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Volumn 52, Issue 40, 2013, Pages 7007-7021

Reactivity and dynamics of H2S, NO, and O2 interacting with hemoglobins from lucina pectinata

Author keywords

[No Author keywords available]

Indexed keywords

DIFFERENT PROPORTIONS; DIFFUSION OF H; GEMINATE REBINDING; LIGAND INTERACTIONS; LUCINA PECTINATA; TERTIARY STRUCTURES; TIME-RESOLVED ABSORPTION; VIBRATIONALLY EXCITED;

EID: 84885450646     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400745a     Document Type: Article
Times cited : (36)

References (66)
  • 1
    • 0029759256 scopus 로고    scopus 로고
    • Gill structure in Lucina pectinata (Bivalvia: Lucinidae) with reference to hemoglobin in bivalves with symbiotic sulphur-oxidizing bacteria
    • Frenkiel, L., Gros, O., and Moueza, M. (1996) Gill structure in Lucina pectinata (Bivalvia: Lucinidae) with reference to hemoglobin in bivalves with symbiotic sulphur-oxidizing bacteria Mar. Biol. (Heidelberg, Ger.) 125, 511-524
    • (1996) Mar. Biol. (Heidelberg, Ger.) , vol.125 , pp. 511-524
    • Frenkiel, L.1    Gros, O.2    Moueza, M.3
  • 2
    • 0025026382 scopus 로고
    • Hemoglobins of the Lucina pectinata /bacteria symbiosis: Molecular properties, kinetics and equilibria of reactions with ligands
    • Kraus, D. W. and Wittenberg, J. B. (1990) Hemoglobins of the Lucina pectinata /bacteria symbiosis: Molecular properties, kinetics and equilibria of reactions with ligands J. Biol. Chem. 265, 16043-16053
    • (1990) J. Biol. Chem. , vol.265 , pp. 16043-16053
    • Kraus, D.W.1    Wittenberg, J.B.2
  • 3
    • 0001114834 scopus 로고
    • Myoglobin and structure of proteins: Crystallographic analysis and data processing techniques reveal molecular architecture
    • Kendrew, J. C. (1963) Myoglobin and structure of proteins: Crystallographic analysis and data processing techniques reveal molecular architecture Science 139, 1259-1266
    • (1963) Science , vol.139 , pp. 1259-1266
    • Kendrew, J.C.1
  • 4
    • 0028409107 scopus 로고
    • Discovery of new ligand binding pathways in myoglobin by random mutagenesis
    • Huang, X. and Boxer, S. G. (1994) Discovery of new ligand binding pathways in myoglobin by random mutagenesis Nat. Struct. Biol. 1, 226-229
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 226-229
    • Huang, X.1    Boxer, S.G.2
  • 5
    • 0031722046 scopus 로고    scopus 로고
    • Myoglobin mutants giving the largest geminate yield in CO rebinding in the nanosecond time domain
    • Sugimoto, T., Unno, M., Shiro, Y., Dou, Y., and Ikeda-Saito, M. (1998) Myoglobin mutants giving the largest geminate yield in CO rebinding in the nanosecond time domain Biophys. J. 75, 2188-2194
    • (1998) Biophys. J. , vol.75 , pp. 2188-2194
    • Sugimoto, T.1    Unno, M.2    Shiro, Y.3    Dou, Y.4    Ikeda-Saito, M.5
  • 7
    • 0033522382 scopus 로고    scopus 로고
    • Heme protein dynamics revealed by geminate nitric oxide recombination in mutants of iron and cobalt myoglobin
    • Kholodenko, Y., Gooding, E. A., Dou, Y., Ikeda-Saito, M., and Hochstrasser, R. M. (1999) Heme protein dynamics revealed by geminate nitric oxide recombination in mutants of iron and cobalt myoglobin Biochemistry 38, 5918-5924
