Rice University
BioSciences at Rice

John Olson

Ralph and Dorothy Looney Professor Emeritus of BioSciences

Our laboratory has been using biochemical, biophysical, chemical, and chemical engineering approaches to examine the fundamental processes involved in oxygen transport and storage in mammalian circulatory systems. We are directing two major research programs, one involving basic molecular biophysics and the other involving the design of O2 delivery pharmaceuticals. (1) Dynamics of O2 binding to heme proteins. The roles of specific amino acids and structural motifs in regulating the kinetics and affinity of O2 binding and the resistance of myoglobins olson_workand hemoglobins to denaturation are being identified by: UV-visible, vibrational, CD, fluorescence, and NMR spectroscopies; rapid mixing and ultrafast laser photolysis kinetic techniques; X-ray crystallography, and various computational methods. (2) The design of Hb-based blood substitutes. Rational and random mutagenesis techniques are being used to optimize seven key properties of extracellular hemoglobin: (a) moderately low O2 affinity and high cooperativity, (b) discrimination against CO binding, (c) high rates of O2 exchange, (d) low rates of reaction with NO, (e) resistance to autooxidation and reactions with H2O2, (f) high affinity for heme, and (g) resistance to denaturation. Our mechanisms are being used by Baxter Hemoglobin Therapeutics, Boulder, CO (formerly Somatogen, Inc.) to develop second generation blood substitutes.

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Sjodt, M., Macdonald, R., Marshall, J. D., Clayton, J., Olson, J. S., Phillips, M., Gell, D. A., Wereszczynski, J. and Clubb, R. T The Energetics of Underlying Hemin Extraction from the α-subunit of Human Hemoglobin by Staphylococcus aureus,.  J. Biol. Chem., ePUB ahead of printing 2018/March 14: PMID: 29540481

Cardenas, A. S. B. Samuel, P. P. Olson, J. S. 2017 Military Supplement: Current Challenges in the Development of Acellular Hemoglobin Oxygen Carriers by Protein Engineering.  Shock, ePUB ahead of printing 2017: PMID 29112633

Strader, M. B. Bangle, R. Parker Siburt, C. J. Varnado, C. L. Soman, J. Benitez Cardenas, A. S. Samuel, P. P. Singleton, E. W. Crumbliss, A. L. Olson, J. S. Alayash, A. I. Engineering oxidative stability in human hemoglobin based on the Hb providence (betaK82D) mutation and genetic cross-linking.  Biochem J, 474 2017: 4171-4192

Bisse, E. Schaeffer-Reiss, C. Van Dorsselaer, A. Alayi, T. D. Epting, T. Winkler, K. Benitez Cardenas, A. S. Soman, J. Birukou, I. Samuel, P. P. Olson, J. S. Hemoglobin Kirklareli (alpha H58L), a New Variant Associated with Iron Deficiency and Increased CO Binding.  J. Biol. Chem., 292 2017: 2542-2555

Samuel, P. P. Ou, W. C. Phillips, G. N., Jr. Olson, J. S. Mechanism of Human Apohemoglobin Unfolding.  Biochemistry, 56 2017: 1444-1459

Sjodt, M., Macdonald, R., Spirig, T., Chan, A. H., Dickson, C. F., Fabian, M., Olson, J. S., Gell, D. A., and Clubb, R. T. The PRE-Derived NMR Model of the 38.8 kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests that it Adaptively Recognizes Human Hemoglobin.  J. Mol. Biol., 428 2016: 1107–1129

Esquerra, R.M., Bibi, B.M., Tipgunlakant, P., Birukou, I., Soman, J.,Olson,J.S., Kliger, D.S., Goldbeck, R. A. The Role of Heme Pocket Water in Allosteric Regulation of Ligand Reactivity in Human Hemoglobin.  Biochemsitry, 55 2016: 4005-17

Samuel, P. P., Phillips, G. N. Jr., Smith, L. P., and Olson, J. S. Apoglobin stability is the major factor governing both cell-free and in vivo expression of holomyoglobin.  J. Biol. Chem., 290 2015: 23479-95

Mueller, C., Marx, A., Epp, S. W., Zhong, Y., Kuo, A., Balo, A. R., Soman, J., Schotte, F., Lemke, H. T., Owen, R. L., Pai, E. F., Pearson, A. R., Olson, J. S., and Anfinrud, P.A., Ernst, O. P., and Miller, R. J. D. Fixed target matrix for femtosecond time-resolved and in situ serial micro-crystallography.  Structural Dynamics, 2 2015: 054302-1 to 15

