메뉴 건너뛰기




Volumn 1747, Issue 2, 2005, Pages 195-203

Tyrosine B10 and heme-ligand interactions of Lucina pectinata hemoglobin II: Control of heme reactivity

Author keywords

Closed conformation; HbI PheB10Tyr mutant; Hemoglobin II; Lucina pectinata; Open conformation

Indexed keywords

HEMOGLOBIN;

EID: 13544277171     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2004.11.005     Document Type: Article
Times cited : (23)

References (37)
  • 1
    • 0035066385 scopus 로고    scopus 로고
    • Nonvertebrate hemoglobins: Functions and molecular adaptations
    • R.E. Weber, and S.N. Vinogradov Nonvertebrate hemoglobins: functions and molecular adaptations Physiol. Rev. 81 2001 569 628
    • (2001) Physiol. Rev. , vol.81 , pp. 569-628
    • Weber, R.E.1    Vinogradov, S.N.2
  • 2
    • 0025026382 scopus 로고
    • Hemoglobins of the Lucina pectinata/bacteria symbiosis
    • D.W. Kraus, and J.B. Wittenberg Hemoglobins of the Lucina pectinata/bacteria symbiosis J. Biol. Chem. 265 1990 16043 16053
    • (1990) J. Biol. Chem. , vol.265 , pp. 16043-16053
    • Kraus, D.W.1    Wittenberg, J.B.2
  • 5
    • 0001723772 scopus 로고    scopus 로고
    • Resonance Raman studies of the heme-ligand active site of hemoglobin I from Lucina pectinata
    • J. Cerda, Y. Echevarría, E. Morales, and J. López-Garriga Resonance Raman studies of the heme-ligand active site of hemoglobin I from Lucina pectinata Biospectroscopy 5 1999 289 301
    • (1999) Biospectroscopy , vol.5 , pp. 289-301
    • Cerda, J.1    Echevarría, Y.2    Morales, E.3    López-Garriga, J.4
  • 6
    • 0032540246 scopus 로고    scopus 로고
    • Solution and crystal structures of a sperm whale myoglobin triple mutant that mimics the sulfide-binding hemoglobin from Lucina pectinata
    • G.N. La Mar, B.D. Nguyen, Z. Xuefeng, and V. Krishnamurthi Solution and crystal structures of a sperm whale myoglobin triple mutant that mimics the sulfide-binding hemoglobin from Lucina pectinata J. Biol. Chem. 273 1998 9517 9526
    • (1998) J. Biol. Chem. , vol.273 , pp. 9517-9526
    • La Mar, G.N.1    Nguyen, B.D.2    Xuefeng, Z.3    Krishnamurthi, V.4
  • 7
    • 0031615694 scopus 로고    scopus 로고
    • Orientation of the heme vinyl groups in the hydrogen sulfide-binding hemoglobin I from Lucina pectinata
    • E. Silfa, M. Almeida, J. Cerda, S. Wu, and J. López-Garriga Orientation of the heme vinyl groups in the hydrogen sulfide-binding hemoglobin I from Lucina pectinata Biospectroscopy 4 1998 311 326
    • (1998) Biospectroscopy , vol.4 , pp. 311-326
    • Silfa, E.1    Almeida, M.2    Cerda, J.3    Wu, S.4    López-Garriga, J.5
  • 8
    • 0032538024 scopus 로고    scopus 로고
    • Unusual rocking freedom of the heme in the hydrogen sulfide-binding hemoglobin from Lucina pectinata
    • J.F. Cerda-Colón, E. Silfa, and J. López-Garriga Unusual rocking freedom of the heme in the hydrogen sulfide-binding hemoglobin from Lucina pectinata J. Am. Chem. Soc. 120 1998 9312 9317
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9312-9317
    • Cerda-Colón, J.F.1    Silfa, E.2    López-Garriga, J.3
  • 13
    • 0030681291 scopus 로고    scopus 로고
    • A comparison of functional and structural consequences of the tyrosine B10 and glutamine E7 motifs in two invertebrate hemoglobins (Ascaris suum and Lucina pectinata)
    • E.S. Peterson, S. Huang, J. Wang, L.M. Miller, G. Vidugiris, A.P. Kloek, D.E. Goldberg, M.R. Chance, J.B. Wittenberg, and J.M. Friedman A comparison of functional and structural consequences of the tyrosine B10 and glutamine E7 motifs in two invertebrate hemoglobins (Ascaris suum and Lucina pectinata) Biochemistry 36 1997 13110 13121
    • (1997) Biochemistry , vol.36 , pp. 13110-13121
    • Peterson, E.S.1    Huang, S.2    Wang, J.3    Miller, L.M.4    Vidugiris, G.5    Kloek, A.P.6    Goldberg, D.E.7    Chance, M.R.8    Wittenberg, J.B.9    Friedman, J.M.10
