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- W1991430178 abstract "Neuroglobin, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O(2) supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. In the absence of exogenous ligands, neuroglobin displays a hexacoordinated heme. O(2) and CO bind to the heme iron, displacing the endogenous HisE7 heme distal ligand. Hexacoordinated human neuroglobin displays a classical globin fold adapted to host the reversible bis-histidyl heme complex and an elongated protein matrix cavity, held to facilitate O(2) diffusion to the heme. The neuroglobin structure suggests that the classical globin fold is endowed with striking adaptability, indicating that hemoglobin and myoglobin are just two examples within a wide and functionally diversified protein homology superfamily." @default.
- W1991430178 created "2016-06-24" @default.
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- W1991430178 date "2003-09-01" @default.
- W1991430178 modified "2023-10-12" @default.
- W1991430178 title "Human Brain Neuroglobin Structure Reveals a Distinct Mode of Controlling Oxygen Affinity" @default.
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- W1991430178 doi "https://doi.org/10.1016/s0969-2126(03)00166-7" @default.
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