메뉴 건너뛰기




Volumn 15, Issue 4, 2006, Pages 312-327

Dynamics of NO rebinding to the heme domain of NO synthase-like proteins from bacterial pathogens

Author keywords

Arginine; Bacterial NOS like proteins; Endothelial NO synthase; Geminate; Heme domain; Rebinding of NO; Tetrahydrobiopterin; Ultrafast kinetics

Indexed keywords

HEME; NITRIC OXIDE SYNTHASE LIKE PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 33750475167     PISSN: 10898603     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.niox.2006.03.010     Document Type: Article
Times cited : (15)

References (52)
  • 2
    • 0035209452 scopus 로고    scopus 로고
    • Nitric oxide: comparative synthesis and signaling in animal and plant cells
    • Wendehenne D., Pugin A., Klessig D.F., and Durner J. Nitric oxide: comparative synthesis and signaling in animal and plant cells. Trends Plant Sci. 6 4 (2001) 177-183
    • (2001) Trends Plant Sci. , vol.6 , Issue.4 , pp. 177-183
    • Wendehenne, D.1    Pugin, A.2    Klessig, D.F.3    Durner, J.4
  • 3
    • 0035091010 scopus 로고    scopus 로고
    • Nitric oxide signaling and transcriptional control of denitrification genes in Pseudomonas stutzeri
    • Vollack, and Zumft. Nitric oxide signaling and transcriptional control of denitrification genes in Pseudomonas stutzeri. J. Bact. 183 (2001) 2516
    • (2001) J. Bact. , vol.183 , pp. 2516
    • Vollack1    Zumft2
  • 4
    • 0042858242 scopus 로고    scopus 로고
    • Nitric oxide formation by Escherichia coli. Dependence on nitrite reductase, the NO-sensing regulator Fnr, and flavohemoglobin Hmp
    • Corker H., and Poole R.K. Nitric oxide formation by Escherichia coli. Dependence on nitrite reductase, the NO-sensing regulator Fnr, and flavohemoglobin Hmp. J. Biol. Chem. 278 (2003) 31584
    • (2003) J. Biol. Chem. , vol.278 , pp. 31584
    • Corker, H.1    Poole, R.K.2
  • 5
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification
    • Zumft W.G. Cell biology and molecular basis of denitrification. Microbiol. Mol. Biol. Rev. 61 4 (1997) 533-616
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , Issue.4 , pp. 533-616
    • Zumft, W.G.1
  • 6
    • 0025802065 scopus 로고
    • Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase
    • Bredt D.S., Hwang P.M., Glatt C.E., Lowenstein C., Reed R.R., and Snyder S.H. Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase. Nature 351 (1991) 714-718
    • (1991) Nature , vol.351 , pp. 714-718
    • Bredt, D.S.1    Hwang, P.M.2    Glatt, C.E.3    Lowenstein, C.4    Reed, R.R.5    Snyder, S.H.6
  • 7
    • 33750443334 scopus 로고    scopus 로고
    • C.S. Raman, P. Martasek, B.S.S. Masters, in: The Porphyrin Handbook, K.M. Kadish, K. M. Smith, R. Guilard (Eds.), vol. 4, 2000, pp. 293-339.
