Resonance Raman study on pentacoordinated and hexacoordinated ferrous nitrosyl myoglobin

The resonance Raman (RR) spectra of the hexacoordinated ferrous nitrosyl sperm whale myoglobin are independent of pH for both the 200–700 cm and 1350–1650 cm −1 regions. In agreement with earlier ESR [Eur. J. Biochem. (1972) 31, 578–584] and contrary to recent RR [Biochemistry (1982) 21, 6989–6995]...

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Bibliographic Details
Published in:FEBS Letters
Main Authors: Mackin, H.C., Benko, B., Yu, N.-T., Gersonde, K.
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 1983
Subjects:
Sperm whale
Online Access:http://dx.doi.org/10.1016/0014-5793(83)80577-8
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2F0014-5793%2883%2980577-8
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2F0014-5793(83)80577-8
https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2883%2980577-8
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Summary:The resonance Raman (RR) spectra of the hexacoordinated ferrous nitrosyl sperm whale myoglobin are independent of pH for both the 200–700 cm and 1350–1650 cm −1 regions. In agreement with earlier ESR [Eur. J. Biochem. (1972) 31, 578–584] and contrary to recent RR [Biochemistry (1982) 21, 6989–6995] results the RR spectra do not indicate a transition to the pentacoordinated ferrous nitrosyl derivative at low pH. However, interaction of the protein with sodium dodecylsulfate, leads to the formation of a pure pentacoordinated state with a typical RR spectrum. Replacement of 14 NO for 15 NO in this pentacoordinated ferrous nitrosyl derivative does not exhibit isotope effects using 413.1 excitation.

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