J
John S. Olson
Researcher at Rice University
Publications - 255
Citations - 19036
John S. Olson is an academic researcher from Rice University. The author has contributed to research in topics: Heme & Myoglobin. The author has an hindex of 73, co-authored 254 publications receiving 18309 citations. Previous affiliations of John S. Olson include Graduate University for Advanced Studies & Case Western Reserve University.
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Watching a Protein as it Functions with 150-ps Time-Resolved X-ray Crystallography
Friedrich Schotte,Manho Lim,Timothy A. Jackson,Aleksandr V. Smirnov,Jayashree Soman,John S. Olson,George N. Phillips,Michael Wulff,Philip A. Anfinrud +8 more
TL;DR: Time-resolved mid-infrared spectroscopy of flash-photolyzed L29F MbCO revealed a short-lived CO intermediate whose 140-ps lifetime is shorter than that found in wild-type protein by a factor of 1000.
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Mechanisms of Ligand Recognition in Myoglobin
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Mechanism of NO-Induced Oxidation of Myoglobin and Hemoglobin†
Raymund F. Eich,Tiansheng Li,Douglas D. Lemon,Daniel H. Doherty,Shawn R. Curry,Jacqueline F. Aitken,Antony J. Mathews,Kenneth A. Johnson,Robert D. Smith,George N. Phillips,John S. Olson +10 more
TL;DR: The results provide a protein engineering strategy for reducing hypertensive events caused by extracellular hemoglobin-based O2 carriers by examining the effects of Phe(B10) and Phe (E11) substitutions on the rates of NO-induced oxidation of the alpha and beta subunits in recombinant human hemoglobin.
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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,Timothy J. Fattor,John S. Olson,Douglas D. Lemon,Douglas D. Lemon +7 more
TL;DR: The results suggest that the rapid reactions of oxy- and deoxyhemoglobin with nitric oxide are the fundamental cause of the hypertension and Hemoglobins with decreased NO-scavenging activity may be more suitable for certain therapeutic applications than those that cause depletion of Nitric oxide.
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High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin.
TL;DR: The high-resolution crystal structures of the Gly64, Val64, Leu64, Thr64 and Gln64 mutants in several liganded forms provide key insights into the mechanisms of ligand binding and discrimination in myoglobin.