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Chemistry

D-Index
58
Citations
10524
World Ranking
10761
National Ranking
610

Overview

Robert R. Eady is affiliated with the University of Liverpool in the United Kingdom. Their research spans fields primarily within Biochemistry, Genetics and Molecular Biology, as well as Materials Science.

The scientist's work engages several subfields including Materials Chemistry, Molecular Biology, Renewable Energy, Sustainability and the Environment, Radiation, and Inorganic Chemistry. Their research topics cover a range of subjects such as Photosynthetic Processes and Mechanisms, Metalloenzymes and iron-sulfur proteins, Metal-Catalyzed Oxygenation Mechanisms, Nanocluster Synthesis and Applications, Microbial Fuel Cells and Bioremediation, Advanced X-ray Imaging Techniques, and Nuclear Physics and Applications.

Frequent publication venues for Robert R. Eady include:

  • Zenodo (CERN European Organization for Nuclear Research)
  • Acta Crystallographica Section A Foundations and Advances
  • Science Advances
  • Coordination Chemistry Reviews
  • FEBS Journal

Co-authors regularly collaborating with Robert R. Eady are:

  • S.V. Antonyuk
  • S.S. Hasnain
  • Samuel L. Rose
  • Takehiko Tosha
  • Masaki Yamamoto

Notable recent papers by Robert R. Eady include:

  • New horizons in structure-function studies of copper nitrite reductase, 2022, Coordination Chemistry Reviews
  • An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures, 2021, Science Advances
  • Reverse protein engineering of a novel 4-domain copper nitrite reductase reveals functional regulation by protein-protein interaction, 2020, FEBS Journal
  • Nature of the copper-nitrosyl intermediates of copper nitrite reductases during catalysis, 2020, Chemical Science
  • Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases, 2022, Proceedings of the National Academy of Sciences

Best Publications

  • Structure−Function Relationships of Alternative Nitrogenases

    Robert R. Eady

  • The alternative nitrogenase of Azotobacter chroococcum is a vanadium enzyme

    Robert L. Robson;Robert R. Eady;Toby H. Richardson;Richard W. Miller

  • Nitrogenase of Klebsiella pneumoniae. Purification and properties of the component proteins.

    R. R. Eady;B. E. Smith;K. A. Cook;J. R. Postgate

  • Current status of structure function relationships of vanadium nitrogenase

    Robert R. Eady

  • Analysis of regulation of Klebsiella pneumoniae nitrogen fixation (nif) gene cluster with gene fusions

    Ray Dixon;Robert R. Eady;Guadalupe Espin;Susan Hill

  • The vanadium nitrogenase of Azotobacter chroococcum. Purification and properties of the VFe protein.

    R R Eady;R L Robson;T H Richardson;R W Miller

  • Atomic Resolution Structures of Resting-State, Substrate- and Product-Complexed Cu-Nitrite Reductase Provide Insight Into Catalytic Mechanism

    Svetlana V. Antonyuk;Richard W. Strange;Gary Sawers;Robert R. Eady

  • Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine

    R R Eady;P J Large

  • Unprecedented proximal binding of nitric oxide to heme: implications for guanylate cyclase.

    David M. Lawson;Clare E.M. Stevenson;Colin R. Andrew;Robert R. Eady

  • Metalloclusters of the nitrogenases

    Barry E. Smith;Robert R. Eady

  • Biological nitrogen fixation by way of an enzyme-bound dinitrogen-hydride intermediate

    Roger N. F. Thorneley;Robert R. Eady;David J. Lowe

  • Vanadium K-edge X-ray absorption spectrum of the VFe protein of the vanadium nitrogenase of Azotobacter chroococcum

    Judith M. Arber;Barry R. Dobson;Robert R. Eady;Philippe Stevens

  • X-ray structure of a blue-copper nitrite reductase in two crystal forms. The nature of the copper sites, mode of substrate binding and recognition by redox partner.

    F. E. Dodd;J. Van Beeumen;R. R. Eady;S. Samar Hasnain

  • Molybdenum and vanadium nitrogenases of Azotobacter chroococcum. Low temperature favours N2 reduction by vanadium nitrogenase.

    R W Miller;R R Eady

  • Ethane formation from acetylene as a potential test for vanadium nitrogenase in vivo

    Michael J. Dilworth;Robert R. Eady;Robert L. Robson;Richard W. Miller

  • The vanadium-iron protein of vanadium nitrogenase from Azotobacter chroococcum contains an iron-vanadium cofactor.

    B E Smith;R R Eady;D J Lowe;C Gormal

  • Quantitative EPR of an S = 7/2 system in thionine-oxidized MoFe proteins of nitrogenase. A redefinition of the P-cluster concept.

    Wilfred R. Hagen;Hans Wassink;Robert R. Eady;Barry E. Smith

  • Structural and kinetic evidence for an ordered mechanism of copper nitrite reductase

    Richard W Strange;Loretta M Murphy;Fraser E Dodd;Zelda H.L Abraham

  • Hydrazine is a product of dinitrogen reduction by the vanadium-nitrogenase from Azotobacter chroococcum.

    M J Dilworth;R R Eady

  • The vanadium nitrogenase of Azotobacter chroococcum. Reduction of acetylene and ethylene to ethane

    M J Dilworth;R R Eady;M E Eldridge

Frequent Co-Authors

S. Samar Hasnain
S. Samar Hasnain University of Liverpool
Richard W. Strange
Richard W. Strange University of Essex
Roger N. F. Thorneley
Roger N. F. Thorneley John Innes Centre
Gary Sawers
Gary Sawers Martin Luther University Halle-Wittenberg
Nigel S. Scrutton
Nigel S. Scrutton University of Manchester
Masaki Yamamoto
Masaki Yamamoto University of Hyogo
Cees Veeger
Cees Veeger Wageningen University & Research
Michael J. Dilworth
Michael J. Dilworth Murdoch University
Daniel Kahn
Daniel Kahn Claude Bernard University Lyon 1
Konstantinos M. Paraskevopoulos
Konstantinos M. Paraskevopoulos Aristotle University of Thessaloniki

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