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Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases
Author(s) -
Martí Marcelo A.,
Capece Luciana,
Bikiel Damián E.,
Falcone Bruno,
Estrin Darío A
Publication year - 2007
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21454
Subject(s) - leghemoglobin , hemoglobin , paramecium caudatum , chemistry , hemeprotein , heme , myoglobin , oxygen , paramecium , biophysics , biochemistry , biology , enzyme , root nodule , organic chemistry , nitrogen fixation , nitrogen
The binding of diatomic ligands, such as O 2 , NO, and CO, to heme proteins is a process intimately related with their function. In this work, we analyzed by means of a combination of classical Molecular Dynamics (MD) and Hybrid Quantum–Classical (QM/MM) techniques the existence of multiple conformations in the distal site of heme proteins and their influence on oxygen affinity regulation. We considered two representative examples: soybean leghemoglobin (Lba) and Paramecium caudatum truncated hemoglobin (PcHb). The results presented in this work provide a molecular interpretation for the kinetic, structural, and mutational data that cannot be obtained by assuming a single distal conformation. Proteins 2007. © 2007 Wiley‐Liss, Inc.