Direct Evidence for a Hydrogen Bond to Bound Dioxygen in a Myoglobin/Hemoglobin Model System and in Cobalt Myoglobin by Pulse‐EPR Spectroscopy | Zendy

Dube Henry | Zendy; Kasumaj Besnik | Zendy; Calle Carlos | Zendy; Saito Makoto | Zendy; Jeschke Gunnar | Zendy; Diederich François | Zendy

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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 .

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