  • 8
    • 33750465598 scopus 로고
    • Purification and characterization of nitric oxide synthase (NOSNoc) from a Nocardia species
    • Chen Y., and Rosazza J.P.N. Purification and characterization of nitric oxide synthase (NOSNoc) from a Nocardia species. J. Bacteriol. Sept 5 (1995) 122-128
    • (1995) J. Bacteriol. , vol.Sept 5 , pp. 122-128
    • Chen, Y.1    Rosazza, J.P.N.2
  • 9
    • 0030780266 scopus 로고    scopus 로고
    • Synthesis of nitric oxide from the two equivalent guanidino nitrogens of l-arginine by Lactobacillus fermentum
    • Morita H., Yoshikawa H., Sakata R., Nagata Y., and Tanaka H. Synthesis of nitric oxide from the two equivalent guanidino nitrogens of l-arginine by Lactobacillus fermentum. J. Bacteriol. 179 (1997) 7812-7815
    • (1997) J. Bacteriol. , vol.179 , pp. 7812-7815
    • Morita, H.1    Yoshikawa, H.2    Sakata, R.3    Nagata, Y.4    Tanaka, H.5
  • 11
    • 0037125928 scopus 로고    scopus 로고
    • Structure of a nitric oxide synthase heme protein from Bacillus subtilis
    • Pant K., Bilwes A.M., Adak S., Stuehr D.J., and Crane B.R. Structure of a nitric oxide synthase heme protein from Bacillus subtilis. Biochemistry 41 37 (2002) 11071-11079
    • (2002) Biochemistry , vol.41 , Issue.37 , pp. 11071-11079
    • Pant, K.1    Bilwes, A.M.2    Adak, S.3    Stuehr, D.J.4    Crane, B.R.5
  • 12
    • 0037013239 scopus 로고    scopus 로고
    • Direct evidence for nitric oxide production by a nitric-oxide synthase-like protein from Bacillus subtilis
    • Adak S., Aulak K.S., and Stuehr D.J. Direct evidence for nitric oxide production by a nitric-oxide synthase-like protein from Bacillus subtilis. J. Biol. Chem. 27 18 (2002) 16167-16171
    • (2002) J. Biol. Chem. , vol.27 , Issue.18 , pp. 16167-16171
    • Adak, S.1    Aulak, K.S.2    Stuehr, D.J.3
  • 13
    • 24644502115 scopus 로고    scopus 로고
    • Structure of a loose dimer in nitric oxide synthase assembly
    • Pant K., and Crane B.R. Structure of a loose dimer in nitric oxide synthase assembly. J. Mol. Biol. 352 (2005) 932-940
    • (2005) J. Mol. Biol. , vol.352 , pp. 932-940
    • Pant, K.1    Crane, B.R.2
  • 15
    • 0036899390 scopus 로고    scopus 로고
    • Crystal structure of SANOS, a bacterial nitric oxide synthase oxygenase protein from Staphylococcus aureus
    • Bird L.E., Ren J., Zhang J., Foxwell N., Hawkins A.R., Charles I.G., and Stammers D.K. Crystal structure of SANOS, a bacterial nitric oxide synthase oxygenase protein from Staphylococcus aureus. Structure (Camb). 10 12 (2002) 1687-1696
    • (2002) Structure (Camb). , vol.10 , Issue.12 , pp. 1687-1696
    • Bird, L.E.1    Ren, J.2    Zhang, J.3    Foxwell, N.4    Hawkins, A.R.5    Charles, I.G.6    Stammers, D.K.7
  • 16
    • 17844383744 scopus 로고    scopus 로고
    • Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan
    • Buddha M.R., and Crane B.R. Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan. Nat. Struct. Mol. Biol. 12 3 (2005) 274-275
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , Issue.3 , pp. 274-275
    • Buddha, M.R.1    Crane, B.R.2
  • 17
    • 2442498473 scopus 로고    scopus 로고
    • A conserved Val to Ile switch near the heme pocket of animal and bacterial nitric-oxide synthases helps determine their distinct catalytic profiles
    • Wang Z.Q., Wei C.C., Sharma M., Pant K., Crane B.R., and Stuehr D.J. A conserved Val to Ile switch near the heme pocket of animal and bacterial nitric-oxide synthases helps determine their distinct catalytic profiles. J. Biol. Chem. 279 18 (2004) 19018-19025
    • (2004) J. Biol. Chem. , vol.279 , Issue.18 , pp. 19018-19025
    • Wang, Z.Q.1    Wei, C.C.2    Sharma, M.3    Pant, K.4    Crane, B.R.5    Stuehr, D.J.6
  • 19
    • 9644264047 scopus 로고    scopus 로고
    • An unusual tryptophanyl tRNA synthetase interacts with nitric oxide synthase in Deinococcus radiodurans
    • Buddha M.R., Tao T., Parry R.J., and Crane B.R. An unusual tryptophanyl tRNA synthetase interacts with nitric oxide synthase in Deinococcus radiodurans. J. Biol. Chem. 279 (2004) 49567-49570
    • (2004) J. Biol. Chem. , vol.279 , pp. 49567-49570
    • Buddha, M.R.1    Tao, T.2    Parry, R.J.3    Crane, B.R.4
  • 20
    • 33750445004 scopus 로고    scopus 로고
    • P. Martasek, P. Nioche, A.-L. Tsai, C.S. Raman, in: 12th International Conference on Cytochrome P450, La Grande Motte, France, Abstract, 2001, P606.
