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99 related items for PubMed ID: 15036299
1. Structural quantitative information on the active sites of hemocyanins and related model compounds by the XAS approach: the role of multiple-scattering calculations. Borghi E, Solari PL. Micron; 2004; 35(1-2):81-6. PubMed ID: 15036299 [Abstract] [Full Text] [Related]
2. Multiple-scattering XAS calculations for the characterization of the binuclear (type 3) copper sites of hemocyanins and related model compounds. Borghi E, Solari PL. J Synchrotron Radiat; 2005 Jan; 12(Pt 1):102-10. PubMed ID: 15616373 [Abstract] [Full Text] [Related]
3. Comparison of the X-ray absorption properties of the binuclear active site of molluscan and arthropodan hemocyanins. Sabatucci A, Ascone I, Bubacco L, Beltramini M, Muro D, Salvato B. J Biol Inorg Chem; 2002 Jan; 7(1-2):120-8. PubMed ID: 11862548 [Abstract] [Full Text] [Related]
4. What are the structural features of the active site that define binuclear copper proteins function? Bubacco L, van Gastel M, Benfatto M, Tepper AW, Canters GW. Micron; 2004 Jan; 35(1-2):143-5. PubMed ID: 15036320 [Abstract] [Full Text] [Related]
5. Structural role of the copper ions in the dinuclear active site of Carcinus aestuarii hemocyanin. Gatto S, De Filippis V, Spinozzi F, Di Muro P, Bubacco L, Beltramini M. Micron; 2004 Jan; 35(1-2):43-4. PubMed ID: 15036286 [Abstract] [Full Text] [Related]
6. Model building of a molluscan hemocyanin from X-ray solution scattering. Mičetić I, Salvato B. Micron; 2004 Jan; 35(1-2):17-20. PubMed ID: 15036281 [Abstract] [Full Text] [Related]
7. Bayes-Turchin approach to XAS analysis. Rehr JJ, Kozdon J, Kas J, Krappe HJ, Rossner HH. J Synchrotron Radiat; 2005 Jan; 12(Pt 1):70-4. PubMed ID: 15616367 [Abstract] [Full Text] [Related]
8. Oxidized derivatives of Octopus vulgaris and Carcinus aestuarii hemocyanins at pH 7.5 and related models by x-ray absorption spectroscopy. Borghi E, Solari PL, Beltramini M, Bubacco L, Di Muro P, Salvato B. Biophys J; 2002 Jun; 82(6):3254-68. PubMed ID: 12023249 [Abstract] [Full Text] [Related]
9. Structure of hemocyanin subunit CaeSS2 of the crustacean Mediterranean crab Carcinus aestuarii. Dolashka-Angelova P, Dolashki A, Savvides SN, Hristova R, Van Beeumen J, Voelter W, Devreese B, Weser U, Di Muro P, Salvato B, Stevanovic S. J Biochem; 2005 Sep; 138(3):303-12. PubMed ID: 16169881 [Abstract] [Full Text] [Related]
10. Contribution of the copper ions in the dinuclear active site to the stability of Carcinus aestuarii hemocyanin. Spinozzi F, Gatto S, De Filippis V, Carsughi F, Di Muro P, Beltramini M. Arch Biochem Biophys; 2005 Jul 01; 439(1):42-52. PubMed ID: 15950169 [Abstract] [Full Text] [Related]
11. Modeling techniques for analysing conformational transitions in hemocyanins by small-angle scattering of X-rays and neutrons. Hartmann H, Müller T, Decker H. Micron; 2004 Jul 01; 35(1-2):11-3. PubMed ID: 15036279 [No Abstract] [Full Text] [Related]
12. Bio-mimicking galactose oxidase and hemocyanin, two dioxygen-processing copper proteins. Gamez P, Koval IA, Reedijk J. Dalton Trans; 2004 Dec 21; (24):4079-88. PubMed ID: 15573156 [Abstract] [Full Text] [Related]
13. Local structure investigation of the active site of the imidazolonepropionase from Bacillus subtilis by XANES spectroscopy and ab initio calculations. Yang F, Chu W, Yu M, Wang Y, Ma S, Dong Y, Wu Z. J Synchrotron Radiat; 2008 Mar 21; 15(Pt 2):129-33. PubMed ID: 18296777 [Abstract] [Full Text] [Related]
16. Structure and stability of arthropodan hemocyanin Limulus polyphemus. Dolashka-Angelova P, Dolashki A, Stevanovic S, Hristova R, Atanasov B, Nikolov P, Voelter W. Spectrochim Acta A Mol Biomol Spectrosc; 2005 Apr 21; 61(6):1207-17. PubMed ID: 15741123 [Abstract] [Full Text] [Related]
17. Skeletal Ru/Cu catalysts prepared from crystalline and quasicrystalline ternary alloy precursors: characterization by X-ray absorption spectroscopy and CO oxidation. Highfield J, Liu T, Loo YS, Grushko B, Borgna A. Phys Chem Chem Phys; 2009 Feb 28; 11(8):1196-208. PubMed ID: 19209363 [Abstract] [Full Text] [Related]
18. Integration of XAS and NMR techniques for the structure determination of metalloproteins. Examples from the study of copper transport proteins. Banci L, Bertini I, Mangani S. J Synchrotron Radiat; 2005 Jan 28; 12(Pt 1):94-7. PubMed ID: 15616371 [Abstract] [Full Text] [Related]
19. X-ray absorption spectroscopic study of the reduced hydroxylases of methane monooxygenase and toluene/o-xylene monooxygenase: differences in active site structure and effects of the coupling proteins MMOB and ToMOD. Rudd DJ, Sazinsky MH, Lippard SJ, Hedman B, Hodgson KO. Inorg Chem; 2005 Jun 27; 44(13):4546-54. PubMed ID: 15962961 [Abstract] [Full Text] [Related]
20. MXAN analysis of the XANES energy region of a mononuclear copper complex: applications to bioinorganic systems. Sarangi R, Benfatto M, Hayakawa K, Bubacco L, Solomon EI, Hodgson KO, Hedman B. Inorg Chem; 2005 Dec 26; 44(26):9652-9. PubMed ID: 16363833 [Abstract] [Full Text] [Related] Page: [Next] [New Search]