메뉴 건너뛰기




Volumn 1764, Issue 4, 2006, Pages 758-765

Hemoglobin I from Lucina pectinata: A model for distal heme-ligand control

Author keywords

Carbon monoxide; Cyanide; Fourier transform infrared resonance; Hemoglobin I; Hydrogen sulfide; Recombinant HbI

Indexed keywords

ASPARAGINE; GLUTAMINE; HEMOGLOBIN; HISTIDINE; LEUCINE; LIGAND; OXYGEN; PHENYLALANINE; RECOMBINANT HEMOGLOBIN; TYROSINE; VALINE; CARBON MONOXIDE; CYANIDE; FERRIC ION; FERROUS ION; HEME;

EID: 33745125408     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.11.006     Document Type: Article
Times cited : (21)

References (24)
  • 1
    • 0025026382 scopus 로고
    • Hemoglobins of the Lucina pectinata/bacteria symbiosis
    • Kraus D.W., and Wittenberg J.B. 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
  • 2
    • 0035066385 scopus 로고    scopus 로고
    • Nonvertebrate hemoglobins: functions and molecular adaptations
    • Weber R.E., and Vinogradov S.N. 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
  • 6
    • 0001723772 scopus 로고    scopus 로고
    • Resonance Raman studies of the heme-ligand active site of hemoglobin I from Lucina pectinata
    • Cerda J., Echevarría Y., Morales E., and López-Garriga J. 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
  • 9
    • 0033667559 scopus 로고    scopus 로고
    • Insight into protein structure and protein-ligand recognition by Fourier transform infrared spectroscopy
    • Jung C. 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
  • 10
    • 0028328331 scopus 로고
    • Structural determinants of the stretching frequency of CO bound to myoglobin
    • Li T., Quillin M.L., Phillips G.N., and Olson J.S. 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
  • 11
    • 0021989717 scopus 로고
    • Investigation of cyanide as an infrared probe of hemeprotein ligand binding sites
    • Yoshikawa S., O'Keeffe D.H., and Caughey W.S. Investigation of cyanide as an infrared probe of hemeprotein ligand binding sites. J. Biol. Chem. 260 (1985) 3518-3528
    • (1985) J. Biol. Chem. , vol.260 , pp. 3518-3528
    • Yoshikawa, S.1    O'Keeffe, D.H.2    Caughey, W.S.3
  • 12
    • 0032538024 scopus 로고    scopus 로고
    • Unusual rocking freedom of the heme in the hydrogen sulfide-binding hemoglobin from Lucina pectinata
    • Cerda-Colón J.F., Silfa E., and Lopéz-Garriga J. 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    Lopéz-Garriga, J.3
  • 13
    • 0029945653 scopus 로고    scopus 로고
    • Structural bases for sulfide recognition in Lucina pectinata hemoglobin I
    • Rizzi M., Wittenberg J.B., Coda A., Ascenzi P., and Bolognesi M. Structural bases for sulfide recognition in Lucina pectinata hemoglobin I. J. Mol. Biol. 258 (1996) 1-5
    • (1996) J. Mol. Biol. , vol.258 , pp. 1-5
    • Rizzi, M.1    Wittenberg, J.B.2    Coda, A.3    Ascenzi, P.4    Bolognesi, M.5
  • 14
    • 8844261238 scopus 로고    scopus 로고
    • High-level production of recombinant sulfide-reactive hemogobinI from Lucina pectinata in Escherichia coli. High yields of fully functional holoprotein synthesis in the BLi5 E. coli strain
    • León R.G., Munier-Lehmann H., Barzu O., Baudin-Creuza V., Pietri R., López-Garriga J., and Cadilla C.L. High-level production of recombinant sulfide-reactive hemogobinI from Lucina pectinata in Escherichia coli. High yields of fully functional holoprotein synthesis in the BLi5 E. coli strain. Protein Expr. Purif. 38 (2004) 184-195
    • (2004) Protein Expr. Purif. , vol.38 , pp. 184-195
    • León, R.G.1    Munier-Lehmann, H.2    Barzu, O.3    Baudin-Creuza, V.4    Pietri, R.5    López-Garriga, J.6    Cadilla, C.L.7
  • 15
    • 0027225870 scopus 로고
    • Oxygen and CO binding to triply NO and asymmetric NO/CO hemoglobin hybrids
    • Kiger L., Poyart C., and Marden M.C. Oxygen and CO binding to triply NO and asymmetric NO/CO hemoglobin hybrids. Biophys. J. 65 (1993) 1050-1058
    • (1993) Biophys. J. , vol.65 , pp. 1050-1058
    • Kiger, L.1    Poyart, C.2    Marden, M.C.3
  • 17
    • 0000348848 scopus 로고    scopus 로고
    • Bound CO is a molecular probe of electrostatic potential in the distal pocket of myoglobin
    • Phillips Jr. G.N., Teodoro M.L., Li T., Smith B., and Olson J.S. Bound CO is a molecular probe of electrostatic potential in the distal pocket of myoglobin. J. Phys. Chem., B 103 (1999) 8817-8829
    • (1999) J. Phys. Chem., B , vol.103 , pp. 8817-8829
    • Phillips Jr., G.N.1    Teodoro, M.L.2    Li, T.3    Smith, B.4    Olson, J.S.5
  • 18
    • 2542445605 scopus 로고    scopus 로고
    • Tyrosine B10 inhibits stabilization of bound carbon monoxide and oxygen in soybean leghemoglobin
    • Kundu S., Blouin G.C., Premer S.A., Sarah G., Olson J.S., and Hargrove M.S. 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
  • 19
    • 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
    • Das T.K., Couture M., Lee H.C., Peisach J., Rousseau D.L., Wittenberg B.A., Wittenberg J.B., and Guertin M. 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) 15360-15368
    • (1999) Biochemistry , vol.38 , pp. 15360-15368
    • 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
  • 21
    • 0037073478 scopus 로고    scopus 로고
    • The solution structure of the recombinant hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state
    • Falzone C.J., Christie V.B., Scott N.L., and Lecomte J.T. The solution structure of the recombinant hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state. J. Mol. Biol. 324 (2002) 1015-1029
    • (2002) J. Mol. Biol. , vol.324 , pp. 1015-1029
    • Falzone, C.J.1    Christie, V.B.2    Scott, N.L.3    Lecomte, J.T.4
  • 23
    • 10644274523 scopus 로고    scopus 로고
    • functional properties of hemoglobins from unicellular organisms as revealed by resonance Raman spectroscopy
    • Egawa T., and Yeh Structural S.R. functional properties of hemoglobins from unicellular organisms as revealed by resonance Raman spectroscopy. J. Inorg. Biochem. 99 (2005) 72-96
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 72-96
    • Egawa, T.1    Yeh Structural, S.R.2
  • 24
    • 2942755861 scopus 로고    scopus 로고
    • Heme distortion modulated by ligand-protein interactions in inducible nitric-oxide synthase
    • Li D., Stuehr D.J., Yeh S.R., and Rousseau D.L. Heme distortion modulated by ligand-protein interactions in inducible nitric-oxide synthase. J. Biol. Chem. 279 (2004) 26489-26499
    • (2004) J. Biol. Chem. , vol.279 , pp. 26489-26499
    • Li, D.1    Stuehr, D.J.2    Yeh, S.R.3    Rousseau, D.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.