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Titolo:
PROTON NUCLEAR-MAGNETIC-RESONANCE INVESTIGATION OF THE [2FE-2S](1-)-CONTAINING RIESKE-TYPE PROTEIN FROM XANTHOBACTER STRAIN PY2
Autore:
HOLZ RC; SMALL FJ; ENSIGN SA;
Indirizzi:
UTAH STATE UNIV,DEPT CHEM & BIOCHEM LOGAN UT 84322
Titolo Testata:
Biochemistry
fascicolo: 48, volume: 36, anno: 1997,
pagine: 14690 - 14696
SICI:
0006-2960(1997)36:48<14690:PNIOT[>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
SPIN-LATTICE RELAXATION; IRON-SULFUR PROTEINS; THEORETICAL INTERPRETATION; PSEUDOMONAS-CEPACIA; CIRCULAR-DICHROISM; 2FE-2S CENTER; PURIFICATION; SPECTROSCOPY; DIOXYGENASE; CLUSTER;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
R.C. Holz et al., "PROTON NUCLEAR-MAGNETIC-RESONANCE INVESTIGATION OF THE [2FE-2S](1-)-CONTAINING RIESKE-TYPE PROTEIN FROM XANTHOBACTER STRAIN PY2", Biochemistry, 36(48), 1997, pp. 14690-14696

Abstract

Proton NMR spectra of the Rieske-type ferredoxin from Xanthobacter strain Py2 were recorded in both H2O and D2O buffered; solutions at pH 7.2. Several well-resolved hyperfine-shifted H-1 NMR signals were observed in the 90 to -20 ppm chemical shift range. Comparison of spectra recorded in H2O and D2O buffered solutions indicated that the signals at -11.4(L) and -15.5 (M) ppm were solvents exchangeable and thus were assigned to the two histidine (NH)-H-epsilon 2 protons. The remaining observed signals were assigned based upon chemical shift, T-1 values, and one-dimensional nuclear Overhauser effect (nOe) saturation transfer experiments to either (CH)-H-beta or (CH)-H-alpha protons of clustercysteinyl or histidine ligands. Upon oxidation of the [2Fe-2S] cluster, only two broad resonances were observed, indicating that the two Fe(III) ions are strongly antiferromagnetically coupled. In addition, the temperature dependence of each observed hyperfine-shifted signal in the reduced state was determined, providing information about the magnetic properties of the [2Fe-2S](1-) cluster. Fits of the temperature data observed for each resonance to equations describing the hyperfine shift with their Boltzmann weighting factors provided a Delta E-L value of 185 +/- 26 cm(-1) which, in turn, gives -2J as 124 cm(-1). These data indicate that the two iron centers in the reduced [2Fe-2S] Rieske-type center are moderately antiferromagnetically coupled, The combination of these data with the available spectroscopic and crystallographic results for Rieske-type proteins has provided new insights into therole of the Rieske-type protein from Xanthobacter strain Py2 in alkene oxidation.

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Documento generato il 27/11/20 alle ore 12:55:28