The Investigation of Coordinated Water in Paramagnetic Metalloproteins through Nuclear Magnetic Resonance Spectroscopy

作者: Ivano Bertini

DOI: 10.1080/02603598108078094

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摘要: Abstract Water molecules bound to metal ions in metalloproteins are rather common. If the ion is paramagnetic or if native diamagnetic can be substituted by a ion, then detection of water and investigation their properties may conveniently carried out through 1H, 2H. 17O NMR spectroscopy. The information which drawn from such an analysis here critically discussed with reference some typical metalloproteins. importance electronic correlation times, as related geometry chromophore high-spin cobalt(II) derivatives, stressed. acid-base coordinated also considered.

参考文章(51)
Dennis R. Burton, Paramagnetic Ions as Relaxation Probes in Biological Systems Springer, Dordrecht. pp. 151- 170 ,(1980) , 10.1007/978-94-009-9524-6_7
I. Bertini, C. Luchinat, A. Scozzafava, Some Structural Aspects of Carbonic Anhydrase Springer, Berlin, Heidelberg. pp. 151- 153 ,(1980) , 10.1007/978-3-642-67572-0_16
Albert S. Mildvan, Raj K. Gupta, [15] Nuclear relaxation measurements of the geometry of enzyme-bound substrates and analogs Methods in Enzymology. ,vol. 49, pp. 322- 359 ,(1978) , 10.1016/S0076-6879(78)49017-2
R Barker, N Boden, G Cayley, S C Charlton, R Henson, M C Holmes, I D Kelly, P F Knowles, Properties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methods Biochemical Journal. ,vol. 177, pp. 289- 302 ,(1979) , 10.1042/BJ1770289
Ivano Bertini, Giorgio Canti, Claudio Luchinat, Andrea Scozzafava, Spectroscopic investigation of copper(II) bovine carbonic anhydrase and its inhibitor derivatives Journal of the Chemical Society, Dalton Transactions. pp. 1269- 1273 ,(1978) , 10.1039/DT9780001269
James W. Wells, Stephen I. Kandel, Seymour H. Koenig, pH dependence of solvent proton relaxation in carbonic anhydrase solutions: paramagnetic and diamagnetic effects. Biochemistry. ,vol. 18, pp. 1989- 1995 ,(1979) , 10.1021/BI00577A022