Similar CO binding sites in bacterial cytochrome bo and mammalian cytochrome c oxidase

Properties of the active site of terminal oxidases may be studied by examining the stable carbon monoxide-bound adducts. The resonance Raman and the infrared absorption spectra of CO-bound mammalian cytochrome c oxidase have revealed several structural characteristics of the heme pocket, including a...

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Bibliographic Details
Published in:Journal of the American Chemical Society 1993-04, Vol.115 (8), p.3390-3391
Main Authors: JIANLING WANG, YUAN-CHIN CHING, ROUSSEAU, D. L, HILL, J. J, RUMBLEY, J, GENNIS, R. B
Format: Article
Language:English
Subjects:
400201 - Chemical & Physicochemical Properties
550200 - Biochemistry
Analytical, structural and metabolic biochemistry
BASIC BIOLOGICAL SCIENCES
Biological and medical sciences
CARBON COMPOUNDS
CARBON MONOXIDE
CARBON OXIDES
CHALCOGENIDES
CYTOCHROME OXIDASE
ENZYMES
Escherichia coli
Fundamental and applied biological sciences. Psychology
HAEM DEHYDROGENASES
Hemoproteins
INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY
Metalloproteins
MOLECULAR STRUCTURE
ORGANIC COMPOUNDS
OXIDES
OXIDOREDUCTASES
OXYGEN COMPOUNDS
PROTEINS
RAMAN SPECTRA
SPECTRA
SPECTROSCOPY
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Summary:Properties of the active site of terminal oxidases may be studied by examining the stable carbon monoxide-bound adducts. The resonance Raman and the infrared absorption spectra of CO-bound mammalian cytochrome c oxidase have revealed several structural characteristics of the heme pocket, including an indication, from the frequencies of the Fe-CO stretching mode at 520 cm super(-1) and the C-O stretching mode at 1963 cm super(-1), that the proximal histidine, trans to the bound CO, has either atypical bonding or is not bound in the CO adduct. In a report on the Raman spectrum of a bacterial terminal oxidase (cytochrome bo), two Fe-CO stretching modes were identified, one at 489 and another at 523 cm super(-1). The latter line, with a frequency very near to that reported for CO-bound cytochrome a sub(3) in mammalian oxidases, was interpreted as a minor component originating from an anomalous CO binding site in the bacterial enzyme. The shift of the major line from 520 cm super(-1) in the mammalian enzyme to 489 cm super(-1) in the bacterial enzyme suggests a qualitative difference in the structure of the oxygen binding site. In an effort to clarify this difference, we have reexamined the Raman spectra of the CO-bound adduct of the cytochrome bo complex.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja00061a072