Artículo

Martí, M.A.; Bikiel, D.E.; Crespo, A.; Nardini, M.; Bolognesi, M.; Estrin, D.A. "Two distinct heme distal site states define Cerebratulus lacteus mini-hemoglobin oxygen affinity" (2006) Proteins: Structure, Function and Genetics. 62(3):641-648
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Abstract:

The nerve tissue hemoglobin of Cerebratulus lacteus (CerHb) is the smallest naturally occurring known hemoglobin. Stabilization of the diatomic bound, species (e.g., O2) is achieved through a network of hydrogen bonds based on three key residues TyrB10, GlnE7, and ThrE11. The first two residues are typically associated in hemoglobins with enhanced O2 affinity, related to hydrogen bond stabilization of the heme-bound O2 resulting in a decrease of the ligand dissociation rates. In contrast to the above observations, the affinity of CerHb for O2 is only moderate, and the rate of O2 dissociation is unexpectedly high. To gain insight on the diverse molecular mechanisms controlling ligand affinities, we have analyzed w.t. CerHb and its ThrE11→Val mutant by means of joint molecular dynamics and quantum mechanics simulation techniques, complementing recent site-directed mutagenesis experiments. Our results suggest that the observed O2 dissociation rates can only be explained through a dynamic equilibrium between high and low affinity states of the w.t. CerHb heme distal site. © 2005 Wiley-Liss, Inc.

Registro:

Documento: Artículo
Título:Two distinct heme distal site states define Cerebratulus lacteus mini-hemoglobin oxygen affinity
Autor:Martí, M.A.; Bikiel, D.E.; Crespo, A.; Nardini, M.; Bolognesi, M.; Estrin, D.A.
Filiación:Departamento de Quimica Inorgnica, Analitica y Quimica Fisica/INQUIMAE-CONICET, Universidad de Buenos Aires, Ciudad Universitaria, Buenos Aires (C1428EHA), Argentina
Department of Biomolecular Sciences and Biotechnology, CNR-INFM, University of Milano, Milano, Italy
Department of Biomolecular Sciences and Biotechnology, CNR-INFM, University of Milano, Via Celoria, 26, I-20131 Milano, Italy
Palabras clave:Computer simulation; Density functional theory; Hemoglobin; Molecular dynamics; Myoglobin; Neural hemoglobin; Quantum mechanical-molecular mechanical (QM-MM); carbon monoxide; heme; hemoglobin; oxygen; Aplysia; article; Cerebratulus lacteus; computer simulation; density functional theory; dissociation constant; energy transfer; enzyme active site; geometry; hydrogen bond; molecular dynamics; nervous tissue; nonhuman; oxygen affinity; priority journal; quantum mechanics; site directed mutagenesis; Amino Acid Substitution; Animals; Annelida; Binding Sites; Heme; Hemoglobins; Humans; Hydrogen Bonding; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Oxyhemoglobins; Protein Structure, Secondary; Recombinant Proteins; Aplysia; Cerebratulus lacteus
Año:2006
Volumen:62
Número:3
Página de inicio:641
Página de fin:648
DOI: http://dx.doi.org/10.1002/prot.20822
Título revista:Proteins: Structure, Function and Genetics
Título revista abreviado:Proteins Struct. Funct. Genet.
ISSN:08873585
CODEN:PSFGE
CAS:carbon monoxide, 630-08-0; heme, 14875-96-8; hemoglobin, 9008-02-0; oxygen, 7782-44-7; Heme, 14875-96-8; Hemoglobins; Oxyhemoglobins; Recombinant Proteins
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08873585_v62_n3_p641_Marti

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Citas:

---------- APA ----------
Martí, M.A., Bikiel, D.E., Crespo, A., Nardini, M., Bolognesi, M. & Estrin, D.A. (2006) . Two distinct heme distal site states define Cerebratulus lacteus mini-hemoglobin oxygen affinity. Proteins: Structure, Function and Genetics, 62(3), 641-648.
http://dx.doi.org/10.1002/prot.20822
---------- CHICAGO ----------
Martí, M.A., Bikiel, D.E., Crespo, A., Nardini, M., Bolognesi, M., Estrin, D.A. "Two distinct heme distal site states define Cerebratulus lacteus mini-hemoglobin oxygen affinity" . Proteins: Structure, Function and Genetics 62, no. 3 (2006) : 641-648.
http://dx.doi.org/10.1002/prot.20822
---------- MLA ----------
Martí, M.A., Bikiel, D.E., Crespo, A., Nardini, M., Bolognesi, M., Estrin, D.A. "Two distinct heme distal site states define Cerebratulus lacteus mini-hemoglobin oxygen affinity" . Proteins: Structure, Function and Genetics, vol. 62, no. 3, 2006, pp. 641-648.
http://dx.doi.org/10.1002/prot.20822
---------- VANCOUVER ----------
Martí, M.A., Bikiel, D.E., Crespo, A., Nardini, M., Bolognesi, M., Estrin, D.A. Two distinct heme distal site states define Cerebratulus lacteus mini-hemoglobin oxygen affinity. Proteins Struct. Funct. Genet. 2006;62(3):641-648.
http://dx.doi.org/10.1002/prot.20822