His paper, we demonstrate by EXAFS analysis that 1F includes a FeFe distance of three.56 and consequently a almost linear FeOFe angle due to theNIHPA Author Manuscript NIHPA Author Manuscript NIHPA Author ManuscriptInorg Chem. Author manuscript; accessible in PMC 2014 April 01.Xue et al.Pageabsence of a hydrogen bond. The presence in the Hbond in 1OH could be accountable for attenuating the Hatom abstracting capability of 1OH. Even so the present DFT calculations comparing 1OH and 1F strongly suggest that the Hbond in 1OH doesn’t considerably adjust the electrophilicity of the reactive FeIV=O unit but rather increases the activation barrier for C bond cleavage by requiring the weakening with the Hbond in the course of HAT by the oxoiron(IV) moiety. This study as a result sheds light on how Nature could employ hydrogen bonding to modulate the reactivities of oxoiron(IV) intermediates within the active websites of many dioxygen activating iron enzymes.NIHPA Author Manuscript NIHPA Author Manuscript NIHPA Author ManuscriptSupplementary MaterialRefer to Net version on PubMed Central for supplementary material.AcknowledgmentsThe operate at Minnesota was supported by US National Institutes of Wellness via grant GM38767 to L.Q. and postdoctoral fellowship GM079839 to A.T.F. C.Y.G. gratefully acknowledges a grant from China Scholarship Council (CSC). C.Y.G., S.Y. and F.N. gratefully acknowledge monetary help by the German Science Foundation (DFG), the University of Bonn and the Max Planck Society. XAS information have been collected on beamline 73 in the Stanford Synchrotron Radiation Laboratory (SSRL), a national user facility operated by Stanford University on behalf in the U.Buy2-(4-Nitrophenyl)ethanol S.886779-69-7 Purity Division of Energy, Office of Basic Energy Sciences.PMID:23695992 The SSRL Structural Molecular Biology System is supported by the Department of Energy, Office of Biological and Environmental Study, and by the National Institutes of Wellness, National Center for Investigation Sources, and Biomedical Technologies System.
NIH Public AccessAuthor ManuscriptBiochemistry. Author manuscript; obtainable in PMC 2014 April 16.Published in final edited type as: Biochemistry. 2013 April 16; 52(15): 2556564. doi:10.1021/bi400146c.NIHPA Author Manuscript NIHPA Author Manuscript NIHPA Author ManuscriptMutational Effects on the Folding Dynamics of a Minimized HairpinMichele Scian, Irene Shu, Katherine A. Olsen, Khalil Hassam, and Niels H. Andersen Division of Chemistry, University of Washington, Seattle WAAbstractThe fold stabilities and folding dynamics of a series of mutants of a model hairpin, KTWNPATGKWTE (HP7), are reported. The parent program and also the corresponding DPATGK loop species show subs folding time constants. The mutational research revealed that ultrafast folding requires each some prestructuring on the loop and a favorable interaction in between the chain termini in the transition state. Inside the case of YYDPETGTWY, yet another subs folding species [Davis, C. M.; Xiao, S.; Raleigh, D. P.; Dyer, R. B. (2012) J. Am. Chem. Soc. 134, 144764482], a hydrophobic cluster provides the latter. Within the case of HP7, the Coulombic interaction involving the terminal NH3 and CO2 units delivers this; a Cterminal Glu to amidated Ala mutation results in a 5fold folding price retardation. The effects of mutations within the reversing loop indicate the balance involving loop flexibility (favoring quickly conformational browsing) and turnformation in the unfolded state is often a significant element in figuring out the folding dynamics. The AAAKX loops examined.
