Premium
Direct Evidence for a Hydrogen Bond to Bound Dioxygen in a Myoglobin/Hemoglobin Model System and in Cobalt Myoglobin by Pulse‐EPR Spectroscopy
Author(s) -
Dube Henry,
Kasumaj Besnik,
Calle Carlos,
Saito Makoto,
Jeschke Gunnar,
Diederich François
Publication year - 2008
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200705180
Subject(s) - myoglobin , chemistry , cobalt , hemeprotein , electron paramagnetic resonance , hydrogen bond , photochemistry , porphyrin , hemoglobin , heme , spectroscopy , inorganic chemistry , molecule , nuclear magnetic resonance , organic chemistry , enzyme , physics , quantum mechanics
Hydrogen bond revealed : In a cobalt(II) porphyrin complex which serves as a model for the dioxygen binding site of myoglobin (Mb) and hemoglobin, a distal hydrogen bond to the bound O 2 was identified and characterized by pulse ENDOR spectroscopy. A similar but stronger hydrogen bond was revealed with the same methods in natural Co‐Mb‐O 2 .