http://www.cnr.it/ontology/cnr/individuo/prodotto/ID1230
Two distinct heme distal site states define Cerebratulus lacteus mini-hemoglobin oxygen affinity (Articolo in rivista)
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- Two distinct heme distal site states define Cerebratulus lacteus mini-hemoglobin oxygen affinity (Articolo in rivista) (literal)
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- 2006-01-01T00:00:00+01:00 (literal)
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Marti, MA; Bikiel, DE; Crespo, A; Nardini, M; Bolognesi, M; Estrin, DA (2006)
Two distinct heme distal site states define Cerebratulus lacteus mini-hemoglobin oxygen affinity
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Marti, MA; Bikiel, DE; Crespo, A; Nardini, M; Bolognesi, M; Estrin, DA (literal)
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- ISI Web of Science (WOS) (literal)
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- Univ Buenos Aires, Fac Ciencias Exactas & Nat, Analit & Quim Fis INQUIMAE,CONICET, Dept Quim Inorgan, Buenos Aires, DF, Argentina; Univ Milan, Dept Biomol Sci & Biotechnol, Milan, Italy; Univ Milan, CNR, INFM, Milan, Italy (literal)
- Titolo
- Two distinct heme distal site states define Cerebratulus lacteus mini-hemoglobin oxygen affinity (literal)
- Abstract
- The nerve tissue hemoglobin of Cerebratulus lacteus (CerHb) is the smallest naturally occurring known hemoglobin. Stabilization of the diatomic bound species (e.g., O-2) 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 O-2 affinity, related to hydrogen bond stabilization of the heme-bound O-2 resulting in a decrease of the ligand dissociation rates. In contrast to the above observations, the affinity of CerHb for O-2 is only moderate, and the rate of O-2 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 O-2 dissociation rates can only be explained through a dynamic equilibrium between high and low affinity states of the w.t. CerHb heme distal site. (literal)
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