HNO Binding in a Heme Protein: Structures, Spectroscopic Properties, and Stabilities
Document Type
Article
Publication Date
9-1-2011
Department
Chemistry and Biochemistry
School
Mathematics and Natural Sciences
Abstract
HNO can interact with numerous heme proteins, but atomic level structures are largely unknown. In this work, various structural models for the first stable HNO heme protein complex, MbHNO (Mb, myoglobin), were examined by quantum chemical calculations. This investigation led to the discovery of two novel structural models that can excellently reproduce numerous experimental spectroscopic properties. They are also the first atomic level structures that can account for the experimentally observed high stabilities. These two models involve two distal His conformations as reported previously for MbCNR and MbNO. However, a unique dual hydrogen bonding feature of the HNO binding was not reported before in heme protein complexes with other small molecules such as CO, NO, and O2. These results shall facilitate investigations of HNO bindings in other heme proteins.
Publication Title
Journal of the American Chemical Society
Volume
133
Issue
35
First Page
13814
Last Page
13817
Recommended Citation
Yang, L.,
Ling, Y.,
Zhang, Y.
(2011). HNO Binding in a Heme Protein: Structures, Spectroscopic Properties, and Stabilities. Journal of the American Chemical Society, 133(35), 13814-13817.
Available at: https://aquila.usm.edu/fac_pubs/8884