Da, Q., Teruya, M., Guchhait, P., Teruya, J., Olson, J.S., and Cruz, M.A. Free Hemoglobin modulates von Willebrand factor-mediated platelet adhesion in vitro: implications on circulatory devices.  Blood, 126 2015: 2338-2341

Strader, M. B., Hicks, W. A., Kassa, T., Singleton, E. W., Soman, J. Olson, J. S., Weiss, M. J., Mollan, T., L., Wilson, M. T., and Alayash, A A Post-translational transformation of methionine to aspartate is catalyzed by heme iron and driven by peroxide: A novel subunit specific mechanism in hemoglobin.  J. Biol. Chem., 289 2014: 22342-57

Hastings, J. W. and Olson, J. S. Quentin H. Gibson 1918-2011.  National Academy of Sciences Biographical Memoirs 2014: 41 pages. http://www.nasonline.org/member-directory/biographical-memoirs.html Free Access

Olson, J.S. and Gutfreund, H. Quentin H. Gibson: December 9, 1918 – March 16, 2011.  Biographical Memoirs of Fellows of the Royal Society, Royal Society of London, 60 2014: 169-210

Mollan, T. L., Jia, Y., Banerjee, S., Wu, G., Kreulen, T., Tsai, A-L., Olson, J. S., Crumbliss, A. L., and Alayash, A. I. Redox Properties of Human Hemoglobin in Complex with Fractionated Dimeric and Polymeric Human Haptoglobin.  Free Rad. Biol. Med., 69 2014: 265-277

Dickson, C.F., Rich, A. M., D’Avigdor, W. M. H., Collins, D., Lowry, J. Mollan, T. L., Khandros, E., Olson, J. S., Weiss, M. J., Mackay, J. P., Lay, P. A., and Gell, D. A. α-Hemoglobin Stabilizing Protein Perturbs the Proximal Heme Pocket of Oxy-α-Hemoglobin and Weakens the Iron-Oxygen Bond.  J. Biol. Chem., 288 2013: 19986-20001

Mollan, T. L., Banerjee, S., Wu, G., Parker Siburt, C. J., Tsai, A-L., Olson, J. S., Weiss, M. J., Crumbliss, A. L., and Alayash, A. I. Alpha-Hemoglobin Stabilizing Protein (AHSP) Markedly Decreases the Redox Potential and Reactivity of α Subunits of Human HbA with Hydrogen Peroxide.  J. Biol. Chem., 288 2013: 4288-98

Nienhaus, K., Olson, J.S., and Nienhaus, G.U. An Engineered Heme-Copper Center in Myoglobin: CO Migration and Binding.  Biochim. Bioophys. Acta. Proteins, 1834 2013: 1824-31

Varnado, C. L., Mollan, T. L., Birukou, I., Smith, B. J. Z., Henderson, D. P., and Olson, J. S. Development of Recombinant Hemoglobin-Based Oxygen Carriers.  Antioxid. Redox Signal.: Forum Review, 18 2013: 2314-28

Boechi, L., Arrar, M., Marti, M. A., Olson, J. S., Roitberg, and A. E., Estrin, D. A. Hydrophobic effect drives oxygen uptake in myoglobin via histidine E7.  J. Biol. Chem., 288 2013: 6754-62

Schotte, F., Hyun Sun Cho, H. S.,.Soman, J., Wulff, M., Olson, J. S., and Anfinrud, P. A. Real-time tracking of CO migration and binding in the alpha and beta subunits of human hemoglobin via 150 ps time-resolved Laue crystallography.  Chem. Physics, 422 2013: 98-106

Zheng, W., Olson, J. S., Vakharia, V., and Tao, Y. J. The crystal structure and RNA-binding of an orthomyxovirus nucleoprotein..  Plos Pathogens, 9 2013: e1003624

Tsai, A. L., Berka, V., Martin, E., and Olson, J. S. A "Sliding-Scale Rule" for Selectivity between NO, CO and O2 by Heme Protein Sensors.  Biochemistry, 51 2012: 172-86

Salter, M. D., Blouin, G. C., Singleton, E. W., Dewilde, S., Moens, L., Pesce, A., Nardini, M., Bolognesi, M., and Olson, J. S. Determination of Ligand Pathways in Globins: Apolar Tunnels versus Polar Gates.  J. Biol. Chem., 287 2012: 33163-33178