    • (1999) Biochemistry , vol.38 , pp. 5918-5924
    • Kholodenko, Y.1    Gooding, E.A.2    Dou, Y.3    Ikeda-Saito, M.4    Hochstrasser, R.M.5
  • 11
    • 0029876402 scopus 로고    scopus 로고
    • The possible role of hydrogen sulfide as an endogenous neuromodulator
    • Abe, K. and Kimura, H. (1996) The possible role of hydrogen sulfide as an endogenous neuromodulator J. Neurosci. 76, 1066-1071
    • (1996) J. Neurosci. , vol.76 , pp. 1066-1071
    • Abe, K.1    Kimura, H.2
  • 12
    • 79959374222 scopus 로고    scopus 로고
    • Hydrogen sulfide as a regulator of systemic functions in vertebrates
    • Varaksin, A. A. and Puschina, E. V. (2011) Hydrogen sulfide as a regulator of systemic functions in vertebrates Neurophysiology 43, 62-72
    • (2011) Neurophysiology , vol.43 , pp. 62-72
    • Varaksin, A.A.1    Puschina, E.V.2
  • 14
    • 35748959038 scopus 로고    scopus 로고
    • Hydrogen sulphide and its therapeutic potential
    • Szabo, C. (2007) Hydrogen sulphide and its therapeutic potential Nat. Rev. Drug Discovery 6, 917-935
    • (2007) Nat. Rev. Drug Discovery , vol.6 , pp. 917-935
    • Szabo, C.1
  • 15
    • 42149180604 scopus 로고    scopus 로고
    • The interaction of human neuroglobin with hydrogen sulphide
    • Brittain, T., Yosaatmadja, Y., and Henty, K. (2008) The interaction of human neuroglobin with hydrogen sulphide IUBMB Life 60, 135-138
    • (2008) IUBMB Life , vol.60 , pp. 135-138
    • Brittain, T.1    Yosaatmadja, Y.2    Henty, K.3
  • 16
    • 57049151773 scopus 로고    scopus 로고
    • The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulfide: Chemical mechanism and physiological significance
    • Cooper, C. E. and Brown, G. C. (2008) The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulfide: Chemical mechanism and physiological significance J. Bioenerg. Biomembr. 40, 533-539
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 533-539
    • Cooper, C.E.1    Brown, G.C.2
  • 17
    • 78650504604 scopus 로고    scopus 로고
    • Structural basis for substrate activation and regulation by cystathionine β-synthase (CBS) domains in cystathionine β-synthase
    • Koutmos, M., Kabil, O., Smith, J. L., and Banerjee, R. (2010) Structural basis for substrate activation and regulation by cystathionine β-synthase (CBS) domains in cystathionine β-synthase Proc. Natl. Acad. Sci. U.S.A. 107, 20958-20963
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 20958-20963
    • Koutmos, M.1    Kabil, O.2    Smith, J.L.3    Banerjee, R.4
  • 18
    • 69849112573 scopus 로고    scopus 로고
    • Heme regulation of human cystathionine-synthase activity: Insights from fluorescence and Raman spectroscopy
    • Weeks, C. L., Singh, S., Madzelan, P., Banerjee, R., and Spiro, T. G. (2009) Heme regulation of human cystathionine-synthase activity: Insights from fluorescence and Raman spectroscopy J. Am. Chem. Soc. 131, 12809-12816
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 12809-12816
    • Weeks, C.L.1    Singh, S.2    Madzelan, P.3    Banerjee, R.4    Spiro, T.G.5
  • 19
    • 0031589557 scopus 로고    scopus 로고
    • The possible role of hydrogen sulfide as an endogenous smooth muscle relaxant in synergy with nitric oxide
