| Year |
Citation |
Score |
| 2020 |
Wang ZC, Watt GD. Large anions induce H-production from the nitrogenase MoFe proteins of Clostridium Pasteurianum and Azotobacter vinelandii. Journal of Inorganic Biochemistry. 208: 111075. PMID 32502717 DOI: 10.1016/J.Jinorgbio.2020.111075 |
0.342 |
|
| 2013 |
Jacobs D, Watt GD. Nucleotide-assisted [Fe4S4] redox state interconversions of the Azotobacter vinelandii Fe protein and their relevance to nitrogenase catalysis. Biochemistry. 52: 4791-9. PMID 23815521 DOI: 10.1021/Bi301547B |
0.396 |
|
| 2012 |
Hilton RJ, Zhang B, Martineau LN, Watt GD, Watt RK. Anion deposition into ferritin. Journal of Inorganic Biochemistry. 108: 8-14. PMID 22265833 DOI: 10.1016/J.Jinorgbio.2011.12.004 |
0.403 |
|
| 2012 |
Watt GD, Kim JW, Zhang B, Miller T, Harb JN, Davis RC, Choi SH. A protein-based ferritin bio-nanobattery Journal of Nanotechnology. DOI: 10.1155/2012/516309 |
0.38 |
|
| 2011 |
Johnson J, Kenealey J, Hilton RJ, Brosnahan D, Watt RK, Watt GD. Non-reductive iron release from horse spleen ferritin using desferoxamine chelation. Journal of Inorganic Biochemistry. 105: 202-7. PMID 21194619 DOI: 10.1016/J.Jinorgbio.2010.11.002 |
0.378 |
|
| 2010 |
Shin KM, Watt RK, Watt GD, Choi SH, Kim H, Kim SI, Kim SJ. Characterization of ferritin core on redox reactions as a nanocomposite for electron transfer Electrochimica Acta. 55: 3486-3490. DOI: 10.1016/J.Electacta.2010.01.086 |
0.317 |
|
| 2007 |
Zhang B, Watt GD. Anaerobic iron deposition into horse spleen, recombinant human heavy and light and bacteria ferritins by large oxidants. Journal of Inorganic Biochemistry. 101: 1676-85. PMID 17804076 DOI: 10.1016/J.Jinorgbio.2007.06.043 |
0.359 |
|
| 2006 |
Lowery TJ, Wilson PE, Zhang B, Bunker J, Harrison RG, Nyborg AC, Thiriot D, Watt GD. Flavodoxin hydroquinone reduces Azotobacter vinelandii Fe protein to the all-ferrous redox state with a S = 0 spin state. Proceedings of the National Academy of Sciences of the United States of America. 103: 17131-6. PMID 17085583 DOI: 10.1073/Pnas.0603223103 |
0.756 |
|
| 2006 |
Zhang B, Wilson PE, Watt GD. Ferritin-catalyzed consumption of hydrogen peroxide by amine buffers causes the variable Fe2+ to O2 stoichiometry of iron deposition in horse spleen ferritin. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 11: 1075-86. PMID 16896807 DOI: 10.1007/S00775-006-0141-6 |
0.702 |
|
| 2006 |
Zhang B, Harb JN, Davis RC, Choi S, Kim JW, Miller T, Chu SH, Watt GD. Electron exchange between Fe(II)-horse spleen ferritin and Co(III)/Mn(III) reconstituted horse spleen and Azotobacter vinelandii ferritins. Biochemistry. 45: 5766-74. PMID 16669620 DOI: 10.1021/Bi060164D |
0.394 |
|
| 2006 |
Wilson PE, Nyborg AC, Kenealey J, Lowery TJ, Crawford K, King CR, Engan AJ, Johnson JL, Watt GD. Evidence for a synergistic salt-protein interaction -- complex patterns of activation vs. inhibition of nitrogenase by salt. Biophysical Chemistry. 122: 184-94. PMID 16603308 DOI: 10.1016/J.Bpc.2006.03.007 |
0.774 |
|
| 2006 |
