NDLI: Ligand binding and protein dynamics in neuroglobin

Content Provider	PubMed Central
Author	Kriegl, Jan M. Bhattacharyya, Aninda J. Nienhaus, Karin Deng, Pengchi Minkow, Oleksandr Nienhaus, G. Ulrich
Copyright Year	2002
Abstract	Neuroglobin (Ngb) is a recently discovered protein in vertebrate brain tissue that belongs to the globin family of proteins. It has been implicated in the neuronal response to hypoxia or ischemia, although its physiological role has been hitherto unknown. Ngb is hexacoordinate in the ferrous deoxy form under physiological conditions. To bind exogenous ligands like O2 and CO, the His E7 endogenous ligand is displaced from the sixth coordination. By using infrared spectroscopy and nanosecond time-resolved visible spectroscopy, we have investigated the ligand-binding reaction over a wide temperature range (3–353 K). Multiple, intrinsically heterogeneous distal heme pocket conformations exist in NgbCO. Photolysis at cryogenic temperatures creates a five-coordinate deoxy species with very low geminate-rebinding barriers. The photodissociated CO is observed to migrate within the distal heme pocket even at 20 K. Flash photolysis near physiological temperature (275–353 K) exhibits four sequential kinetic features: (i) geminate rebinding (t < 1 μs); (ii) extremely fast bimolecular exogenous ligand binding (10 μs < t < 1 ms) with a nontrivial temperature dependence; (iii) endogenous ligand binding (100 μs < t < 10 ms), which can be studied by using flash photolysis on deoxy Ngb; and (iv) displacement of the endogenous by the exogenous ligand (10 ms < t < 10 ks). All four processes are markedly nonexponential, suggesting that Ngb fluctuates among different conformations on surprisingly long time scales.
Related Links	http://dx.doi.org/10.1073/pnas.082244399
Starting Page	7992
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	12
Volume Number	99
Language	English
Publisher	The National Academy of Sciences
Publisher Date	2002-06-11
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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