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Volumn 122, Issue 36, 2000, Pages 8712-8716

Q-band ENDOR (electron nuclear double resonance) of the heme o3 liganding environment at the binuclear center in cytochrome bo3 from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME B; CYTOCHROME BO3; HEME; HEMOPROTEIN; HISTIDINE; METMYOGLOBIN; NITROGEN; OXIDOREDUCTASE; UNCLASSIFIED DRUG; WATER;

EID: 0034644426     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja000688f     Document Type: Article
Times cited : (12)

References (27)
  • 9
  • 20
    • 0343240956 scopus 로고    scopus 로고
    • note
    • NMR is the nuclear Zeeman frequency (=3.75 MHz here).
  • 21
    • 0023858982 scopus 로고    scopus 로고
    • note
    • ⊥ nonexchangeable heme meso proton features were identified in all ferric heme samples, there was no evidence from either cytochrome c or bo3 oxidase for exchangeable proton features, while exchangeable proton features were obvious from aquometmyoglobin.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.