  • 21
    • 33750486903 scopus 로고    scopus 로고
    • C.S. Raman, ibid., CL2-3, (2001).
  • 22
    • 0038712079 scopus 로고    scopus 로고
    • Geminate recombination of nitric oxide to endothelial nitric-oxide synthase and mechanistic implications
    • Negrerie M., Berka V., Vos M.H., Liebl U., Lambry J.C., Tsai A.L., and Martin J.L. Geminate recombination of nitric oxide to endothelial nitric-oxide synthase and mechanistic implications. J. Biol. Chem. 274 35 (1999) 24694-24702
    • (1999) J. Biol. Chem. , vol.274 , Issue.35 , pp. 24694-24702
    • Negrerie, M.1    Berka, V.2    Vos, M.H.3    Liebl, U.4    Lambry, J.C.5    Tsai, A.L.6    Martin, J.L.7
  • 23
    • 0036510622 scopus 로고    scopus 로고
    • Nitric oxide (NO) traffic in endothelial NO synthase. Evidence for a new NO binding site dependent on tetrahydrobiopterin?
    • Slama-Schwok A., Négrerie M., Berka V., Lambry J.C., Tsai A.L., Vos M.H., and Martin J.L. Nitric oxide (NO) traffic in endothelial NO synthase. Evidence for a new NO binding site dependent on tetrahydrobiopterin?. J. Biol. Chem. 277 (2002) 7581-7586
    • (2002) J. Biol. Chem. , vol.277 , pp. 7581-7586
    • Slama-Schwok, A.1    Négrerie, M.2    Berka, V.3    Lambry, J.C.4    Tsai, A.L.5    Vos, M.H.6    Martin, J.L.7
  • 24
    • 0035966114 scopus 로고    scopus 로고
    • Differences in three kinetic parameters underpin the unique catalytic profiles of nitric-oxide synthases I, II, and III*
    • Santolini J., Meade A.L., and Stuehr D.J. Differences in three kinetic parameters underpin the unique catalytic profiles of nitric-oxide synthases I, II, and III*. J. Biol. Chem. 276 (2001) 48887-48898
    • (2001) J. Biol. Chem. , vol.276 , pp. 48887-48898
    • Santolini, J.1    Meade, A.L.2    Stuehr, D.J.3
  • 25
    • 0034625348 scopus 로고    scopus 로고
    • Electron transfer, oxygen binding, and nitric oxide feedback inhibition in endothelial nitric-oxide synthase
    • Abu-Soud H.M., Ichimori K., Presta A., and Stuehr D.J. Electron transfer, oxygen binding, and nitric oxide feedback inhibition in endothelial nitric-oxide synthase. J. Biol. Chem. 275 (2000) 17349-17357
    • (2000) J. Biol. Chem. , vol.275 , pp. 17349-17357
    • Abu-Soud, H.M.1    Ichimori, K.2    Presta, A.3    Stuehr, D.J.4
  • 28
    • 23144435806 scopus 로고    scopus 로고
    • Dominant features of protein reaction dynamics: conformational relaxation and ligand migration
    • Treteau C., and Lavalette D. Dominant features of protein reaction dynamics: conformational relaxation and ligand migration. Biochem. Biophys. Acta 1724 (2005) 411-424
    • (2005) Biochem. Biophys. Acta , vol.1724 , pp. 411-424
    • Treteau, C.1    Lavalette, D.2
  • 31
    • 0000575758 scopus 로고
    • The interconversion of the 5,6,7,8-tetrahydro-, 6,7,8-dihydro-, and radical forms of 6,6,7,7-tetramethyldihydropterin. A model for the biopterin center of aromatic amino acid mixed function oxidases
    • Eberlein G., Bruice T.C., Lazarus R.A., Henrie R., and Benkovic S.J. The interconversion of the 5,6,7,8-tetrahydro-, 6,7,8-dihydro-, and radical forms of 6,6,7,7-tetramethyldihydropterin. A model for the biopterin center of aromatic amino acid mixed function oxidases. J. Am. Chem. Soc. 106 (1984) 7916-7924
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 7916-7924
    • Eberlein, G.1    Bruice, T.C.2    Lazarus, R.A.3    Henrie, R.4    Benkovic, S.J.5
  • 32
    • 0023919078 scopus 로고