Zhang B, Watt RK, Gálvez N, Domínguez-Vera JM, Watt GD. Rate of iron transfer through the horse spleen ferritin shell determined by the rate of formation of Prussian Blue and Fe-desferrioxamine within the ferritin cavity. Biophysical Chemistry. 120: 96-105. PMID 16314026 DOI: 10.1016/J.Bpc.2005.10.005 |
0.43 |
|
| 2006 |
Shin KM, Watt GD, Zhang B, Harb JN, Harrison RG, Kim SI, Kim SJ. Electrochemical analysis of the reduction of ferritin using oxidized methyl viologen Journal of Electroanalytical Chemistry. 598: 22-26. DOI: 10.1016/J.Jelechem.2006.08.005 |
0.305 |
|
| 2005 |
Zhang B, Harb JN, Davis RC, Kim JW, Chu SH, Choi S, Miller T, Watt GD. Kinetic and thermodynamic characterization of the cobalt and manganese oxyhydroxide cores formed in horse spleen ferritin. Inorganic Chemistry. 44: 3738-45. PMID 15877458 DOI: 10.1021/Ic049085L |
0.373 |
|
| 2005 |
Bunker J, Lowry T, Davis G, Zhang B, Brosnahan D, Lindsay S, Costen R, Choi S, Arosio P, Watt GD. Kinetic studies of iron deposition catalyzed by recombinant human liver heavy and light ferritins and Azotobacter vinelandii bacterioferritin using O2 and H2O2 as oxidants. Biophysical Chemistry. 114: 235-44. PMID 15829358 DOI: 10.1016/J.Bpc.2004.11.008 |
0.316 |
|
| 2004 |
Lowery TJ, Bunker J, Zhang B, Costen R, Watt GD. Kinetic studies of iron deposition in horse spleen ferritin using H2O2 and O2 as oxidants. Biophysical Chemistry. 111: 173-81. PMID 15381314 DOI: 10.1016/J.Bpc.2004.05.008 |
0.374 |
|
| 2004 |
Wilson PE, Bunker J, Lowery TJ, Watt GD. Reduction of nitrogenase Fe protein from Azotobacter vinelandii by dithionite: quantitative and qualitative effects of nucleotides, temperature, pH and reaction buffer. Biophysical Chemistry. 109: 305-24. PMID 15110948 DOI: 10.1016/J.Bpc.2003.12.002 |
0.705 |
|
| 2003 |
Lindsay S, Brosnahan D, Lowery TJ, Crawford K, Watt GD. Kinetic studies of iron deposition in horse spleen ferritin using O2 as oxidant. Biochimica Et Biophysica Acta. 1621: 57-66. PMID 12667611 DOI: 10.1016/S0304-4165(03)00030-8 |
0.438 |
|
| 2001 |
Wilson PE, Nyborg AC, Watt GD. Duplication and extension of the Thorneley and Lowe kinetic model for Klebsiella pneumoniae nitrogenase catalysis using a MATHEMATICA software platform. Biophysical Chemistry. 91: 281-304. PMID 11551440 DOI: 10.1016/S0301-4622(01)00182-X |
0.724 |
|
| 2001 |
Lindsay S, Brosnahan D, Watt GD. Hydrogen peroxide formation during iron deposition in horse spleen ferritin using O2 as an oxidant. Biochemistry. 40: 3340-7. PMID 11258954 DOI: 10.1021/Bi001981V |
0.383 |
|
| 2000 |
Johnson JL, Nyborg AC, Wilson PE, Tolley AM, Nordmeyer FR, Watt GD. Mechanistic interpretation of the dilution effect for Azotobacter vinelandii and Clostridium pasteurianum nitrogenase catalysis. Biochimica Et Biophysica Acta. 1543: 36-46. PMID 11087939 DOI: 10.1016/S0167-4838(00)00196-5 |
0.758 |
|
| 2000 |
Johnson JL, Nyborg AC, Wilson PE, Tolley AM, Nordmeyer FR, Watt GD. Analysis of steady state Fe and MoFe protein interactions during nitrogenase catalysis. Biochimica Et Biophysica Acta. 1543: 24-35. PMID 11087938 DOI: 10.1016/S0167-4838(00)00195-3 |
