G. Watt

发表

Electrical energy from carbohydrate oxidation during viologen-catalyzed O2-oxidation: Mechanistic insights

D. Wheeler, G. Watt, Dane C. Hansen, 2011 .

Iron core formation in horse spleen ferritin: magnetic susceptibility, pH, and compositional studies.

R. Frankel, S. Hilty, G. Watt, 1994, Journal of inorganic biochemistry.

Redox properties and Moessbauer spectroscopy of Azotobacter vinelandii bacterioferritin

R. Frankel, G. Papaefthymiou, G. Watt, 1986 .

Bio-Nanobattery Development and Characterization

Glen C. King, P. T. Lillehei, Jae-Woo Kim, 2005 .

Biotemplated Multilayer Structure for Nanoscale Energy Storage Units

Glen C. King, P. T. Lillehei, Jae-Woo Kim, 2005 .

DEVELOPMENT OF NANOSCALE POWER SYSTEM USING BIOLOGICAL SELF-ASSEMBLY METHOD

Glen C. King, Robert C. Davis, P. T. Lillehei, 2003 .

Reduction of mammalian ferritin.

R. Frankel, G. Papaefthymiou, G. Watt, 1985, Proceedings of the National Academy of Sciences of the United States of America.

A chemical preparation of pure reduced viologens for use as biomolecular reducing reagents.

G. Watt, J. L. Corbin, James L. Corbin, 1990, Analytical biochemistry.

Evidence for a Two-Electron Transfer Using the All-Ferrous Fe Protein during Nitrogenase Catalysis*

G. Watt, A. Nyborg, Joseph L. Johnson, 2000, The Journal of Biological Chemistry.

A new future for carbohydrate fuel cells

G. Watt, 2014 .

Isolation and characterization of two rubredoxins from Clostridium thermoaceticum.

L. Ljungdahl, G. Watt, Shiow-Shong Yang, 1980, Biochimica et biophysica acta.

Viologen Catalysts for a Direct Carbohydrate Fuel Cell

D. Wheeler, G. Watt, Dane C. Hansen, 2009 .

Large anions induce H2-production from the nitrogenase MoFe proteins of Clostridium Pasteurianum and Azotobacter vinelandii.

G. Watt, Z.-C. Wang, 2020, Journal of inorganic biochemistry.

Nucleotide-assisted [Fe4S4] redox state interconversions of the Azotobacter vinelandii Fe protein and their relevance to nitrogenase catalysis.

G. Watt, D. Jacobs, 2013, Biochemistry.

Duplication and extension of the Thorneley and Lowe kinetic model for Klebsiella pneumoniae nitrogenase catalysis using a MATHEMATICA software platform.

P. E. Wilson, G. Watt, A. Nyborg, 2001, Biophysical chemistry.

EXAFS studies on the PN and POX states of the P-clusters in nitrogenase

K. Hodgson, B. Hedman, B. Burgess, 1998, JBIC Journal of Biological Inorganic Chemistry.

Stoichiometry, ATP/2e values, and energy requirements for reactions catalyzed by nitrogenase from Azotobacter vinelandii.

W. A. Bulen, G. Watt, A. Burns, 1975, Biochemistry.

Reductant-independent ATP hydrolysis catalyzed by homologous nitrogenase proteins from Azotobacter vinelandii and heterologous crosses with Clostridium pasteuranium.

G. Watt, C. Larsen, S. Christensen, 1995, Archives of biochemistry and biophysics.

Formation of an all ferrous Fe4S4 cluster in the iron protein component of Azotobacter vinelandii nitrogenase

G. Watt, K. Reddy, 1994 .

Comparison of redox and EPR properties of the molybdenum iron proteins of Clostridium pasteurianum and Azotobacter vinelandii nitrogenases.

G. Watt, L. Mortenson, T. Morgan, 1988, Journal of inorganic biochemistry.

Redox reactions of and nucleotide binding to the iron protein of Azotobacter vinelandii

G. Watt, R. R. Knotts, Z.-C. Wang, 1986 .

Redox and spectroscopic properties of oxidized MoFe protein from Azotobacter vinelandii.

