http://www.cnr.it/ontology/cnr/individuo/prodotto/ID11578
Neuroglobin: enzymatic reduction and oxygen affinity. (Articolo in rivista)
- Type
- Label
- Neuroglobin: enzymatic reduction and oxygen affinity. (Articolo in rivista) (literal)
- Anno
- 2008-01-01T00:00:00+01:00 (literal)
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- Giuffrè A; Moschetti T; Vallone B; Brunori M. (literal)
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- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Department of Biochemical Sciences and CNR Institute of Molecular Biology and Pathology, Sapienza University of Rome, I-00185 Rome, Italy. (literal)
- Titolo
- Neuroglobin: enzymatic reduction and oxygen affinity. (literal)
- Abstract
- Neuroglobin (Ngb) is a hexacoordinate globin expressed in the nervous system of vertebrates, involved in neuroprotection. O2 equilibrium measurements on mouse Ngb yielded significantly different P50 values, ranging from ?2 torr to ?10 torr. By a kinetic approach minimizing the effects of protein autoxidation, we measured P50 = 2.2 torr at 20 ?C. As predicted from the structure, O2 binds to the Y44D Ngb mutant more quickly (k = 2.2 s?1 vs 0.15 s?1) and with slightly higher affinity (P50 = 1.3 torr) than wild-type. In addition, we introduced a novel reduction protocol for metNgb based on NADH:flavorubredoxin oxidoreductase (FlRd-red) from Escherichia coli, a candidate for the Ngb reducing activity recently identified in E. coli extracts. Interestingly, E. coli FlRd-red shares sequence similarity with the FAD-binding domain of the human apoptosis-inducing factor, a finding which may have unexpected significance with reference to the mechanism of neuroprotection by Ngb. (literal)
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