  • 14
    • 0001978749 scopus 로고
    • Functions of cytoplasmic hemoglobins and myohemerythrin
    • J.B. Wittenberg Functions of cytoplasmic hemoglobins and myohemerythrin Adv. Comp. Environ. Physiol. 13 1992 59 85
    • (1992) Adv. Comp. Environ. Physiol. , vol.13 , pp. 59-85
    • Wittenberg, J.B.1
  • 15
    • 8844237890 scopus 로고    scopus 로고
    • Functional characterization of the purified holo form of hemoglobin I from Lucina pectinata over-expressed in Escherichia coli
    • E. Collazo, R. Pietri, W. De Jesus, C. Ramos, A. Del Toro, R.G. León, J. López-Garriga, and C.L. Cadilla Functional characterization of the purified holo form of hemoglobin I from Lucina pectinata over-expressed in Escherichia coli Protein J. 23 2004 239 245
    • (2004) Protein J. , vol.23 , pp. 239-245
    • Collazo, E.1    Pietri, R.2    De Jesus, W.3    Ramos, C.4    Del Toro, A.5    León, R.G.6    López-Garriga, J.7    Cadilla, C.L.8
  • 16
    • 0031037679 scopus 로고    scopus 로고
    • Mutation of distal residues of horseradish peroxidase: Influence on substrate binding and cavity properties
    • D.B. Howes, N.J. Rodriguez-López, and T.A. Smith Mutation of distal residues of horseradish peroxidase: influence on substrate binding and cavity properties Biochemistry 36 1997 1532 1543
    • (1997) Biochemistry , vol.36 , pp. 1532-1543
    • Howes, D.B.1    Rodriguez-López, N.J.2    Smith, T.A.3
  • 17
    • 0033667559 scopus 로고    scopus 로고
    • Insight into protein structure and protein-ligand recognition by Fourier transform infrared spectroscopy
    • C. Jung Insight into protein structure and protein-ligand recognition by Fourier transform infrared spectroscopy J. Mol. Recognit. 13 2000 325 351
    • (2000) J. Mol. Recognit. , vol.13 , pp. 325-351
    • Jung, C.1
  • 19
    • 0028241788 scopus 로고
    • Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation
    • M.A. Gilles-González, G. González, M.F. Perutz Ý, L. Kiger, M.C. Marden, and C. Poyart Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation Biochemistry 33 1994 8067 8073
    • (1994) Biochemistry , vol.33 , pp. 8067-8073
    • Gilles-González, M.A.1    González, G.2    Perutz, Ý.M.F.3    Kiger, L.4    Marden, M.C.5    Poyart, C.6
  • 20
    • 0032815529 scopus 로고    scopus 로고
    • Pentacoordinate hemin derivates in sodium dodecyl sulfate micelles: Model system for the assignment of the fifth ligand in ferric heme proteins
    • A. Boffi, T. Kanti Das, S. della Longa, C. Spangnuolo, and D.L. Rousseau Pentacoordinate hemin derivates in sodium dodecyl sulfate micelles: model system for the assignment of the fifth ligand in ferric heme proteins J. Biophys. 77 1999 1143 1149
    • (1999) J. Biophys. , vol.77 , pp. 1143-1149
    • Boffi, A.1    Kanti Das, T.2    Della Longa, S.3    Spangnuolo, C.4    Rousseau, D.L.5
  • 22
    • 0037039353 scopus 로고    scopus 로고
    • Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin
    • B.J. Reeder, D.A. Svistunenko, M.A. Sharpe, and M.T. Wilson Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin Biochemistry 41 2002 367 375
    • (2002) Biochemistry , vol.41 , pp. 367-375
    • Reeder, B.J.1    Svistunenko, D.A.2    Sharpe, M.A.3    Wilson, M.T.4
  • 25
    • 0024962323 scopus 로고
    • Comparative spectral analysis of mammalian, fungal, and bacterial catalases
    • K.D. Sharma, L.A. Anderson, T.M. Loehr, J. Terner, and H.M. Goff Comparative spectral analysis of mammalian, fungal, and bacterial catalases J. Biol. Chem. 264 1989 12772 12779
    • (1989) J. Biol. Chem. , vol.264 , pp. 12772-12779
    • Sharma, K.D.1    Anderson, L.A.2    Loehr, T.M.3    Terner, J.4    Goff, H.M.5
  • 27
    • 0028328331 scopus 로고
    • Structural determinants of the stretching frequency of CO bound to myoglobin
