Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Orientation-selected ENDOR of the active center in Chromatium vinosum [NiFe] hydrogenase in the oxidized "ready" state
Autore:
Gessner, C; Stein, M; Albracht, SPJ; Lubitz, W;
Indirizzi:
Tech Univ Berlin, Max Volmer Inst Biophys Chem & Biochem, D-10623 Berlin, Germany Tech Univ Berlin Berlin Germany D-10623 Biochem, D-10623 Berlin, Germany Univ Amsterdam, EC Slater Inst Biochem Res, NL-1018 TV Amsterdam, Netherlands Univ Amsterdam Amsterdam Netherlands NL-1018 TV V Amsterdam, Netherlands
Titolo Testata:
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
fascicolo: 4, volume: 4, anno: 1999,
pagine: 379 - 389
SICI:
0949-8257(199908)4:4<379:OEOTAC>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSITION-METAL COMPLEXES; BAND PULSED ENDOR; DESULFOVIBRIO-GIGAS; NICKEL; SPECTROSCOPY; SITE; LIGAND; ACTIVATION; RESONANCE; CLUSTER;
Keywords:
[NiFe] hydrogenase; Chromatium vinosum; electron paramagnetic resonance; orientation-selected ENDOR; proton hyperfine tensors;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Lubitz, W Tech Univ Berlin, Max Volmer Inst Biophys Chem & Biochem, Str 17Juni 135,D-10623 Berlin, Germany Tech Univ Berlin Str 17 Juni 135 Berlin Germany D-10623 Germany
Citazione:
C. Gessner et al., "Orientation-selected ENDOR of the active center in Chromatium vinosum [NiFe] hydrogenase in the oxidized "ready" state", J BIOL I CH, 4(4), 1999, pp. 379-389

Abstract

Electron nuclear double resonance (ENDOR) was applied to study the active site of the oxidized ''ready'' state, Ni-r, in the [NiFe] hydrogenase of Chromatium vinosum. The magnetic field dependance of the EPR was used to select specific subsets of molecules contributing to the ENDOR response by stepping through the EPR envelope. Three hyperfine couplings could be clearly followed over the complete field range. Two protons, H1 and H2, display a very similar large isotropic coupling of 12.5 and 12.6 MHz, respectively. Their dipolar coupling is small (2.1 and 1.4 MHz, respectively). A third proton, H3, exhibits a small isotropic coupling of 0.5 MHz and a larger anisotropic contribution of 3.5 MHz. Based on a comparison with structural data obtained from X-ray crystallography of single crystals of hydrogenases from Desulfovibrio gigas and D. vulgaris e known g-tensor orientation of Ni-r,Ni- an assignment of the H-1 hyperfine couplings could be achieved. H1 and H2 were assigned to the beta-CH2 protons of the bridging cysteine Cys533 and H3could belong to a beta-CH2 proton of Cys68 or to a protonated cysteine (-SH) of Cys68 or Cys530.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 05:28:42