Open AccessFe-O2 bonding and oxyheme structure in myoglobin.
Author(s) -
Marvin W. Makinen,
Antonie K. Churg,
Harold A. Glick
Publication year - 1978
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.75.5.2291
Subject(s) - myoglobin , ligand (biochemistry) , crystallography , chemistry , heme , electronic structure , atomic orbital , coordination geometry , absorption spectroscopy , ground state , atomic physics , computational chemistry , molecule , hydrogen bond , physics , electron , biochemistry , receptor , organic chemistry , quantum mechanics , enzyme
In the polarized electronic absorption spectrum of oxymyoglobin in single crystals, charge-transfer states involving orbitals of the iron and dioxygen ligand are defined as probes of oxyheme orbital structure and coordination geometry. The spectrum of sperm whale oxymyoglobin is diagnostic of a bent (formula: see text) oxheme coordination geometry with totally spin-paired, ground-state electronic configurations of the iron and of the dioxygen ligand. In contrast, Aplysia myoglobin is distinguishably different in oxyheme structure, indicating that the geometry of Fe-O2 bonding in heme proteins can be altered by the protein environment.