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Volumn 119, Issue 36, 1997, Pages 8409-8416

Low-power picosecond resonance Raman evidence for histidine ligation to heme a3 after photodissociation of CO from cytochrome c oxidase

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C OXIDASE; HEME;

EID: 0030760534     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja964133p     Document Type: Article
Times cited : (32)

References (82)
  • 39
    • 1842347618 scopus 로고    scopus 로고
    • note
    • 2+, and therefore, normalization to this peak will eliminate all heme a modes from the difference spectra.
  • 40
    • 1842310234 scopus 로고    scopus 로고
    • note
    • We estimate the percentage of CO photolysis by comparing our pump-probe resonance Raman spectrum (Figure 2b) with the transient resonance Raman spectra of Lou et al. (ref 13, their Figure 1) that are shown as a function of laser energy density, i.e., percentage of CO photolysis.
  • 41
    • 1842393197 scopus 로고    scopus 로고
    • note
    • 2+ modes in Rb. sphaeroides oxidase occur at essentially identical positions to these in the beef heart enzyme, we have observed in previous work (e.g., ref 19a) that their Raman cross sections vary substantially from those of the mammalian enzyme.
  • 50
    • 1842309246 scopus 로고    scopus 로고
    • note
    • 2+ macrocycle vibration along with the attenuation of the Fe-His intensity in the photoproduct (cf. Figure 1 in ref 12).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.