    • Hosoki, R., Matsuki, N., and Kimura, H. (1997) The possible role of hydrogen sulfide as an endogenous smooth muscle relaxant in synergy with nitric oxide Biochem. Biophys. Res. Commun. 237, 527-531
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 527-531
    • Hosoki, R.1    Matsuki, N.2    Kimura, H.3
  • 20
    • 66549128367 scopus 로고    scopus 로고
    • Interactions of the gaseous neuromodulators nitric oxide, carbon monoxide, and hydrogen sulfide in the salamander retina
    • Pong, W. W. and Eldred, W. D. (2009) Interactions of the gaseous neuromodulators nitric oxide, carbon monoxide, and hydrogen sulfide in the salamander retina J. Neurosci. Res. 87, 2356-2364
    • (2009) J. Neurosci. Res. , vol.87 , pp. 2356-2364
    • Pong, W.W.1    Eldred, W.D.2
  • 21
    • 78650757014 scopus 로고    scopus 로고
    • Carbon monoxide stimulates global protein methylation via its inhibitory action on cystathionine β-synthase
    • Yamamoto, T., Takano, N., Ishiwata, K., and Suematsu, M. (2011) Carbon monoxide stimulates global protein methylation via its inhibitory action on cystathionine β-synthase J. Clin. Biochem. Nutr. 48, 96-100
    • (2011) J. Clin. Biochem. Nutr. , vol.48 , pp. 96-100
    • Yamamoto, T.1    Takano, N.2    Ishiwata, K.3    Suematsu, M.4
  • 23
    • 77953238444 scopus 로고    scopus 로고
    • Recombinant hemoglobin II from Lucina Pectinata: A large scale method for hemeprotein expression in E. coli
    • Ramos, C., Pietri, R., Lorenzo, W., Roman, E., Cadilla, C., and Lopez-Garriga, J. (2010) Recombinant hemoglobin II from Lucina Pectinata: A large scale method for hemeprotein expression in E. coli Protein J. 29, 143-151
    • (2010) Protein J. , vol.29 , pp. 143-151
    • Ramos, C.1    Pietri, R.2    Lorenzo, W.3    Roman, E.4    Cadilla, C.5    Lopez-Garriga, J.6
  • 25
    • 33746540471 scopus 로고    scopus 로고
    • Photoinduced coordination dynamics of cytochrome c: Ferrous versus ferric species studied by time-resolved resonance Raman and transient absorption spectroscopies
    • Negrerie, M., Cianetti, S., Vos, M. H., Martin, J.-L., and Kruglik, S. G. (2006) Photoinduced coordination dynamics of cytochrome c: Ferrous versus ferric species studied by time-resolved resonance Raman and transient absorption spectroscopies J. Phys. Chem. B 110, 12766-12781
    • (2006) J. Phys. Chem. B , vol.110 , pp. 12766-12781
    • Negrerie, M.1    Cianetti, S.2    Vos, M.H.3    Martin, J.-L.4    Kruglik, S.G.5
  • 26
    • 10744221411 scopus 로고    scopus 로고
    • Investigations of heme protein absorption line shapes, vibrational relaxation, and resonance Raman scattering on ultrafast time scales
    • Ye, X., Demidov, A., Rosca, F., Wang, W., Kumar, A., Ionascu, D., Zhu, L. Y., Barrick, D., Wharton, D., and Champion, P. M. (2003) Investigations of heme protein absorption line shapes, vibrational relaxation, and resonance Raman scattering on ultrafast time scales J. Phys. Chem. A 107, 8156-8165
    • (2003) J. Phys. Chem. A , vol.107 , pp. 8156-8165
    • Ye, X.1    Demidov, A.2    Rosca, F.3    Wang, W.4    Kumar, A.5    Ionascu, D.6    Zhu, L.Y.7    Barrick, D.8    Wharton, D.9    Champion, P.M.10
  • 27
    • 84863142015 scopus 로고    scopus 로고
