9. Goodrich, L.E., Paulat, F., Praneeth, V.K.K., Lehnert, N.: Electronic structure of hemenitrosyls and its significance for nitric oxide reactivity, sensing, transport, and toxicity in
biological systems. Inorg. Chem. 49, 6293–6316 (2010)
10. Shimizu, H., Obayashi, E., Gomi, Y., Arakawa, H., Park, S.Y., Nakamura, H., Adachi, S.,
Shoun, H., Shiro, Y.: Proton delivery in NO reduction by fungal nitric-oxide reductase –
cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type
and mutant enzymes. J. Biol. Chem. 275, 4816–4826 (2000)
11. Paulat, F., Lehnert, N.: Electronic structure of ferric heme nitrosyl complexes with thiolate
coordination. Inorg. Chem. 46, 1547–1549 (2007)
12. Rich, A.M., Armstrong, R.S., Ellis, P.J., Lay, P.A.: Determination of the Fe-ligand bond
lengths and Fe-N-O bond angles in horse heart ferric and ferrous nitrosylmyoglobin using
multiple-scattering XAFS analyses. J. Am. Chem. Soc. 120, 10827–10836 (1998)
13. Lanucara, F., Chiavarino, B., Crestoni, M.E., Scuderi, D., Sinha, R.K., Maitre, P., Fornarini,
S.: Naked five-coordinate Fe-III(NO) porphyrin complexes: vibrational and reactivity features.
Inorg. Chem. 50, 4445–4452 (2011)
14. Wyer, J.A., Nielsen, S.B.: Absorption by isolated ferric heme nitrosyl cations in vacuo.
Angew. Chem. Int. Ed. 51, 10256–10260 (2012)
15. Soldatova, A.V., Ibrahim, M., Olson, J.S., Czernuszewicz, R.S., Spiro, T.G.: New light on NO
bonding in Fe(III) heme proteins from resonance Raman spectroscopy and DFT modeling. J.
Am. Chem. Soc. 132, 4614–4625 (2010)
16. Olson, J.S., Phillips, G.N.: Myoglobin discriminates between O 2 , NO, and CO by electrostatic
interactions with the bound ligand. J. Biol. Inorg. Chem. 2, 544–552 (1997)
17. Spiro, T.G., Soldatova, A.V., Balakrishnan, G.: CO, NO and O 2 as vibrational probes of heme
protein interactions. Coord. Chem. Rev. 257, 511–527 (2013)
18. Laverman, L.E., Wanat, A., Oszajca, J., Stochel, G., Ford, P.C., van Eldik, R.: Mechanistic
studies on the reversible binding of nitric oxide to metmyoglobin. J. Am. Chem. Soc. 123,
285–293 (2001)
19. Sage, J.T., Morikis, D., Champion, P.M.: Spectroscopic studies of myoglobin at low pH –
heme structure and ligation. Biochemistry 30, 1227–1237 (1991)
20. Fang, M., Wilson, S.R., Suslick, K.S.: A four-coordinate Fe(III) porphyrin cation. J. Am.
Chem. Soc. 130, 1134–1135 (2008)
21. Wyer, J.A., Brøndsted Nielsen, S.: Absorption in the Q-band region by isolated ferric heme
+
and heme
+ (histidine) in vacuo. J. Chem. Phys. 133, 084306 (2010)
22. Lykkegaard, M.K., Ehlerding, A., Hvelplund, P., Kadhane, U., Kirketerp, M.-B.S., Brøndsted
Nielsen, S., Panja, S., Wyer, J.A., Zettergren, H.: A soret marker band for four-coordinate
ferric heme proteins from absorption spectra of isolated Fe(III)-heme
+ and Fe(III)-heme
+ (His)
ions in vacuo. J. Am. Chem. Soc. 130, 11856–11857 (2008)
23. Nonose, S., Tanaka, H., Okai, N., Shibakusa, T., Fuke, K.: Photo-induced reactions of
hemin
+ (DMSO) n clusters (n¼0-3) produced with electrospray ionization. Eur. Phys. J. D 20,
619–626 (2002)
24. Adar, F.: Electronic absorption spectra of hemes and hemoproteins. In: Dolphin, D. (ed.) The
Porphyrins. Physical Chemistry, Part A, vol. III. Academic Press, London (1978)
25. Filsinger, F., Ahn, D.S., Meijer, G., von Helden, G.: Photoexcitation of mass/charge selected
hemin
+ , caught in helium nanodroplets. Phys. Chem. Chem. Phys. 14, 13370–13377 (2012)
26. Brunet, C., Antoine, R., Lemoine, J., Dugourd, P.: Soret band of the gas-phase ferricytochrome c. J. Phys. Chem. Lett. 3, 698–702 (2012)
27. Bogumil, R., Maurus, R., Hildebrand, D.P., Brayer, G.D., Mauk, A.G.: Origin of the pHdependent spectroscopic properties of pentacoordinate metmyoglobin variants. Biochemistry
34, 10483–10490 (1995)
28. Cao, W.X., Christian, J.F., Champion, P.M., Rosca, F., Sage, J.T.: Water penetration and
binding to ferric myoglobin. Biochemistry 40, 5728–5737 (2001)
7 Spectroscopy of Ferric Heme and Protoporphyrin IX Ions In Vacuo
137
biological systems. Inorg. Chem. 49, 6293–6316 (2010)
10. Shimizu, H., Obayashi, E., Gomi, Y., Arakawa, H., Park, S.Y., Nakamura, H., Adachi, S.,
Shoun, H., Shiro, Y.: Proton delivery in NO reduction by fungal nitric-oxide reductase –
cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type
and mutant enzymes. J. Biol. Chem. 275, 4816–4826 (2000)
11. Paulat, F., Lehnert, N.: Electronic structure of ferric heme nitrosyl complexes with thiolate
coordination. Inorg. Chem. 46, 1547–1549 (2007)
12. Rich, A.M., Armstrong, R.S., Ellis, P.J., Lay, P.A.: Determination of the Fe-ligand bond
lengths and Fe-N-O bond angles in horse heart ferric and ferrous nitrosylmyoglobin using
multiple-scattering XAFS analyses. J. Am. Chem. Soc. 120, 10827–10836 (1998)
13. Lanucara, F., Chiavarino, B., Crestoni, M.E., Scuderi, D., Sinha, R.K., Maitre, P., Fornarini,
S.: Naked five-coordinate Fe-III(NO) porphyrin complexes: vibrational and reactivity features.
