Kinetic pathways and barriers for ligand binding to myoglobin
Open accessAbstract
Myoglobin is a small globular heme protein that increases the aerobic capacity of striated vertebrate muscle cells by taking up oxygen from blood during rest and delivering O2 to mitochondria during muscle contraction when blood flow through capillaries is restricted. The ferrous form of myoglobin can also react with CO and NO, which are produced in vivo as second messengers for regulating various physiological functions including blood pressure, platelet aggregation, and neurotransmission. Its tertiary structure consists of eight tightly packed helices, and the resulting “myoglobin fold” is very similar to that found for the α and β subunits of hemoglobin.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The k0 for Ngb is 500 fold faster than for Hb and approaching a rate constant characteristic of that which is rate-limited by how fast nitrite can get to the heme pocket.
“This is 500 fold faster than for Hb and approaching a rate constant characteristic of that which rate-limited by how fast nitrite can get to the heme pocket [61, 62].”
From Mechanisms of nitrite bioactivation (2014) · cites this paper as [62]
Cites
Conformational Substates in Proteins
Frauenfelder, H., Parak, F., & Young, R. D. (1988) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.17.060188.002315 · Cited by 995 · see citing works
Mechanisms of Ligand Recognition in Myoglobin
Springer, B. A., Sligar, S. G., Olson, J. S., & Phillips, G. N. J. (1994) · Chemical Reviews · doi:10.1021/cr00027a007 · Cited by 755 · see citing works
Mechanism of NO-induced oxidation of myoglobin and hemoglobin
Eich, R. F., Li, T., Lemon, D. D., Doherty, D. H., Curry, S. R., Aitken, J. F., Mathews, A. J., Johnson, K. A., Smith, R. D., Phillips, et al. (1996) · Biochemistry · doi:10.1021/bi960442g · Cited by 613 · see citing works
Elber, R., & Karplus, M. (1990) · Journal of the American Chemical Society · doi:10.1021/ja00181a020 · Cited by 506 · see citing works
Cavities in proteins: structure of a metmyoglobin xenon complex solved to 1.9 .ANG.
Tilton, R. F., Kuntz, I. D., & Petsko, G. A. (1984) · Biochemistry · doi:10.1021/bi00308a002 · Cited by 476 · see citing works
High-Resolution Crystal Structures of Distal Histidine Mutants of Sperm Whale Myoglobin
Quillin, M. L., Arduini, R. M., Olson, J. S., & Phillips, G. N. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1569 · Cited by 385 · see citing works
Petrich, J. W., Poyart, C., & Martin, J. L. (1988) · Biochemistry · doi:10.1021/bi00411a022 · Cited by 364 · see citing works
Crystal Structures of CO−, Deoxy- and Met-myoglobins at Various pH Values
Yang, F., & Phillips, G. N., Jr. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0123 · Cited by 340 · see citing works
Crystal structure of photolysed carbonmonoxy-myoglobin
Schlichting, I., Berendzen, J., Phillips, G. N., Jr., & Sweet, R. M. (1994) · Nature · doi:10.1038/371808a0 · Cited by 329 · see citing works
Binding of CO to Myoglobin from a Heme Pocket Docking Site to Form Nearly Linear Fe-C-O
Lim, M., Jackson, T. A., & Anfinrud, P. (1995) · Science · doi:10.1126/science.7638619 · Cited by 280 · see citing works
Geminate recombination of carbon monoxide to myoglobin
Henry, E. R., Sommer, J. H., Hofrichter, J., Eaton, W. A., & Gellert, M. F. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80094-1 · Cited by 268 · see citing works
Petrich, J. W., Lambry, J., Kuczera, K., Karplus, M., Poyart, C., & Martin, J. L. (1991) · Biochemistry · doi:10.1021/bi00230a025 · Cited by 210 · see citing works
Conformational Relaxation and Ligand Binding in Myoglobin
Ansari, A., Jones, C. M., Henry, E. R., Hofrichter, J., & Eaton, W. A. (1994) · Biochemistry · doi:10.1021/bi00183a017 · Cited by 202 · see citing works
Reaction of myoglobin with phenylhydrazine: a molecular doorstop
Ringe, D., Petsko, G. A., Kerr, D. E., & de Montellano, P. R. O. (1984) · