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Volumn 130, Issue 44, 2008, Pages 14384-14385

Red-excitation resonance Raman analysis of the νFe=O mode of ferryl-oxo hemoproteins

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; FERRYLMYOGLOBIN; HEMOPROTEIN; IRON; OXYGEN; OXYHEMOGLOBIN; PEROXIDASE; PORPHYRIN;

EID: 55549085579     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja805735g     Document Type: Article
Times cited : (6)

References (15)
  • 2
    • 0003889472 scopus 로고
    • Spiro, T. G, Ed, John Wiley and Sons: New York
    • (b) Spiro, T. G., Ed. Biological Applications of Raman Spectroscopy; John Wiley and Sons: New York, 1987; Vol. 3.
    • (1987) Biological Applications of Raman Spectroscopy , vol.3
  • 15
    • 55549099414 scopus 로고    scopus 로고
    • Abbreviations: ARP: Arthromyces ramosus peroxidase; ARP-II: Compound II of ARP; Compound II: a reaction intermediate of peroxidases that has one oxidative equivalent higher than the ferric state; CcO: Cytochrome c oxidase; HRP: Horseradish peroxidase; HRP-II: Compound II of HRP; Mb: myoglobin; P intermediate: a reaction intermediate of cytochrome c oxidase that has two oxidative equivalents higher than the ferric state produced on heme a3 and having an Fe=O fragment like Compound II with the location of one oxidative equivalent being uncertain; REP: Raman excitation profile; RR: resonance Raman
    • 3 and having an Fe=O fragment like Compound II with the location of one oxidative equivalent being uncertain; REP: Raman excitation profile; RR: resonance Raman.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.