0.782 |
|
| 2000 |
Nyborg AC, Johnson JL, Gunn A, Watt GD. Evidence for a two-electron transfer using the all-ferrous Fe protein during nitrogenase catalysis. The Journal of Biological Chemistry. 275: 39307-12. PMID 11005818 DOI: 10.1074/Jbc.M007069200 |
0.732 |
|
| 2000 |
Nyborg AC, Erickson JA, Johnson JL, Gunn A, Truscott SM, Watt GD. Reactions of Azotobacter vinelandii nitrogenase using Ti(III) as reductant. Journal of Inorganic Biochemistry. 78: 371-81. PMID 10857919 DOI: 10.1016/S0162-0134(00)00066-0 |
0.707 |
|
| 1999 |
Erickson JA, Nyborg AC, Johnson JL, Truscott SM, Gunn A, Nordmeyer FR, Watt GD. Enhanced efficiency of ATP hydrolysis during nitrogenase catalysis utilizing reductants that form the all-ferrous redox state of the Fe protein. Biochemistry. 38: 14279-85. PMID 10572002 DOI: 10.1021/bi991389 |
0.722 |
|
| 1999 |
Johnson JL, Cannon M, Watt RK, Frankel RB, Watt GD. Forming the phosphate layer in reconstituted horse spleen ferritin and the role of phosphate in promoting core surface redox reactions. Biochemistry. 38: 6706-13. PMID 10350490 DOI: 10.1021/Bi982727U |
0.398 |
|
| 1999 |
Johnson JL, Norcross DC, Arosio P, Frankel RB, Watt GD. Redox reactivity of animal apoferritins and apoheteropolymers assembled from recombinant heavy and light human chain ferritins. Biochemistry. 38: 4089-96. PMID 10194323 DOI: 10.1021/Bi982690D |
0.325 |
|
| 1998 |
Musgrave KB, Liu HI, Ma L, Burgess BK, Watt G, Hedman B, Hodgson KO. EXAFS studies on the P(N) and P(OX) states of the P-clusters in nitrogenase Journal of Biological Inorganic Chemistry. 3: 344-352. DOI: 10.1007/S007750050243 |
0.355 |
|
| 1996 |
Johnson JL, Tolley AM, Erickson JA, Watt GD. Steady-state kinetic studies of dithionite utilization, component protein interaction, and the formation of an oxidized iron protein intermediate during Azotobacter vinelandii nitrogenase catalysis Biochemistry. 35: 11336-11342. PMID 8784188 DOI: 10.1021/bi952581o |
0.309 |
|
| 1996 |
Richards TD, Pitts KR, Watt GD. A kinetic study of iron release from azotobacter vinelandii bacterial ferritin Journal of Inorganic Biochemistry. 61: 1-13. PMID 8558133 DOI: 10.1016/0162-0134(95)00029-1 |
0.345 |
|
| 1995 |
Pead S, Durrant E, Webb B, Larsen C, Heaton D, Johnson J, Watt GD. Metal ion binding to apo, holo, and reconstituted horse spleen ferritin Journal of Inorganic Biochemistry. 59: 15-27. PMID 7782791 DOI: 10.1016/0162-0134(94)00050-K |
0.304 |
|
| 1995 |
Ryle MJ, Lanzilotta WN, Mortenson LE, Watt GD, Seefeldt LC. Evidence for a central role of lysine 15 of Azotobacter vinelandii nitrogenase iron protein in nucleotide binding and protein conformational changes. The Journal of Biological Chemistry. 270: 13112-7. PMID 7768906 DOI: 10.1074/Jbc.270.22.13112 |
0.362 |
|
| 1995 |
Izatt RM, Oscarson JL, Gillespie SE, Chen X, Wang P, Watt GD. A calorimetric study of ligand interactions with protons and metal ions in the 100 to 400 °C range Pure and Applied Chemistry. 67: 543-549. DOI: 10.1351/Pac199567040543 |