Ekworomadu, M., Poor, C.B., Owens C.P., Balkabasi, M., Fabian, M., Olson, J. S., Murphy, F., Balkabasi, E., Honsa, E., He, C., Celia W. Goulding, C.W., and Maresso, A. W. Differential Function of Lip Residues in the Mechanism and Biology of an Anthrax Hemophore.  PloS Pathogens, 8(3) 2012: e1002559

Mollan, T. L., Abraham, B., Strader, M. B., Jia, Y. Lozier, J. N., Olson, J. S., and Alayash, A. I. Familial Secondary Erythrocytosis Due to Increased Oxygen Affinity Is Caused by Destabilization of the T State of Hemoglobin Brigham (alpha2beta2(2Pro100Leu)).  Protein Sci., 287 2012: 11338-11350

Tsai, A-L., Martin, E., Berka, V., and Olson, J. S. How do heme-protein sensors exclude oxygen: Lessons learned from cytochrome c', Ns H-NOX and soluble guanylyl cyclase.  Antioxid. Redox Signal.: Forum Review, 17 2012: 1246-63

Khandros, E., Mollan, T. L., Yu, X., Wang, X., Yao, Y., D'Souza, J. D., Gell, D. A., Olson, J. S., and Weiss, M. J. Insights Into Hemoglobin Assembly Through In Vivo Mutagenesis of Alpha-Hemoglobin Stabilizing Protein.  J. Biol. Chem., 287 2012: 11325-11337

Mollan, T. L., Khandros, E., Weiss, M. J., and Olson, J. S. The Kinetics of α-Globin Binding to α-Hemoglobin Stabilizing Protein (AHSP) Indicate Preferential Stabilization of a Hemichrome Folding Intermediate.  J. Biol. Chem., 287 2012: 11338-11350

Birukou, I., Soman, J., and Olson, J. S. Blocking the Gate to Ligand Entry in Human Hemoglobin.  J. Biol. Chem., 286 2011: 10515-52

Crowley, M. A., Mollan, T. L., Abdulmalik, O. Y., Butler, A. D., Goodwin, E. F., Sarkar, A. Stolle, C. A., Gow, A. J., Olson, J. S., Weiss, M. J. Hemoglobin Toms River – A Variant Causing Neonatal Cyanosis and Anemia..  New Eng. J. Med, 364 2011: 1837-43

Pesce, A., Nardini, M., Dewilde, S., Capece, L., Martí, M.A., Congia, S., Salter, M.D., Blouin, G.C., Estrin,D. A., Ascenzi, P., Moens, L., Bolognesi, M., and Olson, J.S. Ligand Migration in the Apolar Tunnel of Cerebratulus lacteus Mini-Hemoglobin..  J. Biol. Chem., 286 2011: 5347-58

Birukou, I., Maillett, D. H., Birukova, A., and Olson, J. S. Modulating Distal Cavities in the alpha and beta Subunits of Human HbA Reveals the Primary Ligand Migration Pathway.  Biochemistry, 50 2011: 7361-74

Lukianova-Hleb, E. Y., Oginsky, A. O., Olson, J. S., and Lapotko, D. O. Short laser pulse-induced irreversible photothermal effects in red blood cells.  Lasers in Surgery & Medicine, 43 2011: 249-60

Honsa, E. S., Fabian, M., Cardenas, A. M., Olson, J. S., and Maresso, A. W. The five near-iron transporter (NEAT) domain anthrax hemophore, IsdX2, scavenges heme from hemoglobin and transfers heme to the surface protein IsdC.   J. Biol. Chem., 286 2011: 33652-60

Blouin, G., Schweers, R. L., and Olson, J.S. Alkyl Isocyanides Serve as Transition State Analogs for Ligand Entry and Exit in Myoglobin.  Biochemistry, 49 2010: 4987-4997

Tarlovsky, Y., Fabian, M., Olson, J.S., and Maresso, A. W. An S-Layer Homology Protein Mediates Heme Delivery to the Isd system in the Bacillus anthracis.  J. Bacteriology, 192 2010: 3503-3511

Pena, M., Davlieva, M., Olson, J. S. Bennett, M., and Shamoo, Y. Evolutionary fates within a microbial population highlight an essential role for reversible and irreversible protein folding during natural selection.  Molecular Systems Biology, on-line journal 2010: Article 387

Culbertson, D. and Olson, J.S. Folding and assembly of myoglobins and hemoglobins.  Protein Folding and Metal Ions: Mechanisms, Biology, and Disease (edited Gomes, C.M. and Wittung-Stafshede, P.), Taylor & Francis Books, Inc., Chapter 6 2010, October : 97-122

