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Volumn 121, Issue 6, 1999, Pages 1415-1416

Infrared evidence for Cu(B) ligation of photodissociated CO of cytochrome c oxidase at ambient temperatures and accompanied deprotonation of a carboxyl side chain of protein [19]

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C OXIDASE;

EID: 0033576974     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja983242w     Document Type: Letter
Times cited : (30)

References (31)
  • 22
    • 0005984305 scopus 로고
    • -1) with a narrow field-of-view (10°) cold stop. Temporal signal differences following photodissociation of CO-CcO by a nanosecond, 532-nm laser pulse operated at 10 Hz were digitized with a 12-bit AD converter and transferred to a computer. The recombination of photolyzed CO-CcO (τ = 15 ms) was assumed to be completed during the photolysis interval (100 ms). Typically the signals from 1024 or 4096 shots were averaged and converted to time-dependent absorbance data. The same measurements were repeated at different wavenumbers in a point-to-point manner. The highest spectral quality obtainable was attained by searching the best lasing mode of the diode laser with careful control of temperature and/or injection current. All of the apparatuses were controlled by a computer through a GPIB interfaçe, which improved the quality of data significantly.
    • (1990) Spectrosc. Int. , vol.2 , pp. 29-35
    • Mäntele, W.1    Hienerwadel, R.2    Lenz, F.3    Riedel, W.J.4    Grisar, R.5    Tacke, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.