TY - JOUR
T1 - HNO-Binding in Heme Proteins
T2 - Effects of Iron Oxidation State, Axial Ligand, and Protein Environment
AU - Khade, Rahul L.
AU - Yang, Yuwei
AU - Shi, Yelu
AU - Zhang, Yong
N1 - Publisher Copyright:
© 2016 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
PY - 2016/11/21
Y1 - 2016/11/21
N2 - HNO plays significant roles in many biological processes. Numerous heme proteins bind HNO, an important step for its biological functions. A systematic computational study was performed to provide the first detailed trends and origins of the effects of iron oxidation state, axial ligand, and protein environment on HNO binding. The results show that HNO binds much weaker with ferric porphyrins than corresponding ferrous systems, offering strong thermodynamic driving force for experimentally observed reductive nitrosylation. The axial ligand was found to influence HNO binding through its trans effect and charge donation effect. The protein environment significantly affects the HNO hydrogen bonding structures and properties. The predicted NMR and vibrational data are in excellent agreement with experiment. This broad range of results shall facilitate studies of HNO binding in many heme proteins, models, and related metalloproteins.
AB - HNO plays significant roles in many biological processes. Numerous heme proteins bind HNO, an important step for its biological functions. A systematic computational study was performed to provide the first detailed trends and origins of the effects of iron oxidation state, axial ligand, and protein environment on HNO binding. The results show that HNO binds much weaker with ferric porphyrins than corresponding ferrous systems, offering strong thermodynamic driving force for experimentally observed reductive nitrosylation. The axial ligand was found to influence HNO binding through its trans effect and charge donation effect. The protein environment significantly affects the HNO hydrogen bonding structures and properties. The predicted NMR and vibrational data are in excellent agreement with experiment. This broad range of results shall facilitate studies of HNO binding in many heme proteins, models, and related metalloproteins.
KW - bioinorganic chemistry
KW - density functional calculations
KW - heme proteins
KW - nitrogen oxides
KW - porphyrinoids
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U2 - 10.1002/anie.201608539
DO - 10.1002/anie.201608539
M3 - Article
C2 - 27797441
AN - SCOPUS:84995756485
SN - 1433-7851
VL - 55
SP - 15058
EP - 15061
JO - Angewandte Chemie - International Edition
JF - Angewandte Chemie - International Edition
IS - 48
ER -