D. Tennent, G. Watt, S. Lough, 1980, Biochemistry.

An electrochemical method for measuring redox potentials of low potential proteins by microcoulometry at controlled potentials.

G. Watt, 1979, Analytical biochemistry.

Flavodoxin hydroquinone reduces Azotobacter vinelandii Fe protein to the all-ferrous redox state with a S = 0 spin state

P. E. Wilson, D. Thiriot, Bo Zhang, 2006, Proceedings of the National Academy of Sciences.

Evidence for a synergistic salt-protein interaction -- complex patterns of activation vs. inhibition of nitrogenase by salt.

P. E. Wilson, T. Lowery, G. Watt, 2006, Biophysical chemistry.

Reduction of nitrogenase Fe protein from Azotobacter vinelandii by dithionite: quantitative and qualitative effects of nucleotides, temperature, pH and reaction buffer.

P. E. Wilson, T. Lowery, G. Watt, 2004, Biophysical chemistry.

Kinetics of dithionite ion utilization and ATP hydrolysis for reactions catalyzed by the nitrogenase complex from Azotobacter vinelandii.

G. Watt, A. Burns, 1977, Biochemistry.

Nitrogenase Reactivity Using Ti(III) as Reductant

G. Watt, A. Nyborg, Joseph L. Johnson, 2002 .

Reactions of Azotobacter vinelandii nitrogenase using Ti(III) as reductant.

J. Johnson, J. Erickson, G. Watt, 2000, Journal of inorganic biochemistry.

Reductant-Dependant ATP Utilization During Nitrogenase Catalysis: Studies Using Ti(III)

J. Erickson, G. Watt, A. Nyborg, 2000 .

Analysis of steady state Fe and MoFe protein interactions during nitrogenase catalysis.

P. E. Wilson, J. Johnson, G. Watt, 2000, Biochimica et biophysica acta.

Enhanced efficiency of ATP hydrolysis during nitrogenase catalysis utilizing reductants that form the all-ferrous redox state of the Fe protein.

J. Johnson, J. Erickson, G. Watt, 1999, Biochemistry.

Steady-state kinetic studies of dithionite utilization, component protein interaction, and the formation of an oxidized iron protein intermediate during Azotobacter vinelandii nitrogenase catalysis.

J. Johnson, J. Erickson, G. Watt, 1996, Biochemistry.

Stoichiometry and spectral properties of the MoFe cofactor and noncofactor redox centers in the MoFe protein of nitrogenase from Azotobacter vinelandii.

D. Tennent, G. Watt, A. Burns, 1981, Biochemistry.

Metal ion binding to apo, holo, and reconstituted horse spleen ferritin.

J. Johnson, G. Watt, B. Webb, 1995, Journal of inorganic biochemistry.

Further redox reactions of metal clusters in the molybdenum-iron protein of Azotobacter vinelandii nitrogenase

G. Watt, Z.-C. Wang, 1986 .

The concentration of cellular nitrogenase proteins in Azotobacter vinelandii whole cells as determined by activity measurements and electron paramagnetic resonance spectroscopy.

G. Watt, D. Mitchell, D. Jacobs, 1995, Archives of biochemistry and biophysics.

Mechanistic interpretation of the dilution effect for Azotobacter vinelandii and Clostridium pasteurianum nitrogenase catalysis.

P. E. Wilson, J. Johnson, G. Watt, 2000, Biochimica et biophysica acta.

Electron paramagnetic resonance spectrum of the iron protein of nitrogenase: existence of a g = 4 spectral component and its effect on spin quantization

G. Watt, J. Mcdonald, J. McDonald, 1985 .

Complex formation and O2 sensitivity of Azotobacter vinelandii nitrogenase and its component proteins.

