Resonance Raman and EPR of nitrosyl human hemoglobin and chains, carp hemoglobin, and model compounds. Implications for the nitrosyl heme coordination state.
We report the joint resonance Raman (RR) and electron paramagnetic resonance (epr) study of five- and six-coordinate nitrosyl heme model compounds and of the titled nitrosyl hemoproteins. Both epr and RR spectra fall into two types which, in the models, correspond to five- and six-coordinate nitrosyl hemes. However, neither RR nor epr spectroscopy is highly sensitive to the nature of the bond between a nitrosyl heme and a coordinated nitrogenous base, nor do the results of one technique uniformly correlate with those of the other. It is not possible to use epr spectroscopy as a test for the coordination state of a nitrosyl heme. The position of the highest frequency (depolarized) RR band possibly provides such a test. Any breaking of the very weak bond between nitrosyl heme and proximal histidine in T state human HbNO is more a consequence of tertiary structural features unique to the human alphaNO chains than it is of properties of the T quaternary conformation.
D000818:Animals; D002347:Carps; D004578:Electron Spin Resonance Spectroscopy; D006418:Heme; D006454:Hemoglobins; D006801:Humans; D009603:Nitroso Compounds; D011487:Protein Conformation; D013045:Species Specificity; D013053:Spectrophotometry; D013059:Spectrum Analysis, Raman
D006454:Hemoglobins; D009603:Nitroso Compounds; D006418:Heme