    • Quaternary structure controls ligand dynamics in soluble guanylate cyclase
    • Yoo, B.-K., Lamarre, I., Martin, J.-L., and Negrerie, M. (2012) Quaternary structure controls ligand dynamics in soluble guanylate cyclase J. Biol. Chem. 287, 6851-6859
    • (2012) J. Biol. Chem. , vol.287 , pp. 6851-6859
    • Yoo, B.-K.1    Lamarre, I.2    Martin, J.-L.3    Negrerie, M.4
  • 28
    • 0023919078 scopus 로고
    • Photophysics and reactivity of heme-proteins: A femtosecond absorption study of hemoglobin, myoglobin and protoheme
    • Petrich, J. W., Poyart, C., and Martin, J. L. (1988) Photophysics and reactivity of heme-proteins: A femtosecond absorption study of hemoglobin, myoglobin and protoheme Biochemistry 27, 4049-405
    • (1988) Biochemistry , vol.27 , pp. 4049-4405
    • Petrich, J.W.1    Poyart, C.2    Martin, J.L.3
  • 31
    • 0030012157 scopus 로고    scopus 로고
    • Spectral and ligand-binding properties of an unusual hemoprotein, the ferric form of soluble guanylate cyclase
    • Stone, J. R., Sands, R. H., Dunham, W. R., and Marletta, M. A. (1996) Spectral and ligand-binding properties of an unusual hemoprotein, the ferric form of soluble guanylate cyclase Biochemistry 35, 3258-3262
    • (1996) Biochemistry , vol.35 , pp. 3258-3262
    • Stone, J.R.1    Sands, R.H.2    Dunham, W.R.3    Marletta, M.A.4
  • 33
    • 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)
    • Peterson, E. S., Huang, S. C., Wang, J. Q., Miller, L. M., Vidugiris, G., Kloek, A. P., Goldberg, D. E., Chance, M. R., Wittenberg, J. B., and Friedman, J. M. (1997) 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, 13110-13121
    • (1997) Biochemistry , vol.36 , pp. 13110-13121
    • Peterson, E.S.1    Huang, S.C.2    Wang, J.Q.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
  • 34
    • 77956390441 scopus 로고    scopus 로고
    • Picosecond primary structural transition of the heme is retarded after nitric oxide binding to heme proteins
    • Kruglik, S. G., Yoo, B.-K., Franzen, S., Vos, M. H., Martin, J.-L., and Negrerie, M. (2010) Picosecond primary structural transition of the heme is retarded after nitric oxide binding to heme proteins Proc. Natl. Acad. Sci. U.S.A. 107, 13678-13783
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 13678-13783
    • Kruglik, S.G.1    Yoo, B.-K.2    Franzen, S.3    Vos, M.H.4    Martin, J.-L.5    Negrerie, M.6
  • 39
    • 0028035164 scopus 로고
    • Structure of the sulfide-reactive hemoglobin from the clam Lucina pectinata: Crystallographic analysis at 1.5 Å resolution
    • Rizzi, M., Wittenberg, J. B., Coda, A., Fasano, M., Ascenzi, P., and Bolognesi, M. (1994) Structure of the sulfide-reactive hemoglobin from the clam Lucina pectinata: Crystallographic analysis at 1.5 Å resolution J. Mol. Biol. 244, 86-99
    • (1994) J. Mol. Biol. , vol.244 , pp. 86-99
    • Rizzi, M.1    Wittenberg, J.B.2    Coda, A.3    Fasano, M.4    Ascenzi, P.5    Bolognesi, M.6
  • 40
    • 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. (1996) Structural bases for sulfide recognition in Lucina pectinata hemoglobin I J. Mol. Biol. 258, 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
  • 41
    • 84864815292 scopus 로고    scopus 로고
