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1.
Qian Li Chuanyu Li Harry K. Mahtani Jian Du Aashka R. Patel Jack R. Lancaster Jr. 《The Journal of biological chemistry》2014,289(29):19917-19927
Dinitrosyliron complexes (DNIC) have been found in a variety of pathological settings associated with •NO. However, the iron source of cellular DNIC is unknown. Previous studies on this question using prolonged •NO exposure could be misleading due to the movement of intracellular iron among different sources. We here report that brief •NO exposure results in only barely detectable DNIC, but levels increase dramatically after 1–2 h of anoxia. This increase is similar quantitatively and temporally with increases in the chelatable iron, and brief •NO treatment prevents detection of this anoxia-induced increased chelatable iron by deferoxamine. DNIC formation is so rapid that it is limited by the availability of •NO and chelatable iron. We utilize this ability to selectively manipulate cellular chelatable iron levels and provide evidence for two cellular functions of endogenous DNIC formation, protection against anoxia-induced reactive oxygen chemistry from the Fenton reaction and formation by transnitrosation of protein nitrosothiols (RSNO). The levels of RSNO under these high chelatable iron levels are comparable with DNIC levels and suggest that under these conditions, both DNIC and RSNO are the most abundant cellular adducts of •NO. 相似文献
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3.
Julie D. Forman-Kaya G. Marius Clore Stephen J. Stahl Angela M. Gronenborn 《Journal of biomolecular NMR》1992,2(5):431-445
Summary The complete assignment of1H and15N backbone resonances and near-complete1H side-chain resonance assignments have been obtained for the reduced form of a mutant of human thioredoxin (105 residues) in which the three non-active site cysteines have been substituted by alanines: C62A, C69A, C73A. The assignments were made primarily on the basis of three-dimensional.15N-separated nuclear Overhauser and Hartmann-Hahn spectroscopy, in conjunction with two-dimensional homonuclear and heteronuclear correlation experiments. Based on comparisons of short-range and interstrand nuclear Overhauser effects, patterns of amide exchange, and chemical-shift differences, the structure appears essentially unchanged from that of the previously determined solution structure of the native protein [Forman-Kay. J.D. et al. (1991)Biochemistry, 30, 2685–2698). An assay for thioredoxin shows that the C62A, C69A, C73A mutant retains activity. The assignment of the spectrum for this mutant of human thioredoxin constitutes the basis for future studies aimed at comparing the details of the active-site conformation in the reduced and oxidized forms of the protein. 相似文献
4.
Summary A 3D1H–15N–13C triple resonance experiment is presented that contains exclusively cross peaks between the1HN and15N nuclei of one residue with the H of the preceding residue. The pulse sequence, designed to minimize the time coherence, is transverse on nuclei with short T2 values. The experiment consists of coherence transfers via one-bond couplings from the HN via N, CO, C to the H and back to the HN for detection; it is called HN(COCA)HA. The experiment was tested on uniformly15N- and13C-enriched T4 lysozyme. 相似文献
5.
The Optically Detected Magnetic Resonance spectrum of lysozyme has been shown to consist of a multiplet of narrow components, at -1565 MHz, 1585 MHz, and 1620 MHz. The 1585 MHz component is the strongest feature of the spectrum. This is consistent with earlier reports which apparently resolved only this principal component in lysozyme. The linewidths reported here are the narrowest ever reported for tryptophan in proteins. Using Microwave-Induced Phosphorescence techniques, the dominant 1585 MHz line is seen to be coupled to a "narrow" phosphorescence emission component at about 4134A. This component has a bandwidth of about 25A compared to 42A for the normal O-O band for tryptophan in lysozyme. 相似文献
6.
