메뉴 건너뛰기




Volumn 128, Issue 7, 2006, Pages 2170-2171

15N HYSCORE characterization of the fully deprotonated, reduced form of the Archaeal Rieske [2Fe-2S] center

Author keywords

[No Author keywords available]

Indexed keywords

HISTIDINE; IRON; IRON SULFUR PROTEIN; LIGAND; NITROGEN 15; SULFUR; SULREDOXIN; UNCLASSIFIED DRUG; ARCHAEAL PROTEIN; NITROGEN; PROTON; RIESKE IRON-SULFUR PROTEIN; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 33644549118     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0562393     Document Type: Article
Times cited : (12)

References (24)
  • 18
    • 33644522872 scopus 로고    scopus 로고
    • note
    • p has been assigned primarily to the peptide nitrogen involved in the NH-S-type hydrogen bond(s) with the bridging sulfide atom(s) of the reduced cluster. Its substantial increase from ∼1.0 MHz at pH 7 to 1.4 MHz at pH 13.3 may reflect a proportional increase of unpaired electron spin density onto the bridging sulfide atoms in the fully deprotonated, reduced Rieske center at pH 13.3, providing additional support for redistribution of the unpaired spin density over the reduced cluster. Additional contribution to this phenomenon is local conformational adjustment of the immediate cluster environment, which is expected for a protein-bound system at pH 13.3, as reported for the oxidized protein near and above pH 12 by resonance Raman spectroscopy (ref 11).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.