    • Photophysics and reactivity of heme proteins: a femtosecond absorption study of hemoglobin, myoglobin, and protoheme
    • Petrich J., Poyart C., and Martin J.-L. Photophysics and reactivity of heme proteins: a femtosecond absorption study of hemoglobin, myoglobin, and protoheme. Biochemistry 27 (1988) 4049-4060
    • (1988) Biochemistry , vol.27 , pp. 4049-4060
    • Petrich, J.1    Poyart, C.2    Martin, J.-L.3
  • 34
    • 0026465102 scopus 로고
    • Diffusion-limited rates for monoclonal antibody binding to cytochrome c
    • Raman C.S., Jemmerson R., Nall B.T., and Allen M.J. Diffusion-limited rates for monoclonal antibody binding to cytochrome c. Biochemistry 31 (1992) 10370-10379
    • (1992) Biochemistry , vol.31 , pp. 10370-10379
    • Raman, C.S.1    Jemmerson, R.2    Nall, B.T.3    Allen, M.J.4
  • 35
    • 0037023751 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: ligand migration among protein cavities studied by Fourier transform infrared/temperature derivative spectroscopy
    • Lamb D.C., Nienhaus K., Arcovito A., Draghi F., Miele A.E., Brunori M., and Nienhaus G.U. Structural dynamics of myoglobin: ligand migration among protein cavities studied by Fourier transform infrared/temperature derivative spectroscopy. J. Biol. Chem. 277 (2002) 11636-11644
    • (2002) J. Biol. Chem. , vol.277 , pp. 11636-11644
    • Lamb, D.C.1    Nienhaus, K.2    Arcovito, A.3    Draghi, F.4    Miele, A.E.5    Brunori, M.6    Nienhaus, G.U.7
  • 36
    • 11344282347 scopus 로고    scopus 로고
    • Dynamics of geminate recombination of NO with myoglobin in aqueous solution probed by femtosecond mid-IR spectroscopy
    • Kim S., Jin G., and Lim M. Dynamics of geminate recombination of NO with myoglobin in aqueous solution probed by femtosecond mid-IR spectroscopy. J. Phys. Chem. 108 (2004) 20366-20375
    • (2004) J. Phys. Chem. , vol.108 , pp. 20366-20375
    • Kim, S.1    Jin, G.2    Lim, M.3
  • 37
    • 0035895937 scopus 로고    scopus 로고
    • Mapping the pathways for O2 entry into and exit from myoglobin
    • Scott E.E., Gibson Q.H., and Olson J.S. Mapping the pathways for O2 entry into and exit from myoglobin. J. Biol. Chem. 276 (2001) 5177-5188
    • (2001) J. Biol. Chem. , vol.276 , pp. 5177-5188
    • Scott, E.E.1    Gibson, Q.H.2    Olson, J.S.3
  • 38
    • 4143105792 scopus 로고    scopus 로고
    • CO-trapping site in heme oxygenase revealed by photolysis of its CO-bound heme complex: mechanism of escaping from product inhibition
    • Sugishima M., Sakamoto H., Noguchi M., and Fukuyama K. CO-trapping site in heme oxygenase revealed by photolysis of its CO-bound heme complex: mechanism of escaping from product inhibition. J. Mol. Biol. 341 (2004) 7-13
    • (2004) J. Mol. Biol. , vol.341 , pp. 7-13
    • Sugishima, M.1    Sakamoto, H.2    Noguchi, M.3    Fukuyama, K.4
  • 40
    • 3042587451 scopus 로고    scopus 로고
    • A survey of active site access channels in cytochromes P450
    • Wade R.C., Winn P.J., Schlichting I., and Sudarko. A survey of active site access channels in cytochromes P450. J. Inorg. Biochem. 98 (2004) 1175-1182
    • (2004) J. Inorg. Biochem. , vol.98 , pp. 1175-1182
    • Wade, R.C.1    Winn, P.J.2    Schlichting, I.3    Sudarko4
  • 42
    • 0035826593 scopus 로고    scopus 로고
    • Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors
    • Li H., Raman C.S., Martasek P., Masters B.S.S., and Poulos T.L. Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors. Biochemistry 40 (2001) 5399