Tsai, A-L., Berka, V., Martin, F., Ma, X., van den Akker, F., Fabian, M., and Olson, J. S. Is Nostoc H-NOX a Gaseous Sensor or a Redox Switch?.  Biochemistry, 49 2010: 6587-6599

Esquerra, R. M., Lopez-Pena, I., Tipgunlakant, P., Birukou, I., Nguyen, R. L., Soman, J., Olson, J.S., Kliger, D.S., and Goldbeck, R. A. Kinetic Spectroscopy of Heme Hydration and Ligand Binding in Myoglobin and Isolated Hemoglobin Chains: An Optical Window into the Functional Dynamics of Water in the Heme Pocket.  Physical Chemistry Chemical Physics, 12 2010: 10270-8

Sodatova, A.V., Ibrahim, M., Olson, J.S., and Spiro, T.G. New light on NO bonding in Fe(III) heme proteins from resonance Raman spectroscopy and DFT modeling.  J Amer Chem Soc, 132 2010: 4614-4625

Smith, R. D., Blouin, G., Johnson, K. A., Phillips, G.N.Jr., and Olson, J.S. Straight-Chain Alkyl Isocyanides Open the Distal Histidine Gate in Crystal Structures of Myoglobin.  Biochemistry, 49 2010: 4977-4986

Birukou, I., Schweers, R. L., and Olson, J. S. The Distal Histidine Stabilizes Bound O2 and Acts as Gate for Ligand Entry n Both Subunits of Human HbA.  J. Biol. Chem., 285 2010: 8840-54

Culbertson, D. S. and Olson, J. S. The Role of Heme in the Unfolding and Assembly of Myoglobin.  Biochemistry, 49 2010: 6052-6063

Blouin, G., and Olson, J.S. The Stretching Frequencies of Bound Alkyl Isocyanides Indicate Two Distinct Ligand Orientations within the Distal Pocket of Myoglobin.  Biochemistry, 49 2010: 4968-4976

Bianchetti, C. M., Blouin, G. C., Bitto, E., Olson, J. S., and Phillips, G. N. Jr. The Structure and NO Binding Properties of the Nitrophorin-like Heme-binding Protein from Arabidopsis thaliana gene locus Atlg79260.1.  Proteins, 78 2010: 917-931

Mollan, T., Yu, X., Weiss, M.J., and Olson, J.S. The role of alpha-hemoglobin stabilizing protein in redox chemistry..  Antioxidants and Redox Signaling, 12 2010: 219-231

Yu, X., Mollan, T. L., Butler, A., Gow, A. J., Olson, J. S., and Weiss M. J. Analysis of Human α Globin Gene Mutations that Impair Binding to the Alpha Hemoglobin Stabilizing Protein (AHSP).  Blood, 113 2009: 5961 - 5969

Asmundson, A. L., van der Walde, A., Lin, D. H, Olson, J. S., and Anthony-Cahill, S. J. Co-Expression of Human α- and Circularly Permuted β-Globins Yields a Hemoglobin with Normal R state but modified T state Properties.  Biochemistry, 48 2009: 5456-5465

Smagghe, B. J., Hoy, J. A., Percifield, R., Kundu, S., Hargrove, M. S., Sarath, G., Hilbert, J-L., Watts, R. A., Dennis, E. S., Peacock, W. J., Dewilde, S., Moens, L., Blouin, G. C., Olson, J. S., and Appleby, C. Correlations between Oxygen Affinity and Sequence Classifications of Plant Hemoglobins.  Biopolymers, 91 2009: 1083-1096

Fabian, M., Solomaha, E., Olson, J.S., and Maresso, A. Heme transfer to the bacterial cell envelope occurs via a secreted hemophore in the gram-positive pathogen Bacillus anthracis.  J Biol Chem, 284 2009: 32138-32146

Golbeck, R.S., Pillsbury, M.L., Jensen, R.A., Mendoza, J.L., Nguyen, R.L., Olson, J.S., Soman, J., Kliger, D.S., and Esquerra, R.M. Optical detection of disordered water within a protein cavity.  J Amer Chem Soc, 131 2009: 12265-12272

Aranda, R. 4th, Cai, H., Worley, C.E., Levin, E.J., Li, R., Olson, J.S., Phillips, G.N. Jr., and Richards, M.P. Structural analysis of bovine, trout IV, and perch hemoglobin: Effects of the heme pocket environment on autooxidation and hemin loss rates.  Proteins, 75 2009: 217-230

