14N quadrupole resonance in polyglycine

Blinc, R.; Mali, M.; Osredkar, R.; Seliger, J.; Ehrenberg, L.

doi:10.1016/0009-2614(74)80041-2

Cited by 24 publications

(16 citation statements)

References 2 publications

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“…6). The values for k and h found in this earlier work were found to be similar to those found in NQR studies of the peptide nitrogens in small di-and tripeptides 69,70 and to the reported cases of ESEEM data arising from the modulation of an amide nitrogen of the peptide backbone in respiratory and in photosynthetic protein complexes. [71][72][73] It was noted at that time that no histidine nitrogen, whose quadrupolar parameters have been well characterised in other quinone binding sites (e.g.…”

Section: Epr Results and Discussionsupporting

confidence: 87%

Elucidating mechanisms in haemcopperoxidases: The high-affinity Q_Hbinding site in quinol oxidase as studied by DONUT-HYSCOREspectroscopy and density functional theory

et al. 2011

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Section: Epr Results and Discussionsupporting

confidence: 87%

Elucidating mechanisms in haemcopperoxidases: The high-affinity Q_Hbinding site in quinol oxidase as studied by DONUT-HYSCOREspectroscopy and density functional theory

et al. 2011

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“…These three frequencies allow one to determine K ϭ 0.87 MHz and ϭ 0.34. The value of the quadrupole coupling constant K is close to the typical values ϳ0.75-0.85 MHz previously reported for peptide nitrogens (43)(44)(45)(46)(47). Calculation of the double-quantum transition for this nitrogen, with A ϭ 0.7 MHz and the nuclear quadrupole interaction parameters found, gives a value 3.4 MHz, consistent with the frequency observed in three-pulse S-band spectrum at g z (Fig.…”

Section: Assignment Of the Frequencies In S-band Spectra-linessupporting

confidence: 88%

“…The amide nitrogen in free peptides, such as in metal complexes of diglycine, which H-bond to the inorganic sulfur atoms of iron-sulfur clusters (43)(44)(45)(46)(47)(48), has a narrow range of quadrupole coupling constants, K ϭ 0.75-0.85 MHz, determined by the electronic structure and the geometry of the planar peptide group. This coupling constant is only slightly perturbed by hydrogen bonding, which has been confirmed by calculations of the quadrupole coupling tensor (46,50,51).…”

Section: Assignment Of the Frequencies In S-band Spectra-linesmentioning

confidence: 99%

Identification of Hydrogen Bonds to the Rieske Cluster through the Weakly Coupled Nitrogens Detected by Electron Spin Echo Envelope Modulation Spectroscopy

Dikanov

Kolling

Endeward

et al. 2006

Journal of Biological Chemistry

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Proteins containing Rieske-type [2Fe-2S] clusters with two histidyl and two cysteinyl ligands play important roles in many biological electron transfer reactions such as aerobic respiration, photosynthesis, and biodegradation of various alkene and aromatic compounds. The distinct biological functions of this protein family are in part associated with the cluster redox potential and the pK of the oxidized form, which are roughly correlated with the number of hydrogen bonds from protein side chains and the peptide backbone to the cluster and its immediate ligands (1-6).In the cytochrome bc 1 /b 6f family, a Rieske iron-sulfur protein (ISP) 4 is a constituent of the high potential electron transfer chain that accepts the first electron in the bifurcated reaction at the ubihydroquinone (quinol, QH 2 ) oxidizing Q o site. In the catalytic mechanism at the Q o site, the redox reaction involves extraction of both an electron and a proton from the bound quinol and their transfer to the ISP through a short pathway that includes the ISP His-161 ring and the H-bond between N ⑀ and the -OH of the quinol substrate (7). It has been proposed that the electron transfer is gated by the low probability of finding the H-atom of the H-bond in the kinetically favorable position, determined by the pK difference between the quinol and the oxidized ISP (ISP ox ) (reviewed in Refs. 5 and 6). The pK on ISP ox is contributed by one of the cluster ligands, His-161 in bovine numbering, and is associated with H ϩ dissociation from the N ⑀ involved in the H-bond. The gating accounts for the fact that this first electron transfer is slower by more than 3 orders of magnitude than would be expected from the short distance (ϳ7 Å) involved (6, 7). The first electron transfer is the ratedetermining step in quinol oxidation under conditions of substrate saturation. Rate determination at this reaction is demonstrated by the fact that the overall rate depends on its driving force in a classical Marcus fashion, as shown through use of mutants of the ISP with modified redox potential (6 -13). Briefly, the driving force, ⌬G o , for the first electron transfer is determined by the redox potential difference between the donor (SQ/QH 2 ) and acceptor (ISP ox /ISPH) couples. Assuming that mutations in the ISP do not change E m (SQ/QH 2 ), a change in * This work was supported by National Institutes of Health Grants GM 35438 (to A. R. C.) and GM 62954 (to S. A. D.), Fogarty Grant PHS 1 RO3 TW 01495 (to A. R. C. and R. I. S.), and National Institutes of Health/National Center for Research Resources Grant S10-RR15878 for instrumentation. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. 1 To whom correspondence may be addressed. E-mail: dikanov@uiuc.edu. 2 Present address: Dept. of Chemistry, Princeton University, Princeton, NJ 08540. 3 To whom correspondence may be addressed. E-mail:...