    • (2001) Biochemistry , vol.40 , pp. 5399
    • Li, H.1    Raman, C.S.2    Martasek, P.3    Masters, B.S.S.4    Poulos, T.L.5
  • 43
    • 0032416666 scopus 로고    scopus 로고
    • Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center
    • Raman C.S., Li H., Martasek P., Kral V., Masters B.S., and Poulos T.L. Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center. Cell 95 7 (1998) 939-950
    • (1998) Cell , vol.95 , Issue.7 , pp. 939-950
    • Raman, C.S.1    Li, H.2    Martasek, P.3    Kral, V.4    Masters, B.S.5    Poulos, T.L.6
  • 45
    • 0034817107 scopus 로고    scopus 로고
    • Unusual role of Tyr588 of neuronal nitric oxide synthase in controlling substrate specificity and electron transfer
    • Sato Y., Sagami I., Matsui T., and Shimizu T. Unusual role of Tyr588 of neuronal nitric oxide synthase in controlling substrate specificity and electron transfer. Biochem. Biophys. Res. Commun. 281 (2001) 621-626
    • (2001) Biochem. Biophys. Res. Commun. , vol.281 , pp. 621-626
    • Sato, Y.1    Sagami, I.2    Matsui, T.3    Shimizu, T.4
  • 46
    • 0030917621 scopus 로고    scopus 로고
    • Mutagenesis of acidic residues in the oxygenase domain of inducible nitric-oxide synthase identifies a glutamate involved in arginine binding
    • Gachhui R., Ghosh D.K., Wu C., Parkinson J., Crane B.R., and Stuehr D.J. Mutagenesis of acidic residues in the oxygenase domain of inducible nitric-oxide synthase identifies a glutamate involved in arginine binding. Biochemistry 36 (1997) 5097-5103
    • (1997) Biochemistry , vol.36 , pp. 5097-5103
    • Gachhui, R.1    Ghosh, D.K.2    Wu, C.3    Parkinson, J.4    Crane, B.R.5    Stuehr, D.J.6
  • 47
    • 0032560966 scopus 로고    scopus 로고
    • Comparative effects of substrates and pterin cofactor on the heme midpoint potential in inducible and neuronal nitric oxide synthase
    • Presta A., Weber-Main A.M., Stankoich M.T., and Stuehr D.J. Comparative effects of substrates and pterin cofactor on the heme midpoint potential in inducible and neuronal nitric oxide synthase. J. Am. Chem. Soc. 120 (1998) 9460-9465
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9460-9465
    • Presta, A.1    Weber-Main, A.M.2    Stankoich, M.T.3    Stuehr, D.J.4
  • 49
    • 0026628064 scopus 로고
    • Protein dynamics
    • Di Ioro E.E. Protein dynamics. FEBS Lett. 307 (1992) 14-19
    • (1992) FEBS Lett. , vol.307 , pp. 14-19
    • Di Ioro, E.E.1
  • 50
    • 0028013478 scopus 로고
    • Thermal expansion of hen egg-white lysozyme. Comparison of the 1.9 Å resolution structures of the tetragonal form of the enzyme at 100 K and 298 K
    • Young A.C., Tilton R.F., and Dewan J.C. Thermal expansion of hen egg-white lysozyme. Comparison of the 1.9 Å resolution structures of the tetragonal form of the enzyme at 100 K and 298 K. J. Mol. Biol. 235 (1994) 302-317
    • (1994) J. Mol. Biol. , vol.235 , pp. 302-317
    • Young, A.C.1    Tilton, R.F.2    Dewan, J.C.3
  • 52
    • 0037035537 scopus 로고    scopus 로고
    • Resonance Raman detection of the Fe{single bond}S bond in endothelial nitric oxide synthase
    • Schelvis J.P., Berka V., Babcock G.T., and Tsai A.L. Resonance Raman detection of the Fe{single bond}S bond in endothelial nitric oxide synthase. Biochemistry 41 (2002) 5695-5701
    • (2002) Biochemistry , vol.41 , pp. 5695-5701
    • Schelvis, J.P.1    Berka, V.2    Babcock, G.T.3    Tsai, A.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.