    • Tyrosine B10 triggers a heme propionate hydrogen bonding network loop with glutamine E7 moiety
    • Ramos-Santana, B. J. and Lopez-Garriga, J. (2012) Tyrosine B10 triggers a heme propionate hydrogen bonding network loop with glutamine E7 moiety Biochem. Biophys. Res. Commun. 424, 771-776
    • (2012) Biochem. Biophys. Res. Commun. , vol.424 , pp. 771-776
    • Ramos-Santana, B.J.1    Lopez-Garriga, J.2
  • 42
    • 0036791007 scopus 로고    scopus 로고
    • Ultrafast ligand rebinding in the heme domain of the oxygen sensors FixL and Dos: General regulatory implications for heme-based sensors
    • Liebl, U., Bouzhir-Sima, L., Negrerie, M., Martin, J.-L., and Vos, M. H. (2002) Ultrafast ligand rebinding in the heme domain of the oxygen sensors FixL and Dos: General regulatory implications for heme-based sensors Proc. Natl. Acad. Sci. U.S.A. 99, 12771-12776
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 12771-12776
    • Liebl, U.1    Bouzhir-Sima, L.2    Negrerie, M.3    Martin, J.-L.4    Vos, M.H.5
  • 43
    • 34250681839 scopus 로고    scopus 로고
    • Subpicosecond oxygen trapping in the heme pocket of the oxygen sensor FixL observed by time-resolved resonance Raman spectroscopy
    • Kruglik, S. G., Jasaitis, A., Hola, K., Yamashita, T., Liebl, U., Martin, J.-L., and Vos, M. H. (2007) Subpicosecond oxygen trapping in the heme pocket of the oxygen sensor FixL observed by time-resolved resonance Raman spectroscopy Proc. Natl. Acad. Sci. U.S.A. 104, 7408-7413
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 7408-7413
    • Kruglik, S.G.1    Jasaitis, A.2    Hola, K.3    Yamashita, T.4    Liebl, U.5    Martin, J.-L.6    Vos, M.H.7
  • 44
    • 84859555292 scopus 로고    scopus 로고
    • Ultrafast heme-ligand recombination in truncated hemoglobin HbO from Mycobacterium tuberculosis: A ligand cage
    • Jasaitis, A., Ouellet, H., Lambry, J. C., Martin, J. L., Friedman, J. M., Guertin, M., and Vos, M. H. (2012) Ultrafast heme-ligand recombination in truncated hemoglobin HbO from Mycobacterium tuberculosis: A ligand cage Chem. Phys. 396, 10-16
    • (2012) Chem. Phys. , vol.396 , pp. 10-16
    • Jasaitis, A.1    Ouellet, H.2    Lambry, J.C.3    Martin, J.L.4    Friedman, J.M.5    Guertin, M.6    Vos, M.H.7
  • 45
    • 0028228087 scopus 로고
    • Ultrafast measurements of geminate recombination of NO with site-specific mutants of human myoglobin
    • Petrich, J. W., Lambry, J. C., Balasubramanian, S., Lambright, D. G., Boxer, S. G., and Martin, J. L. (1994) Ultrafast measurements of geminate recombination of NO with site-specific mutants of human myoglobin J. Mol. Biol. 238, 437-444
    • (1994) J. Mol. Biol. , vol.238 , pp. 437-444
    • Petrich, J.W.1    Lambry, J.C.2    Balasubramanian, S.3    Lambright, D.G.4    Boxer, S.G.5    Martin, J.L.6
  • 46
    • 8844237890 scopus 로고    scopus 로고
    • Functional characterization of the purified holo form of hemoglobin i from Lucina pectinata overexpressed in Escherichia coli
    • Collazo, E., Pietri, R., De Jesús, W., Ramos, C., Del Toro, A., León, R. G., Cadilla, C. L., and López-Garriga, J. (2004) Functional characterization of the purified holo form of hemoglobin I from Lucina pectinata overexpressed in Escherichia coli Protein J. 23, 239-245
