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001-es BibID:	BIBFORM031415
035-os BibID:	WOS:000078985400009 PMID:10499105
Első szerző:	Martel, Paulo J.
Cím:	Comparative redox and Pka calculations on cytochrome c3 from several desulfovibrio species using continuum electrostatic methods / Paulo J. Martel, Cláudio M. Soares, António M. Baptista, Monika Fuxreiter, Gábor Náray-Szabó, Ricardo O. Louro, Maria A. Carrondo
Dátum:	1999
Megjegyzések:	A comparative study of the pH-dependent redox mechanisms of several members of the cytochrome c(3) family has been carried out. In a previous work, the molecular determinants of this dependency (the so-called redox-Bohr effect) were investigated for one species using continuum electrostatic methods to find groups with a titrating range and strength of interaction compatible with a mediating role in the redox-Bohr effect. Here we clarify these aspects in the light of new and improved pK(a) calculations, our findings supporting the hypothesis of propionate D from heme I being the main effector in the pH-dependent modulation of the cytochrome c(3) redox potentials in all the a molecules studied here. However, the weaker (but significant) role of other titrating groups cannot be excluded, their importance and identity changing with the particular molecule under study. We also calculate the relative redox potentials of the four heme centers among the selected members of the c(3) family, using a continuum electrostatic method that takes into account both solvation and interaction effects. Comparison of the calculated values with available data for the microscopic redox potentials was undertaken, the quality of the agreement being dependent upon the choice of the dielectric constant for the protein interior. We find that high dielectric constants give best correlations, while low values result in better magnitudes for the calculated potentials. The possibility that the crystallographic calcium ion in c(3) from Desulfovibrio gigas may be present in the solution structure was tested, and found to be likely.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban külföldön készült közlemény
Megjelenés:	Journal of biological inorganic chemistry. - 4 : 1 (1999), p. 73-86. -
További szerzők:	Soares, Cláudio M. Baptista, António M. Fuxreiter Mónika (1969-) (kutató vegyész) Náray-Szabó Gábor Louro, Ricardo O. Carrondo, Maria A.
Internet cím:	DOI elektronikus változat Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM031407
035-os BibID:	WOS:000243366400009 PMID:17214552
Első szerző:	Mones, Letif
Cím:	Metal-binding sites at the active site of restriction endonuclease BamHI can conform to a one-ion mechanism / Letif Mones, István Simon, Monika Fuxreiter
Dátum:	2007
ISSN:	1431-6730
Megjegyzések:	The number of metal ions required for phosphoryl transfer in restriction endonucleases is still an unresolved question in molecular biology. The two Ca2+ and Mn2+ ions observed in the pre- and post-reactive complexes of BamHI conform to the classical two-metal ion choreography. We probed the Mg2+ cofactor positions at the active site of BamHI by molecular dynamics simulations with one and two metal ions present and identified several catalytically relevant sites. These can mark the pathway of a single ion during catalysis, suggesting its critical role, while a regulatory function is proposed for a possible second ion.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban egyetemen (Magyarországon) készült közlemény
Megjelenés:	Biological chemistry. - 388 : 1 (2007), p. 73-78. -
További szerzők:	Simon István Fuxreiter Mónika (1969-) (kutató vegyész)
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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