Title : Distal Histidine Modulates the Unusual O-Binding of Nitrite to Myoglobin: Evidence from the Quantum Chemical Analysis of EPR Parameters.

Pub. Date : 2015 Aug 3

PMID : 26172912






5 Functional Relationships(s)
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1 Distal Histidine Modulates the Unusual O-Binding of Nitrite to Myoglobin: Evidence from the Quantum Chemical Analysis of EPR Parameters. Nitrites myoglobin Homo sapiens
2 In contrast to the commonly found N-binding motif of nitrite to iron in synthetic models, the less commonly observed O-binding of nitrite to myoglobin ( Copeland , D. M. ; Soares , A. S. ; West , A. H. ; Richter-Addo , G. B. J. Inorg. Nitrites myoglobin Homo sapiens
3 Given to the very similar active sites, there exists a controversy within the two powerful experimental techniques in identifying the coordination motif of nitrite to myoglobin, which is central to understanding the denitrification mechanism. Nitrites myoglobin Homo sapiens
4 Herein, we report the computation of spin Hamiltonian EPR parameters of different linkage isomers of nitrite bound myoglobin using wave function based "ab initio" and density functional theories to shed light on the binding motif of nitrite to ferric iron. Nitrites myoglobin Homo sapiens
5 Herein, we report the computation of spin Hamiltonian EPR parameters of different linkage isomers of nitrite bound myoglobin using wave function based "ab initio" and density functional theories to shed light on the binding motif of nitrite to ferric iron. Nitrites myoglobin Homo sapiens