These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
2. Three-dimensional structure of the reduced C77S mutant of the Chromatium vinosum high-potential iron-sulfur protein through nuclear magnetic resonance: comparison with the solution structure of the wild-type protein. Bentrop D; Bertini I; Capozzi F; Dikiy A; Eltis L; Luchinat C Biochemistry; 1996 May; 35(18):5928-36. PubMed ID: 8639555 [TBL] [Abstract][Full Text] [Related]
3. 15N resonance assignments of oxidized and reduced Chromatium vinosum high-potential iron protein. Li D; Cottrell CE; Cowan JA J Protein Chem; 1995 Apr; 14(3):115-26. PubMed ID: 7576079 [TBL] [Abstract][Full Text] [Related]
4. Sequence-specific assignments of the 1H nuclear magnetic resonance spectra of reduced high-potential ferredoxin (HiPIP) from Chromatium vinosum. Gaillard J; Albrand JP; Moulis JM; Wemmer DE Biochemistry; 1992 Jun; 31(24):5632-9. PubMed ID: 1610810 [TBL] [Abstract][Full Text] [Related]
5. The electronic structure of [Fe4S4]3+ clusters in proteins. An investigation of the oxidized high-potential iron-sulfur protein II from Ectothiorhodospira vacuolata. Banci L; Bertini I; Ciurli S; Ferretti S; Luchinat C; Piccioli M Biochemistry; 1993 Sep; 32(36):9387-97. PubMed ID: 8396428 [TBL] [Abstract][Full Text] [Related]
6. Molecular modeling studies on the proposed NaCl-induced dimerization of Chromatium vinosum high-potential iron protein. Adman ET; Mather MW; Fee JA Biochim Biophys Acta; 1993 Apr; 1142(1-2):93-8. PubMed ID: 8457586 [TBL] [Abstract][Full Text] [Related]
7. The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR. Banci L; Bertini I; Dikiy A; Kastrau DH; Luchinat C; Sompornpisut P Biochemistry; 1995 Jan; 34(1):206-19. PubMed ID: 7819198 [TBL] [Abstract][Full Text] [Related]
8. Two-dimensional NMR investigation of iron-sulfur cluster electronic and molecular structure of oxidized Clostridium pasteurianum ferredoxin. Interpretability of contact shifts in terms of cysteine orientation. Busse SC; La Mar GN; Howard JB J Biol Chem; 1991 Dec; 266(35):23714-23. PubMed ID: 1748648 [TBL] [Abstract][Full Text] [Related]
9. Comparative nuclear magnetic resonance studies of high potential iron-sulfur proteins from Chromatium vinosum and Rhodopseudomonas gelatinosa. Additional hyperfine shifted resonances and pH-dependent structural perturbations. Nettesheim DG; Meyer TE; Feinberg BA; Otvos JD J Biol Chem; 1983 Jul; 258(13):8235-9. PubMed ID: 6863288 [TBL] [Abstract][Full Text] [Related]
10. Three-dimensional solution structure of the oxidized high potential iron-sulfur protein from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced species. Bertini I; Dikiy A; Kastrau DH; Luchinat C; Sompornpisut P Biochemistry; 1995 Aug; 34(31):9851-8. PubMed ID: 7632685 [TBL] [Abstract][Full Text] [Related]
11. 1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nuclear Overhauser effect measurements. Cowan JA; Sola M Biochemistry; 1990 Jun; 29(23):5633-7. PubMed ID: 2386791 [TBL] [Abstract][Full Text] [Related]
12. 1H nuclear-magnetic-resonance investigation of oxidized Fe4S4 ferredoxin from Thermotoga maritima. Hyperfine-shifted resonances, sequence-specific assignments and secondary structure. Wildegger G; Bentrop D; Ejchart A; Alber M; Hage A; Sterner R; Rösch P Eur J Biochem; 1995 May; 229(3):658-68. PubMed ID: 7758460 [TBL] [Abstract][Full Text] [Related]
13. Detection and classification of hyperfine-shifted 1H, 2H, and 15N resonances of the Rieske ferredoxin component of toluene 4-monooxygenase. Xia B; Pikus JD; Xia W; McClay K; Steffan RJ; Chae YK; Westler WM; Markley JL; Fox BG Biochemistry; 1999 Jan; 38(2):727-39. PubMed ID: 9888813 [TBL] [Abstract][Full Text] [Related]
14. Protein expression, selective isotopic labeling, and analysis of hyperfine-shifted NMR signals of Anabaena 7120 vegetative [2Fe-2S]ferredoxin. Cheng H; Westler WM; Xia B; Oh BH; Markley JL Arch Biochem Biophys; 1995 Jan; 316(1):619-34. PubMed ID: 7840674 [TBL] [Abstract][Full Text] [Related]
15. Comparison and characterization of the [Fe4S4]2+/3+ centre in the wild-type and C77S mutated HiPIPs from Chromatium vinosum monitored by Mössbauer, 57Fe ENDOR and EPR spectroscopies. Dilg AW; Capozzi F; Mentler M; Iakovleva O; Luchinat C; Bertini I; Parak FG J Biol Inorg Chem; 2001 Mar; 6(3):232-46. PubMed ID: 11315559 [TBL] [Abstract][Full Text] [Related]
16. 1H NMR of high-potential iron-sulfur protein from the purple non-sulfurbacterium Rhodoferax fermentans. Ciurli S; Cremonini MA; Kofod P; Luchinat C Eur J Biochem; 1996 Mar; 236(2):405-11. PubMed ID: 8612609 [TBL] [Abstract][Full Text] [Related]
17. Factors influencing redox thermodynamics and electron self-exchange for the [Fe4S4] cluster in Chromatium vinosum high potential iron protein: the role of core aromatic residues in defining cluster redox chemistry. Soriano A; Li D; Bian S; Agarwal A; Cowan JA Biochemistry; 1996 Sep; 35(38):12479-86. PubMed ID: 8823183 [TBL] [Abstract][Full Text] [Related]
18. Role of aromatic residues in stabilization of the [Fe4S4] cluster in high-potential iron proteins (HiPIPs): physical characterization and stability studies of Tyr-19 mutants of Chromatium vinosum HiPIP. Agarwal A; Li D; Cowan JA Proc Natl Acad Sci U S A; 1995 Oct; 92(21):9440-4. PubMed ID: 7568150 [TBL] [Abstract][Full Text] [Related]
19. Investigation of the role of a surface patch in the self-association of Chromatium vinosum high potential iron-sulfur protein. Couture MM; Auger M; Rosell F; Mauk AG; Boubour E; Lennox RB; Eltis LD Biochim Biophys Acta; 1999 Aug; 1433(1-2):159-69. PubMed ID: 10446369 [TBL] [Abstract][Full Text] [Related]
20. Further characterization of the spin coupling observed in oxidized hydrogenase from Chromatium vinosum. A Mössbauer and multifrequency EPR study. Surerus KK; Chen M; van der Zwaan JW; Rusnak FM; Kolk M; Duin EC; Albracht SP; Münck E Biochemistry; 1994 Apr; 33(16):4980-93. PubMed ID: 8161560 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]