Axial coordination in nickel porphyrins and nickel-reconstituted heme proteins investigated by Raman-difference and transient-Raman spectroscopy

Conference · Mon Dec 31 23:00:00 EST 1984

OSTI ID:6457669

Shelnutt, J A; Alston, K; Findsen, E W; Ondrias, M R; Rifkind, J M

Nickel-porphyrin complexes and Ni(II)-reconstituted hemoglobin (/sup Ni/Hb) and myoglobin (/sup Ni/Mb) have been investigated using cw and transient resonance Raman spectroscopy. The state of axial coordination at the metal in these materials can be determined using the characteristic frequencies of the Raman marker lines arising from the porphyrin moiety. The Raman frequencies distinguish between 4- and 6-coordination of Ni-porphyrins in non-coordinating and coordinating solvents and give evidence of a novel 5-coordinate species in the reconstituted proteins. The existence of only one axial ligand in the proteins is supported by identification of the axial ligand-Ni stretching vibration by isotopic substitution. The frequency of the Ni-ligand mode is consistent with histidine as the fifth ligand. 64 refs., 4 figs.

• Research Organization: Sandia National Labs., Albuquerque, NM (USA); Benedict Coll., Columbia, SC (USA); New Mexico Univ., Albuquerque (USA); National Inst. on Aging, Baltimore, MD (USA)
• DOE Contract Number: AC04-76DP00789
• OSTI ID: 6457669
• Report Number(s): SAND-85-2256C; CONF-8511135-1; ON: DE86003455
• Country of Publication: United States
• Language: English

Related Subjects

09 BIOMASS FUELS
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550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
CARBOXYLIC ACIDS
COMPLEXES
DATA
EXPERIMENTAL DATA
GLOBIN
HEMOGLOBIN
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
INFORMATION
INFRARED SPECTRA
MOLECULAR STRUCTURE
MYOGLOBIN
NICKEL COMPLEXES
NUMERICAL DATA
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PIGMENTS
PORPHYRINS
PROTEINS
SPECTRA
TRANSITION ELEMENT COMPLEXES