NDLI: Fe-O2 bonding and oxyheme structure in myoglobin.

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Fe-O2 bonding and oxyheme structure in myoglobin.

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Fe-O2 bonding and oxyheme structure in myoglobin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Churg, A. K. Makinen, M. W. Glick, H. A.
Abstract	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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	5
Volume Number	75
Language	English
Publisher	National Academy of Sciences
Publisher Date	1978-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Heme Myoglobin Oxygen Animals Aplysia Chemical Phenomena Chemistry, Physical Metabolism Ligands Molecular Conformation Spectrophotometry, Atomic Structure-Activity Relationship Whales Comparative Study Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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