    • T. Li, M.L. Quillin, G.N. Phillips, and J.S. Olson Structural determinants of the stretching frequency of CO bound to myoglobin Biochemistry 33 1994 1433 1446
    • (1994) Biochemistry , vol.33 , pp. 1433-1446
    • Li, T.1    Quillin, M.L.2    Phillips, G.N.3    Olson, J.S.4
  • 29
    • 0034141829 scopus 로고    scopus 로고
    • Origin of the anomalous Fe-CO stretching mode in the CO complex of Ascaris hemoglobin
    • T.K. Das, J.M. Friedman, A.P. Kloek, D.E. Goldberg, and D.L. Rousseau Origin of the anomalous Fe-CO stretching mode in the CO complex of Ascaris hemoglobin Biochemistry 39 2000 837 842
    • (2000) Biochemistry , vol.39 , pp. 837-842
    • Das, T.K.1    Friedman, J.M.2    Kloek, A.P.3    Goldberg, D.E.4    Rousseau, D.L.5
  • 30
    • 0035831479 scopus 로고    scopus 로고
    • Flavohemoglobin, a globin with a peroxidase-like catalytic site
    • M. Mukai, C.E. Mills, R. Poole, and S.-R. Yeh Flavohemoglobin, a globin with a peroxidase-like catalytic site J. Biol. Chem. 276 2001 7272 7277
    • (2001) J. Biol. Chem. , vol.276 , pp. 7272-7277
    • Mukai, M.1    Mills, C.E.2    Poole, R.3    Yeh, S.-R.4
  • 31
    • 0037059826 scopus 로고    scopus 로고
    • Truncated hemoglobins: A new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants
    • J.B. Wittenberg, M. Bolognesi, B.A. Wittenberg, and M. Guertin Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants J. Biol. Chem. 277 2002 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
  • 32
    • 2542445605 scopus 로고    scopus 로고
    • Tyrosine B10 inhibits stabilization of bound carbon monoxide and oxygen in soybean leghemoglobin
    • S. Kundu, G.C. Blouin, S.A. Premer, G. Sarah, J.S. Olson, and M.S. Hargrove Tyrosine B10 inhibits stabilization of bound carbon monoxide and oxygen in soybean leghemoglobin Biochemistry 43 2004 6241 6252
    • (2004) Biochemistry , vol.43 , pp. 6241-6252
    • Kundu, S.1    Blouin, G.C.2    Premer, S.A.3    Sarah, G.4    Olson, J.S.5    Hargrove, M.S.6
  • 33
    • 0030046276 scopus 로고    scopus 로고
    • Hydrogen bonding of tyrosine B10 to heme-bound oxygen in Ascaris hemoglobin. Direct evidence from UV resonance Raman spectroscopy
    • S. Huang, J. Huang, A.P. Kloek, D.E. Goldberg, and J.M. Friedman Hydrogen bonding of tyrosine B10 to heme-bound oxygen in Ascaris hemoglobin. Direct evidence from UV resonance Raman spectroscopy J. Biol. Chem. 271 1996 958 962
    • (1996) J. Biol. Chem. , vol.271 , pp. 958-962
    • Huang, S.1    Huang, J.2    Kloek, A.P.3    Goldberg, D.E.4    Friedman, J.M.5
  • 34
    • 0033576249 scopus 로고    scopus 로고
    • Identification of the ligands to the ferric heme of Chlamydomonas chloroplast hemoglobin: Evidence for ligation of tyrosine-63 (B10) to the heme
    • T.K. Das, M. Couture, H.C. Lee, J. Peisach, D.L. Rousseau, B.A. Wittenberg, J.B. Wittenberg, and M. Guertin Identification of the ligands to the ferric heme of Chlamydomonas chloroplast hemoglobin: evidence for ligation of tyrosine-63 (B10) to the heme Biochemistry 38 1999 5360 5368
    • (1999) Biochemistry , vol.38 , pp. 5360-5368
    • Das, T.K.1    Couture, M.2    Lee, H.C.3    Peisach, J.4    Rousseau, D.L.5    Wittenberg, B.A.6    Wittenberg, J.B.7    Guertin, M.8
  • 36
    • 0033866598 scopus 로고    scopus 로고
    • Guertin, structural investigations of the hemoglobin of the cyanobacterium Synechocystis PCC6803 reveal a unique distal heme pocket
    • M. Couture, T.K. Das, P.Y. Savard, Y. Ouellet, J.B. Wittenberg, B.A. Wittenberg, and D.L. Rousseau Guertin, structural investigations of the hemoglobin of the cyanobacterium Synechocystis PCC6803 reveal a unique distal heme pocket Eur. J. Biochem. 267 2000 4770 4780
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4770-4780
    • Couture, M.1    Das, T.K.2    Savard, P.Y.3    Ouellet, Y.4    Wittenberg, J.B.5    Wittenberg, B.A.6    Rousseau, D.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.