World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
47
Citations
12317
World Ranking
18584
National Ranking
7595

Overview

James B. Howard was affiliated with the University of Minnesota in the United States. Their research focused on several areas within energy and chemical engineering, with specific attention to renewable energy, sustainability, the environment, and catalysis.

Their main fields of study included:

  • Energy
  • Chemical Engineering

Subfields of their research work encompassed:

  • Renewable Energy, Sustainability and the Environment
  • Catalysis

Howard's scientific contributions addressed topics such as:

  • Metalloenzymes and iron-sulfur proteins
  • Ammonia Synthesis and Nitrogen Reduction
  • Electrocatalysts for Energy Conversion

Their recent publication record includes a paper titled Structural consequences of turnover-induced homocitrate loss in nitrogenase, published in 2023 in Nature Communications. This work has been cited 26 times. The publication venue, Nature Communications, also appears as a frequent publishing platform for their research.

Frequent co-authors during their career included:

  • Rebeccah A. Warmack
  • Ailiena O. Maggiolo
  • Andres Orta
  • Belinda B. Wenke
  • Douglas C. Rees

Best Publications

  • Structural Basis of Biological Nitrogen Fixation.

    James B. Howard;Douglas C. Rees

  • Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor.

    Oliver Einsle;Oliver Einsle;F. Akif Tezcan;Susana L. A. Andrade;Susana L. A. Andrade;Benedikt Schmid

  • The Mode of Action of Vitamin K IDENTIFICATION OF γ-CARBOXYGLUTAMIC ACID AS A COMPONENT OF PROTHROMBIN

    Gary L. Nelsestuen;Thomas H. Zytkovicz;James Bryant Howard

  • Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction.

    Hermann Schindelin;Caroline Kisker;Jamie L. Schlessman;James B. Howard

  • Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase

    Thomas Spatzal;Kathryn A. Perez;Oliver Einsle;James B. Howard;James B. Howard

  • ADP-ribosylation of elongation factor 2 by diphtheria toxin. NMR spectra and proposed structures of ribosyl-diphthamide and its hydrolysis products.

    B G Van Ness;J B Howard;J W Bodley

  • Structural basis of biological nitrogen fixation

    Douglas C Rees;F Akif Tezcan;Chad A Haynes;Mika Y Walton

  • Nitrogenase: Standing at the Crossroads

    Douglas C Rees;James B Howard

  • Nitrogenase: A Nucleotide-Dependent Molecular Switch

    James B. Howard;Douglas C. Rees

  • How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixation

    James B. Howard;Douglas C. Rees

  • The interface between the biological and inorganic worlds: iron-sulfur metalloclusters.

    Douglas C. Rees;James B. Howard

  • Nitrogenase complexes : Multiple docking sites for a nucleotide switch protein

    F. Akif Tezcan;F. Akif Tezcan;Jens T. Kaiser;Jens T. Kaiser;Debarshi Mustafi;Debarshi Mustafi;Mika Y. Walton;Mika Y. Walton

  • ADP-ribosylation of elongation factor 2 by diphtheria toxin. Isolation and properties of the novel ribosyl-amino acid and its hydrolysis products.

    B G Van Ness;J B Howard;J W Bodley

  • Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum.

    Jamie L Schlessman;Deborah Woo;Leemor Joshua-Tor;James B Howard

  • Characterization of alkylamine-sensitive site in alpha 2-macroglobulin.

    Richard P. Swenson;James Bryant Howard

  • Determinants of protein hyperthermostability: purification and amino acid sequence of rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR.

    Paul R. Blake;Jae Bum Park;Frank O. Bryant;Shigetoshi Aono

  • Thiol reactivity of the nitrogenase Fe-protein from Azotobacter vinelandii.

    R P Hausinger;J B Howard

  • Reactive site in human alpha 2-macroglobulin: circumstantial evidence for a thiolester.

    James Bryant Howard

  • Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor

    Thomas Spatzal;Kathryn A Perez;James B Howard;James B Howard;Douglas C Rees

  • MgATP-Bound and Nucleotide-Free Structures of a Nitrogenase Protein Complex between the Leu 127Δ-Fe-Protein and the MoFe-Protein†,‡

    Hsiu-Ju Chiu;John W. Peters;William N. Lanzilotta;Matthew J. Ryle

Frequent Co-Authors

Douglas C. Rees
Douglas C. Rees California Institute of Technology
Oliver Einsle
Oliver Einsle University of Freiburg
Robert P. Hausinger
Robert P. Hausinger Michigan State University
Dennis R. Dean
Dennis R. Dean Virginia Tech
Hermann Schindelin
Hermann Schindelin University of Würzburg
Caroline Kisker
Caroline Kisker University of Würzburg
Gary L. Nelsestuen
Gary L. Nelsestuen University of Minnesota
Michael W. W. Adams
Michael W. W. Adams University of Georgia
Gary P. Roberts
Gary P. Roberts University of Wisconsin–Madison
Alexander N. Glazer
Alexander N. Glazer University of California, Berkeley

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