0.726 |
|
| 1995 |
Wang P, Oscarson JL, Izatt RM, Watt GD, Larsen CD. Thermodynamic parameters for the interaction of adenosine 5′-diphosphate, and adenosine 5′-triphosphate with Mg2+ from 323.15 to 398.15 K Journal of Solution Chemistry. 24: 989-1012. DOI: 10.1007/Bf00973517 |
0.709 |
|
| 1995 |
Oscarson JL, Wang P, Gillespie SE, Izatt RM, Watt GD, Larsen CD, Renuncio JAR. Thermodynamics of protonation of AMP, ADP, and ATP from 50 to 125°C Journal of Solution Chemistry. 24: 171-200. DOI: 10.1007/Bf00972840 |
0.748 |
|
| 1994 |
Hilty S, Webb B, Frankel RB, Watt GD. Iron core formation in horse spleen ferritin: Magnetic susceptibility, pH, and compositional studies Journal of Inorganic Biochemistry. 56: 173-185. PMID 7798900 DOI: 10.1016/0162-0134(94)85004-6 |
0.373 |
|
| 1994 |
Watt GD, Reddy K. Formation of an all ferrous Fe4S4 cluster in the iron protein component of Azotobacter vinelandii nitrogenase Journal of Inorganic Biochemistry. 53: 281-294. DOI: 10.1016/0162-0134(94)85115-8 |
0.437 |
|
| 1993 |
Heqing H, Watt RK, Frankel RB, Watt GD. Role of phosphate in Fe2+ binding to horse spleen holoferritin. Biochemistry. 32: 1681-7. PMID 8431449 DOI: 10.1021/Bi00057A036 |
0.385 |
|
| 1993 |
Watt GD, McDonald JW, Chiu CH, Reddy KR. Further characterization of the redox and spectroscopic properties of Azotobacter vinelandii ferritin. Journal of Inorganic Biochemistry. 51: 745-58. PMID 8245955 DOI: 10.1016/0162-0134(93)85007-U |
0.375 |
|
| 1993 |
George GN, Richards T, Bare RE, Gea Y, Prince RC, Stiefel EI, Watt GD. Direct observation of bis-sulfur ligation to the heme of bacterioferritin Journal of the American Chemical Society. 115: 7716-7718. DOI: 10.1021/Ja00070A015 |
0.309 |
|
| 1992 |
Watt GD, Frankel RB, Jacobs D, Huang H, Papaefthymiou GC. Fe2+ and phosphate interactions in bacterial ferritin from Azotobacter vinelandii. Biochemistry. 31: 5672-9. PMID 1610815 DOI: 10.1021/Bi00139A035 |
0.417 |
|
| 1992 |
Watt RK, Frankel RB, Watt GD. Redox reactions of apo mammalian ferritin. Biochemistry. 31: 9673-9. PMID 1327125 DOI: 10.1021/Bi00155A021 |
0.445 |
|
| 1990 |
Jacobs D, Watt GD, Frankel RB, Papaefthymiou GC. Fe2+ binding to apo and holo mammalian ferritin. Biochemistry. 28: 9216-21. PMID 2557919 DOI: 10.1021/Bi00449A038 |
0.42 |
|
| 1990 |
Rohrer JS, Islam QT, Watt GD, Sayers DE, Theil EC. Iron environment in ferritin with large amounts of phosphate, from Azotobacter vinelandii and horse spleen, analyzed using extended X-ray absorption fine structure (EXAFS) Biochemistry. 29: 259-264. PMID 2322545 DOI: 10.1021/Bi00453A035 |
0.375 |
|
| 1989 |
Jacobs DL, Watt GD, Frankel RB, Papaefthymiou GC. Redox reactions associated with iron release from mammalian ferritin. Biochemistry. 28: 1650-5. PMID 2541760 DOI: 10.1021/Bi00430A033 |
0.378 |
|
| 1988 |