G. Watt, Z. C. Wang, A. Burns, 1985, Biochemistry.

Redox reactions of the nitrogenase complex from Azotobacter vinelandii

G. Watt, S. Lough, A. Burns, 1983 .

Salt inhibition of nitrogenase catalysis and salt effects on the separate protein components

G. Watt, Z. C. Wang, A. Burns, 1985 .

Protein interaction with and higher oxidation states of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii

G. Watt, Z. C. Wang, 1989 .

Double integration and titration of the electron paramagnetic resonance signal in the molybdenum-iron protein of Azotobacter vinelandii

W. Euler, G. Watt, J. Martinsen, 1984 .

Electrochemical and Kinetic Studies of Nitrogenase: Brief Review and Recent Developments

G. Watt, 1980 .

A facile method of isolation for the iron molybdenum cofactor of nitrogenase and bacterial ferritin from extracts of azotobacter vinelandii

G. Watt, D. B. Jacobs, S. Parker, 1988 .

Redox Properties of The Nitrogenase Component Proteins from Azotobacter Vinelandii

G. Watt, 1985 .

Evidence for a Central Role of Lysine 15 of Azotobacter vinelandii Nitrogenase Iron Protein in Nucleotide Binding and Protein Conformational Changes (*)

M. J. Ryle, W. Lanzilotta, L. Seefeldt, 1995, The Journal of Biological Chemistry.

Purification, composition, charge, and molecular weight of the FeMo cofactor from Azotobacter vinelandii nitrogenase.

F. B. Simpson, G. Watt, M. Kofford, 1993, Journal of inorganic biochemistry.

Mathematical and Experimental Analysis of the Rate Performance of Viologen-Mediated Glucose Fuel Cells

J. Harb, G. Watt, Matthew B. Roberts, 2020, Journal of The Electrochemical Society.

Oxidation efficiency of glucose using viologen mediators for glucose fuel cell applications with non-precious anodes

Randy S. Lewis, J. Harb, G. Watt, 2020 .

Purification and characterization of a FeMo cofactor-deficient MoFe protein.

B. Burgess, G. Watt, N. Gavini, 1994, Biochemistry.

Anaerobic iron deposition into horse spleen, recombinant human heavy and light and bacteria ferritins by large oxidants.

Bo Zhang, G. Watt, Bo Zhang, 2007, Journal of inorganic biochemistry.

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.

Bo Zhang, J. Dominguez‐Vera, N. Gálvez, 2006, Biophysical chemistry.

Electrochemical analysis of the reduction of ferritin using oxidized methyl viologen

Kwang Min Shin, Seon Jeong Kim, J. Harb, 2006 .

Monoalkyl viologens are effective carbohydrate O2-oxidation catalysts for electrical energy generation by fuel cells

D. Wheeler, W. Pitt, G. Watt, 2012 .

Kinetic studies of iron deposition in horse spleen ferritin using O2 as oxidant.

T. Lowery, G. Watt, K. Crawford, 2003, Biochimica et biophysica acta.

Further characterization of the redox and spectroscopic properties of Azotobacter vinelandii ferritin.

G. Watt, K. Reddy, C. Chiu, 1993, Journal of inorganic biochemistry.

Redox reactions of apo mammalian ferritin.

R. Frankel, G. Watt, R. K. Watt, 1992, Biochemistry.

Redox Capacity of APO Mammalian Ferritin

R. Frankel, G. Watt, 1991 .

Electron paramagnetic resonance studies of the tungsten-containing formate dehydrogenase from Clostridiumthermoaceticum

C. Durfor, E. Solomon, G. Watt, 1987 .

Molecular entrapment of small molecules within the interior of horse spleen ferritin.

J. Frame, M. Lee, G. Watt, 1994, Archives of biochemistry and biophysics.

Solubilization of the iron molybdenum cofactor of Azotobacter vinelandii nitrogenase in dimethylformamide and acetonitrile.

D. Lyons, G. Watt, D. Jacobs, 1986, Biochemical and biophysical research communications.

Variation of superparamagnetic properties with iron loading in mammalian ferritin

R. Frankel, G. Papaefthymiou, G. Watt, 1991 .

Redox reactivity of animal apoferritins and apoheteropolymers assembled from recombinant heavy and light human chain ferritins.

R. Frankel, J. Johnson, P. Arosio, 1999, Biochemistry.

Redox reactions associated with iron release from mammalian ferritin.