    • (2004) Protein J. , vol.23 , pp. 239-245
    • Collazo, E.1    Pietri, R.2    De Jesús, W.3    Ramos, C.4    Del Toro, A.5    León, R.G.6    Cadilla, C.L.7    López-Garriga, J.8
  • 47
    • 34548674201 scopus 로고    scopus 로고
    • The heme pocket geometry of Lucina pectinata hemoglobin II restricts nitric oxide and peroxide entry: Model of ligand control for the design of a stable oxygen carrier
    • De Jesus-Bonilla, W., Jia, Y. P., Alayash, A. I., and Lopez-Garriga, J. (2007) The heme pocket geometry of Lucina pectinata hemoglobin II restricts nitric oxide and peroxide entry: Model of ligand control for the design of a stable oxygen carrier Biochemistry 46, 10451-10460
    • (2007) Biochemistry , vol.46 , pp. 10451-10460
    • De Jesus-Bonilla, W.1    Jia, Y.P.2    Alayash, A.I.3    Lopez-Garriga, J.4
  • 48
    • 77950548846 scopus 로고    scopus 로고
    • 2 and acts as a gate for ligand entry in both subunits of adult human hemoglobin
    • 2 and acts as a gate for ligand entry in both subunits of adult human hemoglobin J. Biol. Chem. 285, 8840-8854
    • (2010) J. Biol. Chem. , vol.285 , pp. 8840-8854
    • Birukou, I.1    Schweers, R.L.2    Olson, J.S.3
  • 49
    • 0027293798 scopus 로고
    • Kinetics of ligand binding to Pseudoterranova decipiens and Ascaris suum hemoglobins and to Leu-29 to Tyr sperm whale myoglobin mutant
    • Gibson, Q. H., Regan, R., Olson, J. S., Carver, T. E., Dixon, B., Pohajdak, B., Sharma, P. K., and Vinogradov, S. N. (1993) Kinetics of ligand binding to Pseudoterranova decipiens and Ascaris suum hemoglobins and to Leu-29 to Tyr sperm whale myoglobin mutant J. Biol. Chem. 268, 16993-16998
    • (1993) J. Biol. Chem. , vol.268 , pp. 16993-16998
    • Gibson, Q.H.1    Regan, R.2    Olson, J.S.3    Carver, T.E.4    Dixon, B.5    Pohajdak, B.6    Sharma, P.K.7    Vinogradov, S.N.8
  • 53
    • 0345761151 scopus 로고    scopus 로고
    • Oxygen-avid hemoglobin of Ascaris
    • Golberg, D. E. (1999) Oxygen-avid hemoglobin of Ascaris Chem. Rev. 99, 3371-3378
    • (1999) Chem. Rev. , vol.99 , pp. 3371-3378
    • Golberg, D.E.1
  • 55
    • 55249106911 scopus 로고    scopus 로고
    • Ligand binding to truncated hemoglobin N from Mycobacterium tuberculosis is strongly modulated by the interplay between the distal heme pocket residues and internal water
    • Ouellet, Y. H., Daigle, R., Lagüe, P., Dantsker, D., Milani, M., Bolognesi, M., Friedman, J. M., and Guertin, M. (2008) Ligand binding to truncated hemoglobin N from Mycobacterium tuberculosis is strongly modulated by the interplay between the distal heme pocket residues and internal water J. Biol. Chem. 283, 27270-27278
    • (2008) J. Biol. Chem. , vol.283 , pp. 27270-27278
    • Ouellet, Y.H.1    Daigle, R.2    Lagüe, P.3    Dantsker, D.4    Milani, M.5    Bolognesi, M.6    Friedman, J.M.7    Guertin, M.8
  • 56
    • 33744541890 scopus 로고    scopus 로고
    • Role of heme iron coordination and protein structure in the dynamics and geminate rebinding of nitric oxide to H93G myoglobin: Implications for NO-sensors
    • Negrerie, M., Kruglik, S. G., Lambry, J.-C., Vos, M. H., Martin, J.-L., and Franzen, S. (2006) Role of heme iron coordination and protein structure in the dynamics and geminate rebinding of nitric oxide to H93G myoglobin: Implications for NO-sensors J. Biol. Chem. 281, 10389-10398
