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Although the structural data obtained on PF2NH2 and (CH3)2NPF2 add considerable support to a ttbonding model, it should be mentioned that a recent infrared and Raman investigation of N[P(CF3)2]3 suggests that this molecule does not have a planar NP3 skeleton.19The 16N-H coupling constant (83.2 Hz) obtained for PF215NH2 is also consistent with a planar -NH2 group. A relationship between VuN_H and the percentage 2s character in the nitrogen orbital used in the NH bond has been developed.20 This relationship predicts 30% 2s character in the nitrogen orbitals bonded to the hy-(19) P.

We report 441.6 nm excitation resonance Raman spectra of oxidized and reduced monomeric heme a-imidazole, cytochrome oxidase-exogenous ligand complexes in various redox states, and alkaline denatured oxidase. These data show that, in reduced oxidase, the cytochrome a3 Raman spectrum has bands at 215, 364, 1230, and 1670 cm-1 not observed in the cytochrome a spectrum. The appearance of these bands in the reduced cytochrome a3 spectrum is due to interactions between the heme a of cytochrome a3 and its protein environment and not to intrinsic properties of heme a. These interactions are pH sensitive and strongly influence the vibrational spectra of both heme a groups. We assign the 1670-cm-1 band to the heme a formyl substituent and propose that the intensity of the 1670 cm-1 is high for reduced cytochrome a3 because the C==O lies in the porphyrin plane and is very weak for oxidized and reduced cytochrome a, oxidized cytochrome a3, and oxidized and reduced heme a-imidazole because the C==O lies out of the plane. We suggest that movement of the C==O in and out of the plane explains the ligand induced spectral shift in the optical absorption spectrum of reduced cytochrome a3. Finally, we confirm the observation of Adar & Yonetani (private communication) that, under laser illumination, resting oxidase is photoreactive.

Using a He-Ne CW laser source together with a digital photon counting system, we have obtained well resolved Raman spectra for adenosine mono-, di-, and triphosphate (AMP, ADP, ATP) in aqueous solution. Spectra of these compounds were studied as a function of pH from pH = 0.5 to 13.5 and between 550 and 1700 cm(-1). It was found possible to distinguish spectroscopically between the three phosphates over the pH range studied. A qualitative analysis of vibrational modes responsible for various spectral lines is given. Lines at about 960 and 1100 cm(-1) were found to be good indications of the degree of ionization of the terminal phosphate group.

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