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Chemistry

D-Index
42
Citations
5603
World Ranking
17611
National Ranking
961

Overview

Emma Lloyd Raven is affiliated with the University of Bristol in the United Kingdom. Their research spans multiple areas within biochemistry, genetics, and molecular biology, focusing particularly on molecular biology and inorganic chemistry. Additional subfields include radiation, cell biology, and biological psychiatry.

Their scientific contributions cover a range of main topics related to both fundamental and applied biochemical processes. These topics include:

  • Metal-Catalyzed Oxygenation Mechanisms
  • Porphyrin Metabolism and Disorders
  • Heme Oxygenase-1 and Carbon Monoxide
  • Photosynthetic Processes and Mechanisms
  • Hemoglobin structure and function
  • Advanced X-ray Imaging Techniques
  • Tryptophan and brain disorders

Among recent publications, Emma Lloyd Raven has contributed to several peer-reviewed articles published in notable journals. Some of the recent papers include:

  • "Understanding the Logistics for the Distribution of Heme in Cells," 2021, published in JACS Au
  • "Rewiring the 'Push-Pull' Catalytic Machinery of a Heme Enzyme Using an Expanded Genetic Code," 2020, published in ACS Catalysis
  • "Visualizing the protons in a metalloenzyme electron proton transfer pathway," 2020, published in Proceedings of the National Academy of Sciences
  • "Unravelling the mechanisms controlling heme supply and demand," 2021, published in Proceedings of the National Academy of Sciences
  • "Discovery of a heme-binding domain in a neuronal voltage-gated potassium channel," 2020, published in Journal of Biological Chemistry

Emma Lloyd Raven has co-authored extensively, with frequent collaborators including P.C.E. Moody, Hanna Kwon, Jaswir Basran, Samuel L. Freeman, and Alistair J. Fielding.

Their work has been published most often in the following scientific venues:

  • Journal of Biological Chemistry
  • Proceedings of the National Academy of Sciences
  • Angewandte Chemie
  • Zenodo (CERN European Organization for Nuclear Research)
  • Angewandte Chemie International Edition

Best Publications

  • Extraction of glycerol from biodiesel into a eutectic based ionic liquid

    Andrew P. Abbott;Paul M. Cullis;Manda J. Gibson;Robert C. Harris

  • Crystal Structure of Mycobacterium tuberculosis Catalase-Peroxidase.

    Thomas Bertrand;Nigel A.J. Eady;Jamie N. Jones;Jesmin

  • Mechanisms of compound I formation in heme peroxidases.

    Alexander N.P. Hiner;Emma L. Raven;Roger N.F. Thorneley;Francisco Garcı́a-Cánovas

  • Crystal Structure of the Ascorbate Peroxidase-Ascorbate Complex

    Katherine H. Sharp;Martin Mewies;Peter C.E. Moody;Emma Lloyd Raven

  • The Nature and Reactivity of Ferryl Heme in Compounds I and II

    Peter C. E. Moody;Emma L. Raven

  • Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase

    Cecilia M. Casadei;Andrea Gumiero;Clive L. Metcalfe;Emma J. Murphy

  • Kinetic study of the inactivation of ascorbate peroxidase by hydrogen peroxide.

    Alexander N. P. Hiner;José Neptuno Rodríguez-López;Marino B. Arnao;Emma Lloyd Raven

  • Regulation of intracellular heme trafficking revealed by subcellular reporters.

    Xiaojing Yuan;Nicole Rietzschel;Hanna Kwon;Ana Beatriz Walter Nuno

  • Nature of the Ferryl Heme in Compounds I and II

    Andrea Gumiero;Clive L. Metcalfe;Arwen R. Pearson;Emma Lloyd Raven

  • Structure and Reaction Mechanism in the Heme Dioxygenases

    Igor Efimov;Jaswir Basran;Sarah J. Thackray;Sandeep Handa

  • Substrate binding and catalytic mechanism in ascorbate peroxidase: evidence for two ascorbate binding sites.

    Latesh Lad;Martin Mewies;Emma Lloyd Raven

  • Oxidation of L-tryptophan in biology: a comparison between tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase.

    Sara A. Rafice;Nishma Chauhan;Igor Efimov;Jaswir Basran

  • The tuberculosis prodrug isoniazid bound to activating peroxidases.

    Clive L. Metcalfe;Isabel K. Macdonald;Emma J. Murphy;Katherine A. Brown

  • Redox-linked domain movements in the catalytic cycle of cytochrome p450 reductase.

    Wei Cheng Huang;Jacqueline Ellis;Peter C.E. Moody;Emma L. Raven

  • Understanding functional diversity and substrate specificity in haem peroxidases: what can we learn from ascorbate peroxidase?

    Emma Lloyd Raven

  • The mechanism of formation of N-formylkynurenine by heme dioxygenases.

    Jaswir Basran;Igor Efimov;Nishma Chauhan;Sarah J. Thackray

  • A Kinetic, Spectroscopic, and Redox Study of Human Tryptophan 2,3-Dioxygenase†

    Jaswir Basran;Sara A. Rafice;Nishma Chauhan;Igor Efimov

  • Redox and spectroscopic properties of human indoleamine 2,3-dioxygenase and a His303Ala variant: implications for catalysis.

    Nektaria D. Papadopoulou;Martin Mewies;Kirsty J. McLean;Harriet E. Seward

  • An analysis of substrate binding interactions in the heme peroxidase enzymes: a structural perspective.

    Andrea Gumiero;Emma J. Murphy;Clive L. Metcalfe;Peter C.E. Moody

  • Detection of a tryptophan radical in the reaction of ascorbate peroxidase with hydrogen peroxide

    Alexander N. P. Hiner;Jesús I. Martínez;Marino B. Arnao;Manuel Acosta

Frequent Co-Authors

Gordon C. K. Roberts
Gordon C. K. Roberts University of Leicester
Michael R. F. Lee
Michael R. F. Lee Harper Adams University
Stephen K Chapman
Stephen K Chapman University of Edinburgh
Andrew W. Munro
Andrew W. Munro University of Manchester
Andrew J. Thomson
Andrew J. Thomson University of East Anglia
Myles R. Cheesman
Myles R. Cheesman University of East Anglia
Anne L. Martel
Anne L. Martel University of Toronto
Marino B. Arnao
Marino B. Arnao University of Murcia
Francisco García-Cánovas
Francisco García-Cánovas University of Murcia

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