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Volumn 129, Issue 48, 2007, Pages 14952-14958

Fourier transform infrared characterization of a CuB-nitrosyl complex in cytochrome ba3 from Thermus thermophilus: Relevance to NO reductase activity in heme-copper terminal oxidases

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; ELECTRONS; FOURIER TRANSFORM INFRARED SPECTROSCOPY; INFRARED RADIATION; NITRIC OXIDE; PROTEINS;

EID: 36849009272     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja074600a     Document Type: Article
Times cited : (28)

References (66)
  • 37
    • 36849007580 scopus 로고    scopus 로고
    • Because our Raman measurements utilize notch filters to attenuate the Raleigh scattering and can produce baseline perturbations below 200 cm -1, minor changes in this region are not discussed
    • -1, minor changes in this region are not discussed.
  • 38
    • 36849005619 scopus 로고    scopus 로고
    • While our instrumentation measures absolute Raman frequencies within 1 cm-1, relative shifts of <0.6 cm-1 can be reliably measured when two spectra are collected successively with no modification of the optical alignment and the spectrograph settings
    • -1 can be reliably measured when two spectra are collected successively with no modification of the optical alignment and the spectrograph settings.
  • 41
    • 36849013676 scopus 로고    scopus 로고
    • Kitagawa, T., Heme protein structure and the iron-histidine stretching mode. In Biological applications of Raman spectroscopy. 3. Resonance Raman spectra of hemes and metalloproteins; Spiro, T. G., Ed.; John Wiley & Sons: New York, 1988; 3, pp 97-131.
    • Kitagawa, T., Heme protein structure and the iron-histidine stretching mode. In Biological applications of Raman spectroscopy. Vol. 3. Resonance Raman spectra of hemes and metalloproteins; Spiro, T. G., Ed.; John Wiley & Sons: New York, 1988; Vol. 3, pp 97-131.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.