Inorg. Chem. 50, 4445–4452 (2011)
14. Wyer, J.A., Nielsen, S.B.: Absorption by isolated ferric heme nitrosyl cations in vacuo.
Angew. Chem. Int. Ed. 51, 10256–10260 (2012)
15. Soldatova, A.V., Ibrahim, M., Olson, J.S., Czernuszewicz, R.S., Spiro, T.G.: New light on NO
bonding in Fe(III) heme proteins from resonance Raman spectroscopy and DFT modeling. J.
Am. Chem. Soc. 132, 4614–4625 (2010)
16. Olson, J.S., Phillips, G.N.: Myoglobin discriminates between O 2 , NO, and CO by electrostatic
interactions with the bound ligand. J. Biol. Inorg. Chem. 2, 544–552 (1997)
17. Spiro, T.G., Soldatova, A.V., Balakrishnan, G.: CO, NO and O 2 as vibrational probes of heme
protein interactions. Coord. Chem. Rev. 257, 511–527 (2013)
18. Laverman, L.E., Wanat, A., Oszajca, J., Stochel, G., Ford, P.C., van Eldik, R.: Mechanistic
studies on the reversible binding of nitric oxide to metmyoglobin. J. Am. Chem. Soc. 123,
285–293 (2001)
19. Sage, J.T., Morikis, D., Champion, P.M.: Spectroscopic studies of myoglobin at low pH –
heme structure and ligation. Biochemistry 30, 1227–1237 (1991)
20. Fang, M., Wilson, S.R., Suslick, K.S.: A four-coordinate Fe(III) porphyrin cation. J. Am.
Chem. Soc. 130, 1134–1135 (2008)
21. Wyer, J.A., Brøndsted Nielsen, S.: Absorption in the Q-band region by isolated ferric heme
+
and heme
+ (histidine) in vacuo. J. Chem. Phys. 133, 084306 (2010)
22. Lykkegaard, M.K., Ehlerding, A., Hvelplund, P., Kadhane, U., Kirketerp, M.-B.S., Brøndsted
Nielsen, S., Panja, S., Wyer, J.A., Zettergren, H.: A soret marker band for four-coordinate
ferric heme proteins from absorption spectra of isolated Fe(III)-heme
+ and Fe(III)-heme
+ (His)
ions in vacuo. J. Am. Chem. Soc. 130, 11856–11857 (2008)
23. Nonose, S., Tanaka, H., Okai, N., Shibakusa, T., Fuke, K.: Photo-induced reactions of
hemin
+ (DMSO) n clusters (n¼0-3) produced with electrospray ionization. Eur. Phys. J. D 20,
619–626 (2002)
24. Adar, F.: Electronic absorption spectra of hemes and hemoproteins. In: Dolphin, D. (ed.) The
Porphyrins. Physical Chemistry, Part A, vol. III. Academic Press, London (1978)
25. Filsinger, F., Ahn, D.S., Meijer, G., von Helden, G.: Photoexcitation of mass/charge selected
hemin
+ , caught in helium nanodroplets. Phys. Chem. Chem. Phys. 14, 13370–13377 (2012)
26. Brunet, C., Antoine, R., Lemoine, J., Dugourd, P.: Soret band of the gas-phase ferricytochrome c. J. Phys. Chem. Lett. 3, 698–702 (2012)
27. Bogumil, R., Maurus, R., Hildebrand, D.P., Brayer, G.D., Mauk, A.G.: Origin of the pHdependent spectroscopic properties of pentacoordinate metmyoglobin variants. Biochemistry
34, 10483–10490 (1995)
28. Cao, W.X., Christian, J.F., Champion, P.M., Rosca, F., Sage, J.T.: Water penetration and
binding to ferric myoglobin. Biochemistry 40, 5728–5737 (2001)
7 Spectroscopy of Ferric Heme and Protoporphyrin IX Ions In Vacuo
137