John Peters

Professor and Chair

University of Oklahoma

United States

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John Peters is a Professor and Chair at the University of Oklahoma in the United States. His research areas encompass the catalytic properties of hydrogenases, nitrogen fixation mechanisms, and the electronic structure of iron/sulfur clusters. Recent articles co-authored by him explore the dynamics of nitrogenase proteins and biochemical aspects of nitrogen-fixing bacteria.

Articles (13)

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2025

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2025

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2023

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2023

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2022

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2022

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2022

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2022

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2022

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2022

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2022

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2021

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2021

Collaborators (10)

Luis M. Rubio

SPAIN

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Patricia Dos Santos

professor

Wake Forest University

UNITED STATES

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Oliver Einsle

University of Freiburg

GERMANY

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Oleg A. Zadvornyy

Montana State University

UNITED STATES

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Dana Shaw

Assistant Professor

Washington State University

UNITED STATES

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GORDANA DUKOVIC

University of Colorado Boulder

UNITED STATES

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Alan G. Goodman

College of Veterinary Medicine

UNITED STATES

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Katherine Shulenberger

Assistant Professor of Chemistry

Brandeis University

UNITED STATES

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Lance Seefeldt

Professor

Utah State University

UNITED STATES

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Dennis Dean

University Distinguished Professor

Virginia Polytechnic Institute and State University

UNITED STATES

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John Peters

Research Interests

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About

Articles (13)

H-cluster Intermediates and Catalytic Properties of Clostridium pasteurianum [FeFe]-Hydrogenase III

The Properties That Allow Tuning the Reduction Potentials over a Volt Range in Biological Iron/Sulfur Clusters

Mechanisms for Generating Low Potential Electrons across the Metabolic Diversity of Nitrogen-Fixing Bacteria

Low-temperature trapping of N2 reduction reaction intermediates in nitrogenase MoFe protein–CdS quantum dot complexes

Overview of physiological, biochemical, and regulatory aspects of nitrogen fixation in Azotobacter vinelandii

Correction for Sidak-Loftis et al., “The Unfolded-Protein Response Triggers the Arthropod Immune Deficiency Pathway”

The Unfolded-Protein Response Triggers the Arthropod Immune Deficiency Pathway

The Kinetics of Electron Transfer from CdS Nanorods to the MoFe Protein of Nitrogenase

Rnf and Fix Have Specific Roles during Aerobic Nitrogen Fixation in Azotobacter vinelandii

Dissecting Electronic-Structural Transitions in the Nitrogenase MoFe Protein P-Cluster during Reduction

A site-differentiated [4Fe–4S] cluster controls electron transfer reactivity of Clostridium acetobutylicum [FeFe]-hydrogenase I

Metabolic Model of the Nitrogen-Fixing Obligate Aerobe Azotobacter vinelandii Predicts Its Adaptation to Oxygen Concentration and Metal Availability

Comment on “Structural evidence for a dynamic metallocofactor during N 2 reduction by Mo-nitrogenase”

Collaborators (10)

Luis M. Rubio

Patricia Dos Santos

Oliver Einsle

Oleg A. Zadvornyy

Dana Shaw

GORDANA DUKOVIC

Alan G. Goodman

Katherine Shulenberger

Lance Seefeldt

Dennis Dean

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