Hussain, F., Olson, J.S., and Wittung-Stafshede, P. Conserved residues modulate copper release in human copper chaperone Atox1.  Proceedings of the National Academy of Sciences, USA, 105 2008: 11158-11163

Villarreal, D.M., Phillipds, C.L., Kelley, A.M., Villarreal, S., Villaloboz, A., Hernandez, P., Olson, J.S., and Henderson, D.P. Enhancement of recombinant hemoglobin production in Escherichia coli BL21(DE3) containing the Plesiomonas shigelloides heme transport system.  Appl. Environ. Microbiol., 74 2008: 5854-5856

Graves, P.E, Henderson, D.P., Horsman, J.M., Solomon, B.J., and Olson, J.S. Enhancing stability and expression of recombinant human hemoglobin in E. coli: Progress in the development of a recombinant HBOC source.  Biochim. Biophys. Acta, 1784 2008: 1471-1479

Maillett, D.H., Simplaceanu, V., Shen, T.J., Ho, N.T., Olson, J.S. and Ho, C. Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin.  Biochemistry, 47 2008: 10551-10563

Zhu, H., Xie, G., Liu, M., Olson, J.S., Fabian, M., Dooley, D.M., and Lei, B. Pathway for heme uptake from human methemoglobin by the iron-regulated surface determinants system of Staphylococcus aureus.  J. Biol. Chem., 283 2008: 18450-18460

Salter, M.D., Nienhaus, K., Nienhaus, G.U., Dewilde, S., Moens, L., Pesce, A., Nardini, M., Bolognesi, M., and Olson, J.S. The apolar channel in cerebratulus lacteus hemoglobin is the route for O2 entry and exit.  J. Biol. Chem., 283 2008: 35689-35702

Ran, Y., Zhu, H., Liu, M., Fabian, M., Olson, J.S., Aranda, R. IV., Phillips, G.N., Jr., Dooley, D.M., and Lei, B. Bis-methionine coordination in Shp facilitates rapid heme transfer to HtsA of the HtsABC transporter in a plug-in mechanism.  J. Biol. Chem., 282 2007: 31380-31388

Aranda, R., Worley, C.E., Liu, M., Bitto, E., Cates, M.S., Olson, J.S., Lei, B., and Phillips, G.N. Jr. Bis-methionyl coordination and heme stacking in the crystal structure of the heme-binding domain of the streptococcal cell surface protein Shp.  J. Mol. Biol., 374 2007: 374-383

Olson, J.S., Soman, J., and Phillips, G.N. Jr, Ligand pathways in myoglobin: A review of Trp cavity mutations.  IUBMB Life, 59 2007: 552-562

Olson, J.S., and Ghosh, A. Mammalian myoglobin as a model for understanding ligand affinities and discrimination in heme proteins.  Chapter 1, The Smallest Biomolecules: Perspectives on Heme-Diatomic Interactions 2007In Press

Mocny, J.C., Olson, J.S., and Connell, T.D. Passively released heme from hemoglobin and myoglobin is a potential source of nutrient iron for Bordetella bronchiseptica.  Infection & Immunity, 75 2007: 4857-4866

Deng, P., Nienhaus, K., Palladino, P., Olson, J.S., Blouin, G., Moens, L., Dewilde, S., Gevens, E., and Nienhaus, G.U. Transient ligand docking sites in Cerebratus lacteus mini-hemoglobin.  Gene, 398 2007: 208-223

Zhou, S., Olson, J.S., Fabian, M., Weiss, M.J., and Gow, A.J. Biochemical fates of alpha hemoglobin bound to alpha hemoglobin stabilizing protein (AHSP).  J. Biol. Chem., 281 2006: 32611-32618

Gardner, P.A., Gardner, A.M., Brashear, W.T., Suzuki, T., Hvitved, A.N., Setchell, K.D.R., and Olson, J.S. Hemoglobins Deoxygenate NO with High Fidelity.  Journal of Inorganic Biochemistry, 100 2006: 542-550

Nygaard, T.K., Blouin, G.C., Liu, M., Fukumura, M., Olson, J.S., Fabian, M., Dooley, D.M., and Lei, B. The mechanism of heme transfer from the Streptococcal cell surface protein Shp to HtsA of the HtsABC transporter.  J. Biol. Chem., 281 2006: 20761-20771

