Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the  Paramecium caudatum  hemoglobin cases | Zendy

Martí Marcelo A. | Zendy; Capece Luciana | Zendy; Bikiel Damián E. | Zendy; Falcone Bruno | Zendy; Estrin Darío A | Zendy

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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.

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