TY - JOUR
T1 - HNO binding in a heme protein
T2 - Structures, spectroscopic properties, and stabilities
AU - Yang, Liu
AU - Ling, Yan
AU - Zhang, Yong
PY - 2011/9/7
Y1 - 2011/9/7
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=80052339896&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=80052339896&partnerID=8YFLogxK
U2 - 10.1021/ja204072j
DO - 10.1021/ja204072j
M3 - Article
C2 - 21834502
AN - SCOPUS:80052339896
SN - 0002-7863
VL - 133
SP - 13814
EP - 13817
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 35
ER -