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“…This analysis assumes that the orientation of the tensor is the same as in non-distorted peptide planes and this may introduce errors in the constants determined. For the second less-distorted plane the values e *iQ/h ~ 3'°S ± 0 -I 3 a n d V = o-81 ±0-19 were found which are in good agreement with the constants for poly-glycine (Blinc et al, 1974) and the second amide nitrogen in Gly-Gly-Gly (Edmonds & Speight, 1971).…”

Section: Experimental Example Of a Single Crystal Of L-ala-gly-gly Ussupporting

confidence: 75%

Protein structure by solid-state NMR spectroscopy

Opella

Stewart

Valentine

1987

Quart. Rev. Biophys.

181

134

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The three-dimensional structures of proteins are among the most valuable contributions of biophysics to the understanding of biological systems (Dickerson & Geis, 1969; Creighton, 1983). Protein structures are utilized in the description and interpretation of a wide variety of biological phenomena, including genetic regulation, enzyme mechanisms, antibody recognition, cellular energetics, and macroscopic mechanical and structural properties of molecular assemblies. Virtually all of the information currently available about the structures of proteins at atomic resolution has been obtained from diffraction studies of single crystals of proteins (Wyckoff et al, 1985). However, recently developed NMR methods are capable of determining the structures of proteins and are now being applied to a variety of systems, including proteins in solution and other non-crystalline environments that are not amenable for X-ray diffraction studies. Solid-state NMR methods are useful for proteins that undergo limited overall reorientation by virtue of their being in the crystalline solid state or integral parts of supramolecular structures that do not reorient rapidly in solution. For reviews of applications of solid-state NMR spectroscopy to biological systems see Torchia and VanderHart (1979), Griffin (1981), Oldfield et al. (1982), Opella (1982), Torchia (1982), Gauesh (1984), Torchia (1984) and Opella (1986). This review describes how solid-state NMR can be used to obtain structural information about proteins. Methods applicable to samples with macroscopic orientation are emphasized.

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14N quadrupole resonance in polyglycine

Cited by 24 publications

References 2 publications

Elucidating mechanisms in haemcopperoxidases: The high-affinity Q_Hbinding site in quinol oxidase as studied by DONUT-HYSCOREspectroscopy and density functional theory

Elucidating mechanisms in haemcopperoxidases: The high-affinity Q_Hbinding site in quinol oxidase as studied by DONUT-HYSCOREspectroscopy and density functional theory

Identification of Hydrogen Bonds to the Rieske Cluster through the Weakly Coupled Nitrogens Detected by Electron Spin Echo Envelope Modulation Spectroscopy

Protein structure by solid-state NMR spectroscopy

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14N quadrupole resonance in polyglycine

Cited by 24 publications

References 2 publications

Elucidating mechanisms in haemcopperoxidases: The high-affinity QHbinding site in quinol oxidase as studied by DONUT-HYSCOREspectroscopy and density functional theory

Elucidating mechanisms in haemcopperoxidases: The high-affinity QHbinding site in quinol oxidase as studied by DONUT-HYSCOREspectroscopy and density functional theory

Identification of Hydrogen Bonds to the Rieske Cluster through the Weakly Coupled Nitrogens Detected by Electron Spin Echo Envelope Modulation Spectroscopy

Protein structure by solid-state NMR spectroscopy

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Elucidating mechanisms in haemcopperoxidases: The high-affinity Q_Hbinding site in quinol oxidase as studied by DONUT-HYSCOREspectroscopy and density functional theory

Elucidating mechanisms in haemcopperoxidases: The high-affinity Q_Hbinding site in quinol oxidase as studied by DONUT-HYSCOREspectroscopy and density functional theory