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2VRY

Mouse Neuroglobin with heme iron in the reduced ferrous state

Summary for 2VRY
Entry DOI10.2210/pdb2vry/pdb
Related1Q1F 1W92
DescriptorNEUROGLOBIN, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (4 entities in total)
Functional Keywordsoxygen storage-transport complex, metal- binding, photoreduction, oxygen transport, iron, heme, ferrous, transport, neuroglobin, globin fold, heme protein, metal-binding, oxygen storage/transport
Biological sourceMUS MUSCULUS (MOUSE)
Total number of polymer chains1
Total formula weight18115.19
Authors
Arcovito, A.,Moschetti, T.,D'Angelo, P.,Mancini, G.,Vallone, B.,Brunori, M.,Della Longa, S. (deposition date: 2008-04-16, release date: 2008-05-06, Last modification date: 2023-12-13)
Primary citationArcovito, A.,Moschetti, T.,D'Angelo, P.,Mancini, G.,Vallone, B.,Brunori, M.,Della Longa, S.
An X-Ray Diffraction and X-Ray Absorption Spectroscopy Joint Study of Neuroglobin.
Arch.Biochem.Biophys., 475:7-, 2008
Cited by
PubMed Abstract: Neuroglobin (Ngb) is a member of the globin family expressed in the vertebrate brain, involved in neuroprotection. A combined approach of X-ray diffraction (XRD) on single crystal and X-ray absorption spectroscopy (XAS) in solution, allows to determine the oxidation state and the structure of the Fe-heme both in the bis-histidine and the CO-bound (NgbCO) states. The overall data demonstrate that under X-ray the iron is photoreduced fairly rapidly, and that the previously reported X-ray structure of ferric Ngb [B. Vallone, K. Nienhaus, M. Brunori, G.U. Nienhaus, Proteins 56 (2004) 85-92] very likely refers to a photoreduced species indistinguishable from the dithionite reduced protein. Results from the XAS analysis of NgbCO in solution are in good agreement with XRD data on the crystal. However prolonged X-ray exposure at 15K determines CO release. This preliminary result paves the way to experiments aimed at the characterization of pentacoordinate ferrous Ngb, the only species competent in binding external ligands such as O2, CO or NO.
PubMed: 18406335
DOI: 10.1016/J.ABB.2008.03.026
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.87 Å)
Structure validation

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