NDLI: Coupling of the Distal H-bond Network to the Exogenous Ligand in Substrate-bound, Resting State Human Heme Oxygenase ‡

Content Provider	PubMed Central
Author	Peng, Dungeng Ogura, Hiroshi Zhu, Wenfeng Ma, Li-hua Evans, John P. Montellano, Paul R. Ortiz De Mar, Gerd N. La
Abstract	Mammalian heme oxygenase, HO, possesses catalytically implicated distal ordered water molecules within an extended H-bond network, with one of the ordered water molecules (#1) providing a bridge between the iron-coordinated ligand and the catalytically critical Asp140, that, in turn, serves as an acceptor for the Tyr58 OH H-bond. The degree of H-bonding by the ligated water molecule and the coupling of this water molecule to the H-bond network are of current interest and are herein investigated by 1H NMR. 2D NMR allowed sufficient assignments to provide both the H-bond strength and hyperfine shifts, the latter of which were used to quantify the magnetic anisotropy in both the ferric high-spin aquo and low-spin hydroxo complexes. The anisotropy in the aquo complex indicates that the H-bond donation to water #1 is marginally stronger than in a bacterial HO, while the anisotropy for the hydroxo complex reveals a conventional (dxz, dyz)1 ground state indicative of only moderate to weak H-bond acceptance by the ligated hydroxide. Mapping out the changes of the H-bond strengths in the network during the ligated water → hydroxide conversion by correcting for the effects of magnetic anisotropy, reveals a very substantial change in H-bond strength for Tyr58 OH, and lesser effects on nearby H-bonds. The effect of pH on the H-bonding network in human HO is much larger and transmitted much further from the iron than in a pathogenic bacterial HO. The implications for the HO mechanism of the H-bond of Tyr58 to Asp140 are discussed.
Related Links	http://dx.doi.org/10.1021/bi901216s
Ending Page	11242
Page Count	12
Starting Page	11231
File Format	PDF
ISSN	00062960
e-ISSN	15204995
Journal	Biochemistry
Issue Number	47
Volume Number	48
Language	English
Publisher Date	2009-12-01
Access Restriction	Open
Subject Keyword	Biochemistry Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biochemistry

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