R. Frankel, G. Papaefthymiou, G. Watt, 1989, Biochemistry.

Redox reactivity of bacterial and mammalian ferritin: is reductant entry into the ferritin interior a necessary step for iron release?

R. Frankel, G. Watt, D. Jacobs, 1988, Proceedings of the National Academy of Sciences of the United States of America.

The enthalpy of binding of various transition metal ions to bovine apocarbonic anhydrase.

J. Sturtevant, G. Watt, R. Henkens, 1969, Biochemistry.

Copper(II) complexes of -phenethylamine and mescaline

G. Watt, 1974 .

Thermodynamics of metal cyanide coordination. VI. Copper(I)- and silver(I)-cyanide systems

R. M. Izatt, J. J. Christensen, G. Watt, 1967 .

Fe2+ and phosphate interactions in bacterial ferritin from Azotobacter vinelandii.

R. Frankel, G. Papaefthymiou, G. Watt, 1992, Biochemistry.

Azotobacter cytochrome b557.5 is a bacterioferritin

G. Watt, E. Stiefel, EDWARD I. STIEFEL, 1979, Nature.

Reversible binding of acetylene by oxobis(diethyldithiocarbamate)molybdenum

W. Newton, G. Watt, R. Wentworth, 1978 .

Thermochemical studies of molybdenum dithio-carbamate complexes as models for molybdoenzymes

W. Newton, G. Watt, J. McDonald, 1977 .

Electron paramagnetic resonance studies of the tungsten-containing formate dehydrogenase from Clostridium thermoaceticum.

C. Durfor, E. Solomon, G. Watt, 1987, Biochemical and biophysical research communications.

Thermodynamic parameters for the interaction of adenosine 5′-diphosphate, and adenosine 5′-triphosphate with Mg2+ from 323.15 to 398.15 K

R. M. Izatt, J. L. Oscarson, G. Watt, 1995 .

Iron environment in ferritin with large amounts of phosphate, from Azotobacter vinelandii and horse spleen, analyzed using extended X-ray absorption fine structure (EXAFS).

Elizabeth C. Theil, D. Sayers, G. Watt, 1990, Biochemistry.

Fe2+ binding to apo and holo mammalian ferritin.

R. Frankel, G. Papaefthymiou, G. Watt, 1989, Biochemistry.

Non-reductive iron release from horse spleen ferritin using desferoxamine chelation.

G. Watt, J. Kenealey, R. J. Hilton, 2011, Journal of inorganic biochemistry.

Thermodynamics of protonation of AMP, ADP, and ATP from 50 to 125°C

R. M. Izatt, J. Renuncio, J. L. Oscarson, 1995 .

A kinetic study of iron release from Azotobacter vinelandii bacterial ferritin.

G. Watt, T. Richards, K. Pitts, 1996, Journal of inorganic biochemistry.

Role of phosphate in Fe2+ binding to horse spleen holoferritin.

R. Frankel, G. Watt, H. Heqing, 1993, Biochemistry.

A calorimetric study of ligand interactions with protons and metal ions in the 100 to 400 C range

R. M. Izatt, X. Chen, J. L. Oscarson, 1995 .

Electron-mediated carbohydrate fuel cells: Characterizing the homogeneous viologen-mediated electron transfer rate of carbohydrate oxidation

Randy S. Lewis, J. Harb, G. Watt, 2020 .

A microcalorimetric procedure for evaluating the kinetic parameters of enzyme-catalyzed reactions: kinetic measurements of the nitrogenase system.

G. Watt, G D Watt, 1990, Analytical biochemistry.

An Asymmetric Viologen-Based Negolyte with a Low Redox Potential for Neutral Aqueous Redox Flow Batteries

J. Harb, G. Watt, M. Bahari, 2021 .

Kinetic evaluation of the viologen-catalyzed carbohydrate oxidation reaction for fuel cell application

G. Watt, 2014 .

Binding of Fe2+ by mammalian ferritin

R. Frankel, G. Watt, G. C. Papaefthymiou, 1987 .

Anion deposition into ferritin.

