    • Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp
    • Tarricone, C., A. Galizzi, A. Coda, P. Ascenzi, and M. Bolognesi. 1997. Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp. Structure. 14:497-507.
    • (1997) Structure , vol.14 , pp. 497-507
    • Tarricone, C.1    Galizzi, A.2    Coda, A.3    Ascenzi, P.4    Bolognesi, M.5
  • 38
    • 0028899076 scopus 로고
    • X-ray absorption spectroscopy and applications in structural biology
    • Yachandra, V. K. 1995. X-ray absorption spectroscopy and applications in structural biology. Methods Enzymol. 246:638-675.
    • (1995) Methods Enzymol. , vol.246 , pp. 638-675
    • Yachandra, V.K.1
  • 39
    • 0029986887 scopus 로고    scopus 로고
    • Crystal structure of CO-, deoxy, and met-myoglobin at various H values
    • Yang, F., and G. N. Phillips, Jr. 1996. Crystal structure of CO-, deoxy, and met-myoglobin at various H values. J. Mol. Biol. 256:762-770.
    • (1996) J. Mol. Biol. , vol.256 , pp. 762-770
    • Yang, F.1    Phillips Jr., G.N.2
  • 40
    • 0036282685 scopus 로고    scopus 로고
    • Defining redox state of x-ray crystal structures by single-crystal ultraviolet-visible microspectrophotometry
    • Wilmot, C. M., T. Sjogren, G. H. Carlsson, G. I. Berglund, and J. Hajdu. 2002. Defining redox state of x-ray crystal structures by single-crystal ultraviolet-visible microspectrophotometry. Methods Enzymol. 353:301-318.
    • (2002) Methods Enzymol. , vol.353 , pp. 301-318
    • Wilmot, C.M.1    Sjogren, T.2    Carlsson, G.H.3    Berglund, G.I.4    Hajdu, J.5
  • 41
    • 0037059826 scopus 로고    scopus 로고
    • Truncated hemoglobins: A new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes and plants
    • Wittenberg, J. B., M. Bolognesi, B. A. Wittenberg, and M. Guertin. 2002. Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes and plants. J. Biol. Chem. 277:871-874.
    • (2002) J. Biol. Chem. , vol.277 , pp. 871-874
    • Wittenberg, J.B.1    Bolognesi, M.2    Wittenberg, B.A.3    Guertin, M.4
  • 42
    • 0031003561 scopus 로고    scopus 로고
    • Multiple-edge XAS studies of cyanide-bridged iron-copper molecular assemblies relevant to cyanide-inhibited heme-copper oxidases using four-body multiple-scattering analysis
    • Zhang, H. H., A. Filipponi, A. Di Cicco, M. J. Scott, R. H. Holm, B. Hedman, and K. O. Hodgson. 1997. Multiple-edge XAS studies of cyanide-bridged iron-copper molecular assemblies relevant to cyanide-inhibited heme-copper oxidases using four-body multiple-scattering analysis. J. Am. Chem. Soc. 119:2470-2476.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2470-2476
    • Zhang, H.H.1    Filipponi, A.2    Di Cicco, A.3    Scott, M.J.4    Holm, R.H.5    Hedman, B.6    Hodgson, K.O.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.