Summary NMR View is a computer program designed for the visualization and analysis of NMR data. It allows the user to interact with a practically unlimited number of 2D, 3D and 4D NMR data files. Any number of spectral windows can be displayed on the screen in any size and location. Automatic peak picking and facilitated peak analysis features are included to aid in the assignment of complex NMR spectra. NMR View provides structure analysis features and data transfer to and from structure generation programs, allowing for a tight coupling between spectral analysis and structure generation. Visual correlation between structures and spectra can be done with the Molecular Data Viewer, a molecular graphics program with bidirectional communication to NMR View. The user interface can be customized and a command language is provided to allow for the automation of various tasks.Inquiries concerning the availability of NMR View and the Molecular Data Viewer should be sent via email to johnsonb@merck.com or to Bruce A. Johnson, Merck Research Laboratories, RY80Y-103, P.O. Box 2000, Rahway, NJ 07065, U.S.A. 相似文献
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用共振拉曼和紫外-可见吸收光谱研究了水溶金属卟啉4-N-乙酸乙酯基-吡啶基铜卟啉和镍卟啉[简称Cu(NEAE)和Ni(NEAE)]及4-N-乙腈基-吡啶基铜卟啉[简称Cu(NACN)]与小牛胸腺DNA的相互作用。分析表明Cu(NEAE)、Ni(NEAE)和Cu(NACN)分别以外部键联、部分插入和沟槽方式与DNA作用;卟啉插入DNA时吡啶基团向卟啉环平面转动但不可能转成与之共面;而以非插入方式作用时吡啶基团会向垂直于或者平行于卟啉环平面转动。吡啶取代基的大小和空间位阻是影响相互作用方式的关键因素之一。 相似文献
9.
Robin T. Clowes Wayne Boucher Colin H. Hardman Peter J. Domaille Ernest D. Laue 《Journal of biomolecular NMR》1993,3(3):349-354
Summary We recently proposed a novel four-dimensional (4D) NMR strategy for the assignment of backbone nuclei in spectra of 13C/15N-labelled proteins (Boucher et al. (1992) J. Am. Chem. Soc., 114, 2262–2264 and J. Biomol. NMR, 2, 631–637). In this paper we extend this approach with a new constant time 4D HCC(CO)NNH experiment that also correlates the chemical shifts of the aliphatic sidechain (1H and 13C) and backbone (1H, 13C and 15N) nuclei. It separates the sidechain resonances, which may heavily overlap in spectra of proteins with large numbers of similar residues, according to the backbone nitrogen and amide proton chemical shifts. When used in conjunction with a 4D HCANNH or HNCAHA experiment it allows, in principle, complete assignment of aliphatic sidechain and backbone resonances with just two 4D NMR experiments. 相似文献
10.
Sjaak Peelen Sybren S. Wijmenga Paul J. A. Erbel Robert L. Robson Robert R. Eady Jacques Vervoort 《Journal of biomolecular NMR》1996,7(4):315-330
Summary The 1H, 15N and 13C backbone and 1H and 13C beta resonance assignments of the long-chain flavodoxin from Azotobacter chroococcum (the 20-kDa nifF product, flavodoxin-2) in its oxidized form were made at pH 6.5 and 30°C using heteronuclear multidimensional NMR spectroscopy. Analysis of the NOE connectivities, together with amide exchange rates, 3JHnH coupling constants and secondary chemical shifts, provided extensive solution secondary structure information. The secondary structure consists of a five-stranded parallel -sheet and five -helices. One of the outer regions of the -sheet shows no regular extended conformation, whereas the outer strand 4/6 is interrupted by a loop, which is typically observed in long-chain flavodoxins. Two of the five -helices are nonregular at the N-terminus of the helix. Loop regions close to the FMN are identified. Negatively charged amino acid residues are found to be mainly clustered around the FMN, whereas a cluster of positively charged residues is located in one of the -helices. Titration of the flavodoxin with the Fe protein of the A. chroococcum nitrogenase enzyme complex revealed that residues Asn11, Ser68 and Asn72 are involved in complex formation between the flavodoxin and Fe protein. The interaction between the flavodoxin and the Fe protein is influenced by MgADP and is of electrostatic nature.Abbreviations SQ
semiquinone
- FMN
riboflavin 5-monophosphate; nif, nitrogen fixation
- TSP
3-(trimethylsilyl)propionate sodium salt
- DSS
2,2-dimethyl-2-silapentane-5-sulfonate sodium salt
Supplementary Material is available on request, comprising a Materials and Methods section for the expression and purification of the A. chroococcum flavodoxin, a Table S1 containing the parameters of the titration of A. chroococcum flavodoxin with the Fe protein, and a Table S2 containing the 15N, HN, 13C, 1H, 13C, 1H and 13CO chemical shifts.To whom correspondence should be addressed. 相似文献