G. Watt, R. J. Hilton, R. K. Watt, 2012, Journal of inorganic biochemistry.

Electrochemically controlled reconstitution of immobilized ferritins for bioelectronic applications

Glen C. King, P. T. Lillehei, Jae-Woo Kim, 2007 .

Bacterioferritin: a hemoprotein member of the ferritin family.

R. Prince, G. George, R. Bare, 1994, Advances in experimental medicine and biology.

Kinetic studies of iron deposition catalyzed by recombinant human liver heavy and light ferritins and Azotobacter vinelandii bacterioferritin using O2 and H2O2 as oxidants.

R. Costen, P. Arosio, G. Watt, 2005, Biophysical chemistry.

Kinetic studies of iron deposition in horse spleen ferritin using H2O2 and O2 as oxidants.

R. Costen, T. Lowery, G. Watt, 2004, Biophysical chemistry.

Forming the phosphate layer in reconstituted horse spleen ferritin and the role of phosphate in promoting core surface redox reactions.

R. Frankel, J. Johnson, G. Watt, 1999, Biochemistry.

Ferritin-catalyzed consumption of hydrogen peroxide by amine buffers causes the variable Fe2+ to O2 stoichiometry of iron deposition in horse spleen ferritin

P. E. Wilson, G. Watt, Bo Zhang, 2006, JBIC Journal of Biological Inorganic Chemistry.

Hydrogen peroxide formation during iron deposition in horse spleen ferritin using O2 as an oxidant.

G. Watt, S. Lindsay, D. Brosnahan, 2001, Biochemistry.

Cobalt oxide hollow nanoparticles derived by bio-templating.

Glen C. King, P. T. Lillehei, Jae-Woo Kim, 2005, Chemical communications.

Direct observation of bis-sulfur ligation to the heme of bacterioferritin

R. Prince, G. George, R. Bare, 1993 .

H2-uptake activity of the MoFe protein component of Azotobacter vinelandii nitrogenase.

G. Watt, Z. C. Wang, 1984, Proceedings of the National Academy of Sciences of the United States of America.

Thermodynamics of the binding of S-peptide to S-protein to form ribonuclease S..

F. Richards, J. Sturtevant, G. Watt, 1971, Biochemistry.

Electrical conductivity of ferritin proteins by conductive AFM.

Robert C. Davis, J. Harb, Robert C Davis, 2005, Nano letters.

The new HERA data and the determination of the infrared behaviour of the BFKL amplitude

H. Kowalski, G. Watt, L. Lipatov, 2011 .

Thermodynamics of Metal Cyanide Coördination. II. ΔG0, ΔH0, and ΔS0 Values for Tetracyanoniccolate(II) Ion Formation in Aqueous Solution at 25°

R. T. Pack, R. M. Izatt, J. J. Christensen, 1963 .

Thermodynamics of Metal Cyanide Coordination. III. ΔG°, ΔH°, and ΔS° Values for Ferrocyanide and Ferricyanide Ion Formation in Aqueous Solution at 25°

R. M. Izatt, J. J. Christensen, G. Watt, 1965 .

Soluble viologen polymers as carbohydrate oxidation catalysts for alkaline carbohydrate fuel cells

Randy S. Lewis, J. Harb, P. Bhowmik, 2018, Journal of Electroanalytical Chemistry.

Characterization of ferritin core on redox reactions as a nanocomposite for electron transfer

Kwang Min Shin, Hyug-Han Kim, S. I. Kim, 2010 .

Thermodynamics of Metal Cyanide Coordination. IV. Log βi°, ΔHi°, and ΔSi°, Values for the Zinc(II)-Cyanide System at 25°

R. M. Izatt, J. J. Christensen, G. Watt, 1965 .

The enthalpy change accompanying the oxidation of ferrocytochrome c in the pH range 6-11 at 25 degrees.

J. Sturtevant, G. Watt, 1969, Biochemistry.

Electron exchange between Fe(II)-horse spleen ferritin and Co(III)/Mn(III) reconstituted horse spleen and Azotobacter vinelandii ferritins.

Robert C. Davis, J. Harb, Jae-Woo Kim, 2006, Biochemistry.