Goldbeck, R.A., Bhaskaran, S., Ortega, C., Mendoza, J., Olson, J. Soman, J., Kliger, D.S., and Esquerra, R.M. Water and ligand entry in myoglobin: Assessing the speed and extent of heme pocket hydration after CO photodissociation.  Proc. Natl. Acad. Sci., 103 2006: 1254-1259

Zhang, W., Olson, J.S., and Phillips, G.N., Jr. Biophysical, kinetic characterization, and crystallization of HemAT: An aerotaxis transducer from Bacillus subtilis.  Biophys. J., 88 2005: 2801-2814

Olson, J.S., and Maillett, D.H. Designing recombinant hemoglobin for use as a blood substitute.  Chapter 27 Blood Substitutes 2005: 354-374

Helmick, R.A., Fletcher, A.E., Gardner, A.M., Gessner, C.R., Hvitved, A.N., Gustin, M.C., and Gardner, P.R. Imidazole antibiotics inhibit the nitric oxide dioxygenase function of microbial flavohemoglobin.  Antimicrob. Agents Chemother, 49 2005: 1837-1843

Ionascu, D., Gruis, F., Ye, X., Yu, A., Rosca, F., Beck, C., Demidov, A., Olson, J.S., and Champion, P.M. Temperature dependent studies of NO recombination to heme and heme proteins.  J. Amer. Chem. Soc. 2005In Press

Nienhaus, K., Olson, J.S., Franzen, S., and Nienhaus, G.U. The origin of stark splitting in the initial photoproduct state of MbCO.  J. Amer. Chem. Soc., 127 2005: 40-42

Dantsker, D., Roche, C., Samuni, U., Blouin, G., Olson, J.S., and Friedman, J. The position 68(E11) side chain in myoglobin regulates ligand capture bond formation with the heme iron, and internal movement into the Xe cavities.  J. Biol. Chem., 280 2005: 38740-38755

Miranda, J.J.L., Maillett, D.H., Soman, J., and Olson, J.S. Thermoglobin, oxygen-avid hemoglobin in a eubacterial hyperthermophile.  J. Biol. Chem., 280 2005: 36754-36761

Unno, M., Matsui, T., Chu, G.C., Couture, M., Yoshida, T., Rousseau, D.L., Olson, J.S., and Ikeda-Saito, M. Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: Implications for heme oxygenase function.  J. Biol. Chem., 279 2004: 21055-21061

Puranik, M., Nielsen, S.B., Youn, H., Bourassa, J.L., Case, M.A., Hvitved, A.N., Tengroth, C., Balakrishnan, G., Thorsteinsson, M.V., Olson, J.S., Roberts, G.P., Groves, J.T., McLendon, G.L., and Spiro, T.G. Dynamics of carbon monoxide binding to the CooA protein.  J. Biol. Chem., 279 2004: 21096-21108

Olson, J.S., Foley, E.W., Rogge, C., Tsai, A-L., Doyle, M.P., and Lemon, D.D. NO Savenging and the hypertensive effect of Hb-based blood substitutes.  Free Radical Biol. Med., 36 2004: 685-697

Geuens, E., Dewilde, S., Hoogewijs, D., Pesce, A., Nienhaus, K., Olson, J.S., Vanfleteren, J., Bolognesi, M., and Moens, L. Nerve hemoglobins in invertebrates.  IUBMB Journal 2004In Press

Schotte, F., Soman, J., Olson, J.S., Wulff, M., and Anfinrud, P.A. Picosecond time-resolved X-ray crystallography: Probing protein function in real time.  J. Biol. Struct., 147 2004: 235-246

Nienhaus, K., Olson, J.S., Franzen, S., Nienhaus, G.U. The Origin of Stark Splitting in the Initial Photoproduct State of MbCO.  J. Amer. Chem. Soc. 2004In Press

Pesce, A., Nardini, M., Ascenzi, P., Geuens, E., Dewilde, S., Moens, L., Bolognesi, M., Riggs, A.F., Hale, A., Deng, P., Nienhaus, G.U., Olson, J.S., and Nienhaus, K. ThrE11 Regulates O2 affinity in Cerebratulus lacteus minihemoglobin.  J. Biol. Chem., 279 2004: 33662-33672

Kundu, S., Blouin, G.C., Premer, S.A., Sarath, G., Olson, J.S., and Hargrove, M.S. TyrB10 inhibits stabilization of bound CO and O2 in soybean leghemoglobin.  Biochemistry, 43 2004: 6241-6252