Watt GD, Jacobs D, Frankel RB. Redox reactivity of bacterial and mammalian ferritin: is reductant entry into the ferritin interior a necessary step for iron release? Proceedings of the National Academy of Sciences of the United States of America. 85: 7457-61. PMID 2845407 DOI: 10.1073/pnas.85.20.7457 |
0.338 |
|
| 1985 |
Watt GD, Frankel RB, Papaefthymiou GC. Reduction of mammalian ferritin. Proceedings of the National Academy of Sciences of the United States of America. 82: 3640-3. PMID 3858840 DOI: 10.1073/Pnas.82.11.3640 |
0.416 |
|
| 1985 |
Wang ZC, Burns A, Watt GD. Complex formation and O2 sensitivity of Azotobacter vinelandii nitrogenase and its component proteins. Biochemistry. 24: 214-21. PMID 2986674 DOI: 10.1021/bi00322a031 |
0.3 |
|
| 1977 |
Watt GD, Burns A. Kinetics of dithionite ion utilization and ATP hydrolysis for reactions catalyzed by the nitrogenase complex from Azotobacter vinelandii. Biochemistry. 16: 264-70. PMID 836787 DOI: 10.1021/Bi00621A017 |
0.346 |
|
| 1970 |
Izatt RM, Watt GD, Bartholomew CH, Christensen JJ. Calorimetric study of Prussian blue and Turnbull's blue formation Inorganic Chemistry. 9: 2019-2021. DOI: 10.1021/Ic50091A012 |
0.435 |
|
| 1970 |
IZATT RM, WATT GD, BARTHOLOMEW CH, CHRISTENSEN JJ. ChemInform Abstract: BILDUNGSENTHALPIE VON LOESLICHEM PREUSSISCH BLAU UND TURNBULLS BLAU (KOMPLEXBILDUNGSMECHANISMUS) Chemischer Informationsdienst. Organische Chemie. 1: no-no. DOI: 10.1002/Chin.197046048 |
0.395 |
|
| 1968 |
Izatt RM, Watt GD, Bartholomew CH, Christensen JJ. Thermodynamics of metal cyanide coordination. VIII. A calorimetric study of Co2+-CN- interaction Inorganic Chemistry. 7: 2236-2239. DOI: 10.1021/Ic50069A012 |
0.469 |
|
| 1967 |
Izatt RM, Watt GD, Eatough D, Christensen JJ. Thermodynamics of metal cyanide co-ordination. Part VII. Log K, ΔH°, and ΔS°values for the interaction of CN- with Pd2+. ΔH°values for the interaction of Cl- and Br- with Pd2+ Journal of the Chemical Society a: Inorganic, Physical, and Theoretical Chemistry. 1304-1308. DOI: 10.1039/J19670001304 |
0.576 |
|
| 1967 |
Izatt RM, Johnston HD, Watt GD, Christensen JJ. Thermodynamics of metal cyanide coordination. VI. Copper(I)- and silver(I)-cyanide systems Inorganic Chemistry. 6: 132-135. DOI: 10.1021/Ic50047A030 |
0.431 |
|
| 1965 |
Izatt RM, Christensen JJ, Hansen JW, Watt GD. Thermodynamics of Metal Cyanide Coordination. IV. Log βi°, ΔHi°, and ΔSi°, Values for the Zinc(II)-Cyanide System at 25° Inorganic Chemistry. 4: 718-721. DOI: 10.1021/Ic50027A026 |
0.46 |
|
| 1965 |
Watt GD, Christensen JJ, Izatt RM. Thermodynamics of Metal Cyanide Coordination. III. ΔG°, ΔH°, and ΔS° Values for Ferrocyanide and Ferricyanide Ion Formation in Aqueous Solution at 25° Inorganic Chemistry. 4: 220-222. DOI: 10.1021/Ic50024A020 |
0.497 |
|
| 1963 |
Christensen JJ, Izatt RM, Hale JD, Pack RT, Watt GD. Thermodynamics of Metal Cyanide Coördination. II. ΔG0, ΔH0, and ΔS0Values for Tetracyanoniccolate(II) Ion Formation in Aqueous Solution at 25° Inorganic Chemistry. 2: 337-339. DOI: 10.1021/Ic50006A024 |
0.68 |
|
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