    • (2006) J. Biol. Chem. , vol.281 , pp. 10389-10398
    • Negrerie, M.1    Kruglik, S.G.2    Lambry, J.-C.3    Vos, M.H.4    Martin, J.-L.5    Franzen, S.6
  • 57
    • 33947491915 scopus 로고    scopus 로고
    • Molecular basis for nitric oxide dynamics and affinity with Alcaligenes xylosoxidans cytochrome c ′
    • Kruglik, S. G., Lambry, J.-C., Cianetti, S., Martin, J.-L., Eady, R. R., Andrew, C. R., and Negrerie, M. (2007) Molecular basis for nitric oxide dynamics and affinity with Alcaligenes xylosoxidans cytochrome c ′ J. Biol. Chem. 282, 5053-5062
    • (2007) J. Biol. Chem. , vol.282 , pp. 5053-5062
    • Kruglik, S.G.1    Lambry, J.-C.2    Cianetti, S.3    Martin, J.-L.4    Eady, R.R.5    Andrew, C.R.6    Negrerie, M.7
  • 58
    • 84874619845 scopus 로고    scopus 로고
    • Picosecond binding of the His ligand to four-coordinate heme in cytochrome c′: A one-way gate for releasing proximal NO
    • Yoo, B.-K., Lamarre, I., Martin, J.-L., Andrew, C., and Negrerie, M. (2013) Picosecond binding of the His ligand to four-coordinate heme in cytochrome c′: A one-way gate for releasing proximal NO J. Am. Chem. Soc. 135, 3248-3254
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 3248-3254
    • Yoo, B.-K.1    Lamarre, I.2    Martin, J.-L.3    Andrew, C.4    Negrerie, M.5
  • 60
    • 47049122888 scopus 로고    scopus 로고
    • Hemoglobins from Mycobacterium tuberculosis and Campylobacter jejuni: A comparative study with resonance Raman spectroscopy
    • Lu, C., Egawa, T., Mukai, M., Poole, R. K., and Yeh, S.-R. (2008) Hemoglobins from Mycobacterium tuberculosis and Campylobacter jejuni: A comparative study with resonance Raman spectroscopy Methods Enzymol. 437, 255-286
    • (2008) Methods Enzymol. , vol.437 , pp. 255-286
    • Lu, C.1    Egawa, T.2    Mukai, M.3    Poole, R.K.4    Yeh, S.-R.5
  • 61
    • 79955783127 scopus 로고    scopus 로고
    • A hydrogen-bonding network formed by the B10-E7-E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxification
    • Igarashi, J., Kobayashi, K., and Matsuoka, A. (2011) A hydrogen-bonding network formed by the B10-E7-E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxification JBIC, J. Biol. Inorg. Chem. 16, 599-609
    • (2011) JBIC, J. Biol. Inorg. Chem. , vol.16 , pp. 599-609
    • Igarashi, J.1    Kobayashi, K.2    Matsuoka, A.3
  • 63
  • 65
    • 0032032160 scopus 로고    scopus 로고
    • Nitric oxide myoglobin: Crystal structure and analysis of ligand geometry
    • Brucker, E. A., Olson, J. S., Ikeda-Saito, M., and Phillips, G. N. (1998) Nitric oxide myoglobin: Crystal structure and analysis of ligand geometry Proteins 30, 352-356
    • (1998) Proteins , vol.30 , pp. 352-356
    • Brucker, E.A.1    Olson, J.S.2    Ikeda-Saito, M.3    Phillips, G.N.4
  • 66
    • 0036667731 scopus 로고    scopus 로고
    • Rotamer libraries in the 21st century
    • Dunbrack, R. L. (2002) Rotamer libraries in the 21st century Curr. Opin. Struct. Biol. 12, 431-440
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 431-440
    • Dunbrack, R.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.