Papers since 2004 (out of ~200 refereed publications)
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, in press (2009). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19441024
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, 5961-5969 (2009). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19349619
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, 5456-5465 (2009). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19397368
Aranda, R, 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 75 217-230 (2009). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18831041
Salter, M. D., Nienhaus, K., Nienhaus, G. U., Dewilde, S., Moens, L., Pesece, 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, 35689-35702 (2008). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18840607
Maillett, D. H., Simplaceanu, V., Shen, T-J., Ho, N.T., Olson, J. S., and Ho, C. Interfacial and distal pocket mutations exhibit additive effects on the structure and function of hemoglobin. Biochemistry 47, 10551-10563 (2008). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18788751
Hussain, F., Olson, J. S., and Wittung-Stafshede, P. Conserved residues modulate protein stability and copper release in human copper chaperone Atox1. Proc Natl. Acad. Sci., USA, 105, 11158-63 (2008). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18685091
Villarreal, D.M., Phillips, C. L., Kelley, A. M., Villarreal, S., Villaloboz, A., Hernandez, P., Olson, J. S., and Hendersen, D. P. Enhancing Recombinant Hemoglobin Production in Escherichia coli BL21(DE3) containing the Plesiomonas Shigelloides Heme Transport System. J. Appl. Enviro. Micro. 74, 5854-6 (2008). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18676700
Olson, J. S. From O2 Diffusion Into Red Blood Cells To Ligand Pathways In Globins. Chapter 14 (pp. 161-182) in DIOXYGEN BINDING AND SENSING PROTEINS, A Tribute to Beatrice and Jonathan Wittenberg (Eds. M. Bolognesi, G. di Prisco, C. Verde), Springer-Verlag Italia Srl, Milano, Italy, July 2008.
Graves, P.E., Henderson, D. P., Horstman, M. J., Solomon, B. J., and Olson, J. S. Enhancing Stability and Expression of Recombinant Hemoglobin in E. coli: Progress in the Development of a Recombinant HBOC Source. Biochem. Biophys. Acta. Proteins and Proteomics, 1784, 1471-1479 (2008). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18489914
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 (Isd) System of Staphylococcus aureus. J. Biol. Chem. 283, 18450-60 (2008). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18467329
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,
374-83 (2007). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17920629
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, 31380-8
(2007). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17699155
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 (Ed.
Abhik Ghosh) Elsevier, London, in press (2007).
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,
4857-66 (2007). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17664260
Olson, J. S., Soman, J., and Phillips, G. N. Jr. Ligand Pathways
in Myoglobin: A Review of Trp Cavity Mutations, IUBMB Life 59,
552-562 (2007). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17701550
Deng, P., Nienhaus K., Palladino, P., Olson J. S., Blouin. G., Moens, L.,
Dewilde, S., Geuens, E., and Nienhaus, G. U. Transient Ligand Docking Sites
in Cerebratulus lacteus Mini-Hemoglobin, Gene 398, 208-223 (2007) http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17531406
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, 32611-8 (2006). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16901899
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, 20761-71 (2006). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16717094
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, 542-550 (2006). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16439024
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., USA, 103, 1254-1259 (2006). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16432219
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., 127, 16921-16934
(2005). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16316238
Olson, J. S. and Maillett, D. H Designing Recombinant Hemoglobin for Use
as a Blood Substitute, Chapter 31 in Blood Substitutes (Robert
Winslow, Kim D. Vandegriff, Eds.) Elsevier, London, UK (2005), pp. 354-374.
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, 38740-38755 (2005). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16155005
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, 36754-36761 (2005). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16135523
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, 40-42 (2005). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15631438
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, 2801-2814 (2005). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15653746
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, 56, 653-664 (2004). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15804828
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, 235-246 (2004). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15450293
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, 33662-33672
(2004). http://www.ncbi.nlmnih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15161908
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, 6241-6252 (2004). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15147208
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, 21055-21061
(2004). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14966119
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, 21096-21108 (2004). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14990568
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, 685-697 (2004). http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14990349