Vogel, K.M., Coyle, C.M., Rush III, T.S., Kozlowski, P.M., Williams, R., Spiro, T.G., Dou, Y., Ikeda-Saito, M., Olson, J.S., and Zgierski, M.Z., FeNO structure in distal pocket mutants of myoglobin from resonance Raman spectroscopy.  Biochemistry, 42 2003: 4896-4903

Nienhaus, K., Deng, P., Olson, J.S., Warren, J.J., and Nienhaus, G.U. Structural Dynamics of Myoglobin: Ligand Migration and Binding in Valine 68 Mutants.  J. Biol. Chem., 278 2003: 42532-42544

Schotte, F., Lim, M., Jackson, T.A., Smirnov, A.V., Soman, J., Olson, J.S., Phillips, G.N., Jr., Wulff, M., and Anfinrud, P.A. Watching a protein as it functions with 150 ps time-resolved X-ray crystallography.  Science, 300 2003: 1944-1947

Draghi, F., Miele, A.E., Travaglini-Allocatelli, C., Vallone, B., Brunori, M., Gibson, Q.H., and Olson, J.S. Controlling ligand binding in myoglobin by mutagenesis.  J. Biol. Chem., 277 2002: 7509-7519

Dou, Y., Maillett, D.H., Eich, R.F., and Olson, J.S. Myoglobin as a model system for designing heme protein based blood substitutes.  Biophys. Chem, 98 2002: 127-148

Scott, E.E., Gibson, Q.H., and Olson, J.S. Mapping Pathways for O2 Entry and Exit from Myoglobin.  J. Biol. Chem., 276 2001: 5177-5188

Liong, E.C., Dou, Y., Scott, E.E., Olson, J.S., and Phillips, G.N. Jr. Water-Proofing the Heme Pocket: the Role of Proximal Amino Acid Side Chains in Preventing Hemin Loss from Myoglobin.  J. Biol. Chem., 276 2001: 9093-9100

Hargrove, M.S., Brucker, E.A., Stec, B., Sarath, G., Arrendondo-Peter, R., Klucas, R.V., Olson, J.S., and Phillips, G.N., Jr. Crystal Structure of a Non-Symbiotic Plant Hemoglobin.  Structure, 8 2000: 1005-1014

Qui, Y., Maillett, D.H., Knapp, J., Olson, J.S., and Riggs, A.F. Lamprey Hemoglobin: Structural Basis of the Bohr Effect.  J. Biol. Chem., 275 2000: 13515-13528

Gardner, P.R., Martin, L.A., Gardner, A.M., Dou, Y., Li, T., and Olson, J.S. Nitric Oxide Dioxygenase Activity and Function of Microbial Flavohemoglobin.  J. Biol. Chem., 275 2000: 31581-31587

Gardner, A.M., Martin, L.A., Gardner, P.R., Dou, Y., and Olson, J.A. Steady-State and Transient Kinetics of Escherichia coli Nitric Oxide Dioxygenase (Flavohemoglobin): The Tyrosine B10 Hydroxyl Is Essential for Oxygen Binding and Catalysis.  J. Biol. Chem., 275 2000: 12581-12589

Scott, E.E., Paster, E.V., and Olson, J.S. The Stabilities of Mammalian Apomyoglobins Vary Over a 600-fold Range and Can Be Enhanced by Comparative Mutagenesis.  J. Biol. Chem., 275 2000: 27129-27136

Thorsteinsson, M.V., Bevan, D.R., Potts, M., Dou, Y., Eich, R.F., Hargrove, M.S., Gibson, Q.H., and Olson, J.S. A Bacterial Hemoglobin with Unusual Ligand Binding Kinetics and Stability Properties.  J. Biol. Chem. B, 38 1999: 2117-2126

Phillips, G.N., Jr., Teodoro, M., Li, T., Smith, B., Gilson, M.M., and Olson, J.S. Bound CO Is a Molecular Probe of Electrostatic Potential in the Distal Pocket of Myoglobin.  J. Phys. Chem. B, 103 1999: 8817-8829

Alayash, A.I., Brockner Ryan, B.A., Eich, R.F., Olson, J.S., and Cashon, R.E. Reactions of Sperm Whale Myoglobin with Hydrogen Peroxide: Effects of Distal Pocket Mutations on the Formation and Stability of the Ferryl Intermediate.  J. Biol. Chem., 274 1999: 2029-2037

Tomita, T., Hirota, S., Ogure, T., Olson, J.S., and Kitagawa, T. Resonance Raman Investigation of Fe-N-O Structure of Nitrosylheme in Myoglobin and Its Mutants.  J. Phys. Chem., 103 1999: 7044-7054

