World's Best Scientists 2026 revealed!

D-Index & Metrics

Chemistry

D-Index
98
Citations
39188
World Ranking
1381
National Ranking
534

Research.com Recognitions

  • 2005 - Fellow of the American Association for the Advancement of Science (AAAS)

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Gene
  • Amino acid

Thomas L. Poulos mainly investigates Stereochemistry, Heme, Cytochrome, Active site and Biochemistry. His Stereochemistry study combines topics from a wide range of disciplines, such as Ligand, Cytochrome P450, Hydrogen bond, Protein structure and Binding site. His Heme study incorporates themes from Peroxidase, Tetrahydrobiopterin and Histidine.

His Cytochrome research integrates issues from Camphor, Mutant, Substrate, Hemeprotein and Cytochrome P450 reductase. His biological study spans a wide range of topics, including Crystallography, Catalytic cycle, Molecular model and Ligand. In the field of Biochemistry, his study on Nitric oxide synthase and Fatty acid overlaps with subjects such as GUCY1B3 and GUCY1A3.

His most cited work include:

  • High-resolution crystal structure of cytochrome P450cam. (1140 citations)
  • The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450. (644 citations)
  • Heme Enzyme Structure and Function (580 citations)

What are the main themes of his work throughout his whole career to date?

Thomas L. Poulos mostly deals with Stereochemistry, Heme, Biochemistry, Active site and Cytochrome. In his study, Photochemistry is inextricably linked to Cytochrome c peroxidase, which falls within the broad field of Stereochemistry. His research investigates the connection with Heme and areas like Protein structure which intersect with concerns in Helix.

His Active site research is multidisciplinary, incorporating elements of Substrate and Hydrogen bond. His research integrates issues of Hydroxylation, Mutant, Cytochrome P450, Electron transfer and Cytochrome P450 reductase in his study of Cytochrome. The various areas that Thomas L. Poulos examines in his Electron transfer study include Redox and Electron transport chain.

He most often published in these fields:

  • Stereochemistry (56.81%)
  • Heme (36.03%)
  • Biochemistry (29.10%)

What were the highlights of his more recent work (between 2012-2020)?

  • Stereochemistry (56.81%)
  • Biochemistry (29.10%)
  • Active site (21.94%)

In recent papers he was focusing on the following fields of study:

Thomas L. Poulos mainly focuses on Stereochemistry, Biochemistry, Active site, Heme and Nitric oxide synthase. His Stereochemistry research includes themes of Oxidoreductase, Mutant, Cytochrome, Redox and Binding site. Thomas L. Poulos usually deals with Active site and limits it to topics linked to Molecule and Crystal structure.

In his work, Docking is strongly intertwined with Biophysics, which is a subfield of Heme. His studies deal with areas such as Bacillus anthracis and Microbiology as well as Nitric oxide synthase. His research in Crystallography intersects with topics in Ligand and Cytochrome c peroxidase.

Between 2012 and 2020, his most popular works were:

  • Heme Enzyme Structure and Function (580 citations)
  • Structural Basis for Effector Control and Redox Partner Recognition in Cytochrome P450 (113 citations)
  • Understanding the mechanism of cytochrome P450 3A4: recent advances and remaining problems (84 citations)

In his most recent research, the most cited papers focused on:

  • Enzyme
  • Gene
  • Amino acid

His primary scientific interests are in Stereochemistry, Biochemistry, Active site, Nitric oxide synthase and Binding site. The concepts of his Stereochemistry study are interwoven with issues in Oxidoreductase, Redox, Protein structure and Plasma protein binding. His Oxidoreductase research focuses on Mutant and how it relates to Cytochrome, Cyanide and Hydrogen bond.

His Biochemistry study deals with Nitric oxide intersecting with Cell type, Melanocyte, Metastasis, Cancer research and Melanoma. His work carried out in the field of Active site brings together such families of science as Catalytic cycle, Hemeprotein, Crystal structure and Porphyrin. His Heme research includes elements of Peroxidase, Biophysics, Docking and Enzyme structure.

Best Publications

  • High-resolution crystal structure of cytochrome P450cam.

    Thomas L. Poulos;Barry C. Finzel;Andrew J. Howard

  • Heme Enzyme Structure and Function

    Thomas L. Poulos

  • The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450.

    T L Poulos;B C Finzel;I C Gunsalus;G C Wagner

  • The stereochemistry of peroxidase catalysis.

    T L Poulos;J Kraut

  • Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution.

    B C Finzel;T L Poulos;J Kraut

  • Crystal structure of horseradish peroxidase C at 2.15 A resolution.

    Michael Gajhede;David J. Schuller;Anette Henriksen;Andrew T. Smith

  • Engineered ascorbate peroxidase as a genetically encoded reporter for electron microscopy

    Jeffrey D Martell;Thomas J Deerinck;Yasemin Sancak;Yasemin Sancak;Thomas L Poulos

  • Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center.

    C.S Raman;Huiying Li;Pavel Martásek;Vladimir Král

  • Crystal structure of substrate-free Pseudomonas putida cytochrome P-450.

    Thomas L. Poulos;Barry C. Finzel;Andrew J. Howard

  • Crystal structure of cytochrome P450 14α-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors

    Larissa M. Podust;Thomas L. Poulos;Michael R. Waterman

  • The use of an imaging proportional counter in macromolecular crystallography

    A. J. Howard;G. L. Gilliland;Barry C Finzel;T. L. Poulos

  • Structure of a cytochrome P450-redox partner electron-transfer complex.

    Irina F. Sevrioukova;Huiying Li;Hong Zhang;Julian A. Peterson

  • The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid

    Huiying Li;Thomas L. Poulos

  • The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid.

    Munirathinam Sundaramoorthy;James Terner;Thomas L Poulos

  • Structure of cytochrome P450eryF involved in erythromycin biosynthesis

    Jill R. Cupp-Vickery;Thomas L. Poulos

  • Crystallographic refinement of lignin peroxidase at 2 A.

    T.L. Poulos;S.L. Edwards;H. Wariishi;M.H. Gold

  • The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution.

    Munirathinam Sundaramoorthy;K. Kishi;M. H. Gold;T. L. Poulos

  • The crystal structure of cytochrome c peroxidase.

    T L Poulos;S T Freer;R A Alden;S L Edwards

  • A hypothetical model of the cytochrome c peroxidase . cytochrome c electron transfer complex.

    T.L. Poulos;J. Kraut

  • Crystal structure of human heme oxygenase-1

    Schuller Dj;Wilks A;Wilks A;Ortiz de Montellano Pr;Poulos Tl

Frequent Co-Authors

Huiying Li
Huiying Li University of California, Irvine
Richard B. Silverman
Richard B. Silverman Northwestern University
Pavel Martásek
Pavel Martásek Charles University
Paul R. Ortiz de Montellano
Paul R. Ortiz de Montellano University of California, San Francisco
Stephen G. Sligar
Stephen G. Sligar University of Illinois at Urbana-Champaign
Michael H. Gold
Michael H. Gold Oregon Health & Science University
Chander Raman
Chander Raman University of Alabama at Birmingham
Joseph Kraut
Joseph Kraut University of California, San Diego
Ilia G. Denisov
Ilia G. Denisov University of Illinois at Urbana-Champaign

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