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Titolo:
C-13 MAS NMR EVIDENCE FOR STRUCTURAL SIMILARITY OF L162YL MUTANT AND RHODOBACTER-SPHAEROIDES R26 RC, DESPITE WIDELY DIFFERENT CYTOCHROME C(2)-MEDIATED REREDUCTION KINETICS OF THE OXIDIZED PRIMARY DONOR
Autore:
VANROSSUM BJ; WACHTVEITL J; RAAP J; VANDERHOEF K; GAST P; LUGTENBURG J; OESTERHELT D; DEGROOT HJM;
Indirizzi:
LEIDEN UNIV,GORLAEUS LABS,LEIDEN INST CHEM,POB 9502 NL-2300 RA LEIDENNETHERLANDS LEIDEN UNIV,GORLAEUS LABS,LEIDEN INST CHEM NL-2300 RA LEIDEN NETHERLANDS MAX PLANCK INST BIOCHEM,DEPT MEMBRANE BIOCHEM D-82152 MARTINSRIED GERMANY LEIDEN UNIV,HUYGENS LAB,DEPT BIOPHYS NL-2300 RA LEIDEN NETHERLANDS
Titolo Testata:
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
fascicolo: 12, volume: 53, anno: 1997,
pagine: 2201 - 2208
SICI:
1386-1425(1997)53:12<2201:CMNEFS>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOTOSYNTHETIC REACTION-CENTER; PHOTOOXIDIZED BACTERIOCHLOROPHYLL DIMER; L-SUBUNIT PLAYS; RHODOPSEUDOMONAS-VIRIDIS; ELECTRON-TRANSFER; MEDIATED REREDUCTION; TETRAHEME CYTOCHROME; MAGNETIC-RESONANCE; PROTEIN SUBUNITS; SPECIAL PAIR;
Keywords:
PHOTOSYNTHESIS; ISOTOPE LABELING; MAS NMR; R26; MUTANT;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
B.J. Vanrossum et al., "C-13 MAS NMR EVIDENCE FOR STRUCTURAL SIMILARITY OF L162YL MUTANT AND RHODOBACTER-SPHAEROIDES R26 RC, DESPITE WIDELY DIFFERENT CYTOCHROME C(2)-MEDIATED REREDUCTION KINETICS OF THE OXIDIZED PRIMARY DONOR", SPECT ACT A, 53(12), 1997, pp. 2201-2208

Abstract

CP/MAS NMR data collected from L162YL mutant [4'-C-13]Tyr-enriched Rhodobacter sphaeroides RCs reveal that Tyr L162 is in a slightly heterogeneous and probably rigid section of the protein complex. The differences in chemical shifts of the individual components relative to thoseof the [4'-C-13]Tyr Rhodobacter sphaeroides R26 response are 0.2 ppm or less. This is small compared to the total dispersion of [4'-C-13] isotropic shifts, similar to 5 ppm, which measures the shift range due to variations in the microscopic environment between the various tyrosines in the protein complex. The structural changes in the mutant withrespect to Rhodobacter sphaeroides R26, as probed by the labels, are thus minimal on the scale of the NMR. This suggests that the dramatic decrease of re-reduction rate of the oxidized primary donor P upon mutation (Farchaus et al., Biochemistry 32 (1993) 10885-10893) cannot be attributed to significant structural changes in the protein. Hence theNMR is in line with the current view that the decrease of the re-reduction rate in the mutant originates from slow reorientation of the docked cytochrome. (C) 1997 Elsevier Science B.V.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 17:27:37