Tang, Q., Kalsbeck, W.A., Olson, J.S., and Bocian, D.F. Disruption of the Heme Iron-Proximal Histidine Bond Requires Unfolding of Deoxymyoglobin.  Biochemistry, 37 1998: 7047-7056

Unno, M., Christian, J.F., Olson, J.S., and Champion, P.M. Evidence of Hydrogen Bonding Effects in the Iron Ligand Vibrations of Carbonmonoxy Myoglobin.  J. Amer. Chem. Soc., 120 1998: 2670-2671

Mansy, S.S., Olson, J.S., Gonzalez, G., and Gilles-Gonzalez, M.A. Imidazole Is a Sensitive Probe of Steric Hindrance in the Distal Pockets of Oxygen-binding Heme Proteins.  Biochemistry, 37 1998: 12452-12457

Brucker, E.A., Olson, J.S., Ikeda-Saito, M., and Phillips, G.N., Jr. Nitric Oxide Myoglobin: Crystal Structure and Analysis of Ligand Geometry.  PROTEINS: Structure, Function, Genetics, 30 1998: 352-356

Unzai, S., Eich, R., Shibayama, N., Olson, J.S., and Morimoto, H. Rate Constants for O2 and CO Binding to the a and b Subunits within the R and T States of Human Hemoglobin.  J. Biol. Chem., 273 1998: 23150-23159

Doherty, D.H., Doyle, M.P., Curry, S.R., Vali, R.J., Fattor, T.J., Olson, J.S., and Lemon, D.D. Rate of Reaction with Nitric Oxide Determines the Hypertensive Effect of Cell-free Hemoglobin.  Nature Biotechnology, 16 1998: 672-676

Nguyen, B.D., Zhao, X., Krishnamurthi, V., La Mar, G.N., Lile, R.A., Brucker, E.A., Phillips, G.N., Jr., Olson, J.S., and Wittenberg, J.B. Solution and Crystal Structures of a Sperm Whale Myoglobin Triple-Mutant that Mimics the Sulfide Binding Hemoglobin from Lucina pectinata.  J. Biol. Chem., 273 1998: 9517-9526

Kryzwda, S., Murshudov, G.N., Brzozowski, A.M., Jaskolski, M., Scott, E.E., Klizas, S.A., Gibson, Q.H., Olson, J.S., and Wilkinson, A.J. Stabilizing Bound O2 in Myoglobin by Valine68(E11) to Asparagine Substitution.  Biochemistry, 37 1998: 15896-15907

Migita, C.T., Matera, K.M., Ikeda-Saito, M., Olson, J.S., Fujii, H., Yoshimura, T., Zhou, H., and Yoshida, T. The Oxygen and Carbon Monoxide Reactions of Heme Oxygenase.  Biochemistry, 273 1998: 945-949

Nakashima, S., Kitagawa, T., and Olson, J.S. Time-Resolved Resonance Raman Study of Intermediates Generated After Photodissociation of Wild-type and Mutant CO Myoglobins.  Chem. Phys., 228 1998: 323-336

Mukai, M., Nakashima, S., Olson, J.S., and Kitagawa, T. Time-Resolved UV Resonance Raman Detection of a Transient Open Form of the Ligand Pathway in Tyr64(E7) Myoglobin.  J. Phys. Chem., B102 1998: 3624-3630

Olson, J.S., and Phillips, G.N., Jr. Kinetic Pathways and Barriers for Ligand Binding to Myoglobin.  J. Biol. Chem., 271 1996: 17593-17596

Thom, C. S., Dickson, C. F., Olson, J. S., Gell, D. A., and Weiss, M. J. Normal and Abnormal Hemoglobins.  Chapter 19, NATHAN and OSKI's HEMATOLOGY OF INFANCY AND CHILDHOOD 8th Edition January 3, 2015

  • B.S. Chemistry (1968) University of Illinois
  • Ph.D. Biochemistry (1972) Cornell University
  • Institute of Biosciences and Bioengineering
  • Keck Center for Quantitative Biomedical Sciences
Research Areas
  • Biochemical, biophysical, and physiological properties of myoglobins, hemoglobins, and red blood cells. Genetic engineering of heme protein based blood substitutes. Application of ultrafast mixing and laser kinetic techniques to biological problems.
Contact Information
Email: olson@rice.edu
Phone: 713-348-4762
Office: 309 Keck Hall,