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Resonance Raman investigation of nitric oxide bonding in nitrosylhemoglobin A and -myoglobin: detection of bound N-O stretching and Fe-NO stretching vibrations from the hexacoordinated NO-heme complex.

Abstract：

:With excitation at 406.7 nm, we have observed the resonance Raman enhancement of the bound v(N-O) stretch at approximately 1623 cm-1 in nitrosylhemoglobin A and nitrosylmyoglobin, indicating the existence of a charge-transfer transition underlying the strong Soret band. The v(Fe-NO) stretch at 551 cm-1 has also been detected in the Soret as well as in the Q-band region, a phenomenon similar to the v(Fe-O2) and v(Fe-CO) stretches in oxy and carbon monoxy hemoproteins. It appears that these iron-ligand vibrations ay be resonance enhanced via porphyrin pi leads to pi transitions. Upon addition of inositol hexaphosphate at pH 6.0, the v(Fe-NO) stretch at 551 cm-1 and a low-frequency mode at 301 cm-1 exhibit an intensity decrease by approximately one-half. Contrary to the work of Stong et al. [Stong, J. D., Burke, J. M., Daly, P., Wright. P., & Spiro, T. G. (1980) J. Am. Chem. Soc. 102, 5815], who employed an excitation wavelength at 454.5 nm, we observed no intensity increase at 592 cm-1 attributable to the v(Fe-NO) stretch from the pentacoordinated NO-heme complex in the alpha subunits.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Tsubaki M,Yu NT

doi

10.1021/bi00535a005

subject

Has Abstract

pub_date

1982-03-16 00:00:00

pages

1140-4

issue

6

eissn

0006-2960

issn

1520-4995

journal_volume

21

pub_type

杂志文章

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