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Titolo:
CONCERTED MOVEMENT OF SIDE-CHAINS IN THE HEME VICINITY OBSERVED ON LIGAND-BINDING IN CYTOCHROME C' FROM RHODOBACTER-CAPSULATUS
Autore:
TAHIROV TH; MISAKI S; MEYER TE; CUSANOVICH MA; HIGUCHI Y; YASUOKA N;
Indirizzi:
HIMEJI INST TECHNOL,FAC SCI,DEPT LIFE SCI HIMEJI HYOGO 67812 JAPAN HIMEJI INST TECHNOL,FAC SCI,DEPT LIFE SCI HIMEJI HYOGO 67812 JAPAN UNIV ARIZONA,DEPT BIOCHEM TUCSON AZ 85721 AZERBAIJAN ACAD SCI,INST INORGAN & PHYS CHEM BAKU 370143 AZERBAIJAN
Titolo Testata:
Nature structural biology
fascicolo: 5, volume: 3, anno: 1996,
pagine: 459 - 464
SICI:
1072-8368(1996)3:5<459:CMOSIT>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
RHODOSPIRILLUM-MOLISCHIANUM; CHROMATIUM-VINOSUM; FERRICYTOCHROME C'; BACTERIAL CYTOCHROMES-C'; ETHYL ISOCYANIDE; HEME PROTEIN; RESOLUTION; DISSOCIATION; CYANIDE; STATE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
T.H. Tahirov et al., "CONCERTED MOVEMENT OF SIDE-CHAINS IN THE HEME VICINITY OBSERVED ON LIGAND-BINDING IN CYTOCHROME C' FROM RHODOBACTER-CAPSULATUS", Nature structural biology, 3(5), 1996, pp. 459-464

Abstract

We have determined the structure of n-butylisocyanide-bound Rhodobacter capsulatus cytochrome c'. This is the first example of a ligand-bound structure of a class IIa cytochrome c. Compared with the structure of native cytochrome c', there are significant conformational changes of amino acid residues in the haem vicinity, accompanied by a rearrangement of the hydrogen bonding pattern. The results suggest that rearrangements resulting from ligand binding could drive dimer dissociation in some species and also that the haem propionate may participate in proton transfer.

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Documento generato il 14/07/20 alle ore 17:59:43