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HNO Binding in a Heme Protein: Structures, Spectroscopic Properties, and Stabilities

[Image: see text] 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...

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Detalles Bibliográficos
Autores principales: Yang, Liu, Ling, Yan, Zhang, Yong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2011
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3164212/
https://www.ncbi.nlm.nih.gov/pubmed/21834502
http://dx.doi.org/10.1021/ja204072j
Descripción
Sumario:[Image: see text] 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 O(2). These results shall facilitate investigations of HNO bindings in other heme proteins.