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Chemistry

D-Index
69
Citations
12896
World Ranking
6376
National Ranking
1931

Overview

James A. Fee was affiliated with the Scripps Research Institute in the United States. Throughout their career, Fee contributed to the scientific community within this prestigious research institution.

There are no records of recent papers authored by Fee available in the provided data. Similarly, no frequent co-authors or publication venues have been documented for their body of work.

The profile also lacks explicit information regarding main fields or subfields of study as well as specific topics of research covered by Fee. There is no data on book publications or awards received over the course of their career.

The scientist is deceased, which frames their contributions as part of the historical academic landscape associated with Scripps Research Institute.

Best Publications

  • Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus.

    Myoung S. Lah;Melinda M. Dixon;Katherine A. Pattridge;William C. Stallings

  • copper proteins systems containing the “Blue” copper center

    James A. Fee

  • Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulation (fur) locus.

    E C Niederhoffer;C M Naranjo;K L Bradley;J A Fee

  • Steady-state and transient-state kinetic studies on the oxidation of 3,4-dimethoxybenzyl alcohol catalyzed by the ligninase of Phanerocheate chrysosporium Burds.

    M Tien;T K Kirk;C Bull;J A Fee

  • Purification and characterization of the Rieske iron-sulfur protein from Thermus thermophilus. Evidence for a [2Fe-2S] cluster having non-cysteine ligands.

    J A Fee;K L Findling;T Yoshida;R Hille

  • Electron−nuclear double resonance spectroscopy of 15N-enriched phthalate dioxygenase from Pseudomonas cepacia proves that two histidines are coordinated to the [2Fe-2S] Rieske-type clusters

    Ryszard J. Gurbiel;Christopher J. Batie;Mohanram Sivaraja;Anne E. True

  • The mechanism of iron EDTA catalyzed superoxide dismutation

    Christopher Bull;Gregory J. McClune;James A. Fee

  • Steady-state kinetic studies of superoxide dismutases: properties of the iron containing protein from Escherichia coli

    Christopher Bull;James A. Fee

  • Evidence that superoxide dismutase plays a role in protecting red blood cells against peroxidative hemolysis

    James A. Fee;H.David Teitelbaum

  • Kinetic studies of superoxide dismutases: properties of the manganese-containing protein from Thermus thermophilus

    Christopher Bull;Eric C. Niederhoffer;Tatsuro Yoshida;James A. Fee

  • Anion Binding to Bovine Erythrocyte Superoxide Dismutase EVIDENCE FOR MULTIPLE BINDING SITES WITH QUALITATIVELY DIFFERENT PROPERTIES

    James A. Fee;Bruce P. Gaber

  • Iron superoxide dismutase. Nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structures.

    A Carlioz;M L Ludwig;W C Stallings;J A Fee

  • Evidence for N coordination to Fe in the [2Fe-2S] clusters of Thermus Rieske protein and phthalate dioxygenase from Pseudomonas.

    J F Cline;B M Hoffman;W B Mims;E LaHaie

  • Reduction potentials of Rieske clusters: importance of the coupling between oxidation state and histidine protonation state.

    Yanbing Zu;Manon M.-J. Couture;Derrick R. J. Kolling;Antony R. Crofts

  • The Oxygen Sensitivity of Spinach Ferredoxin and Other Iron-Sulfur Proteins THE FORMATION OF PROTEIN-BOUND SULFUR-ZERO

    David Petering;James A. Fee;Graham Palmer

  • Stopped flow spectrophotometric observation of superoxide dismutation in aqueous solution.

    Gregory J. McClune;James A. Fee

  • The iron electron-nuclear double resonance (ENDOR) of two-iron ferredoxins from spinach, parsley, pig adrenal cortex and Pseudomonas putida.

    J. Fritz;R. Anderson;James A. Fee;Graham Palmer

  • Properties of a copper-containing cytochrome ba3: a second terminal oxidase from the extreme thermophile Thermus thermophilus.

    Barbara H. Zimmermann;Carmen I. Nitsche;James A. Fee;Frank Rusnak

  • Water-soluble, recombinant CuA-domain of the cytochrome ba3 subunit II from Thermus thermophilus.

    Claire E. Slutter;Donita Sanders;Pernilla Wittung;Bo G. Malmström

  • Iron superoxide dismutase from Escherichia coli at 3.1-A resolution: a structure unlike that of copper/zinc protein at both monomer and dimer levels.

    William C. Stallings;Thomas B. Powers;Katherine A. Pattridge;James A. Fee

Frequent Co-Authors

C. David Stout
C. David Stout Scripps Research Institute
Bo G. Malmström
Bo G. Malmström University of Gothenburg
Graham Palmer
Graham Palmer Rice University
Eckard Münck
Eckard Münck Carnegie Mellon University
Michael G. Hill
Michael G. Hill Occidental College
Robert B. Gennis
Robert B. Gennis University of Illinois at Urbana-Champaign
Brian M. Hoffman
Brian M. Hoffman Northwestern University
Martha L. Ludwig
Martha L. Ludwig University of Michigan–Ann Arbor
Louis Noodleman
Louis Noodleman Scripps Research Institute
David A. Case
David A. Case Rutgers, The State University of New Jersey

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