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Chemistry

D-Index
90
Citations
25192
World Ranking
2104
National Ranking
764

Overview

John S. Olson is affiliated with Rice University in the United States. Their research centers on multiple areas at the intersection of biochemistry, molecular biology, and medicine, with an additional focus on economics, econometrics, and finance.

Their main fields of study include:

  • Biochemistry, Genetics and Molecular Biology
  • Medicine
  • Economics, Econometrics and Finance

Subfields of Olson's research encompass:

  • Cell Biology
  • Economics and Econometrics
  • Pediatrics, Perinatology and Child Health
  • Molecular Biology
  • Genetics

Olson has contributed extensively to topics such as:

  • Hemoglobin structure and function
  • Neonatal Health and Biochemistry
  • Heme Oxygenase-1 and Carbon Monoxide
  • Fiscal Policy and Economic Growth
  • Taxation and Compliance Studies
  • Iron Metabolism and Disorders
  • Nitric Oxide and Endothelin Effects

Their frequently published venues include:

  • Biophysical Journal
  • Journal of Biological Chemistry
  • Molecular Aspects of Medicine
  • Journal of Inorganic Biochemistry
  • International Tax and Public Finance

Notable recent publications by Olson and associates are:

  • "Kinetic mechanisms for O2 binding to myoglobins and hemoglobins," 2021, Molecular Aspects of Medicine
  • "The Interplay between Molten Globules and Heme Disassociation Defines Human Hemoglobin Disassembly," 2020, Biophysical Journal
  • "Mechanisms of nitric oxide reactions with globins using mammalian myoglobin as a model system," 2022, Journal of Inorganic Biochemistry
  • "How taxes affect growth: evidence from cross-country panel data," 2025, International Tax and Public Finance
  • "Molten Globules and Metallocofactor Disassociation Steer Human Hemoglobin Disassembly," 2020, Biophysical Journal

Olson has collaborated frequently with a number of researchers in their field, including:

  • David A. Case
  • G.N. Phillips
  • Laura Kawano
  • Joel Slemrod
  • Meng Hsuan Hsieh

Best Publications

  • Watching a Protein as it Functions with 150-ps Time-Resolved X-ray Crystallography

    Friedrich Schotte;Manho Lim;Timothy Albert Jackson;Aleksandr V. Smirnov

  • Mechanisms of Ligand Recognition in Myoglobin

    Barry A. Springer;Stephen G. Sligar;John S. Olson;George N. Jr. Phillips

  • Mechanism of NO-Induced Oxidation of Myoglobin and Hemoglobin†

    Raymund F. Eich;Tiansheng Li;Douglas D. Lemon;Daniel H. Doherty

  • Rate of reaction with nitric oxide determines the hypertensive effect of cell-free hemoglobin

    Daniel H. Doherty;Michael P. Doyle;Shawn R. Curry;Rita J. Vali

  • The mechanism of autooxidation of myoglobin.

    R E Brantley;S J Smerdon;A J Wilkinson;E W Singleton

  • High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin.

    Michael L. Quillin;Robert M. Arduini;John S. Olson;George N. Phillips

  • The Mechanism of Action of Xanthine Oxidase

    John S. Olson;David P. Ballou;Graham Palmer;Vincent Massey

  • Structural Determinants of the Stretching Frequency of CO Bound to Myoglobin

    Tiansheng Li;Michael L. Quillin;George N. Phillips;John S. Olson

  • Mapping the pathways for O2 entry into and exit from myoglobin.

    Emily E. Scott;Quentin H. Gibson;John S. Olson

  • Kinetic Pathways and Barriers for Ligand Binding to Myoglobin

    John S. Olson;George N. Phillips

  • No scavenging and the hypertensive effect of hemoglobin-based blood substitutes.

    John S. Olson;Erin W. Foley;Corina Rogge;Ah Lim Tsai

  • Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin. Site-directed mutagenesis of the distal histidine.

    B. A. Springer;K. D. Egeberg;Stephen G. Sligar;R. J. Rohlfs

  • Two hemoglobin genes in Arabidopsis thaliana: the evolutionary origins of leghemoglobins.

    B Trevaskis;R A Watts;C R Andersson;D J Llewellyn

  • The effects of amino acid substitution at position E7 (residue 64) on the kinetics of ligand binding to sperm whale myoglobin.

    Ronald J. Rohlfs;Antony J. Mathews;Theodore E. Carver;John S. Olson

  • Myoglobin discriminates between O2, NO, and CO by electrostatic interactions with the bound ligand

    J. S. Olson;George N. Phillips

  • Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis.

    D M Miller rd;J S Olson;J W Pflugrath;F A Quiocho

  • The role of the distal histidine in myoglobin and haemoglobin

    John S. Olson;Antony J. Mathews;Ronald J. Rohlfs;Barry A. Springer

  • The Association Rate Constant for Heme Binding to Globin Is Independent of Protein Structure

    Mark S. Hargrove;Doug Barrick;John S. Olson

  • BOUND CO IS A MOLECULAR PROBE OF ELECTROSTATIC POTENTIAL IN THE DISTAL POCKET OF MYOGLOBIN

    George N. Phillips;Miguel L. Teodoro;Tiansheng Li;Benjamin Smith

  • The rate of oxygen uptake by human red blood cells

    J T Coin;J S Olson

  • His64(E7)→Tyr apomyoglobin as a reagent for measuring rates of hemin dissociation

    M S Hargrove;E W Singleton;M L Quillin;L A Ortiz

Frequent Co-Authors

George N. Phillips
George N. Phillips Rice University
Quentin H. Gibson
Quentin H. Gibson Rice University
Mark S. Hargrove
Mark S. Hargrove Iowa State University
Masao Ikeda-Saito
Masao Ikeda-Saito Tohoku University
G. Ulrich Nienhaus
G. Ulrich Nienhaus Karlsruhe Institute of Technology
Graham Palmer
Graham Palmer Rice University
Mitchell J. Weiss
Mitchell J. Weiss St. Jude Children's Research Hospital
Sylvia Dewilde
Sylvia Dewilde University of Antwerp
Luc Moens
Luc Moens University of Antwerp
Anthony J. Wilkinson
Anthony J. Wilkinson University of York

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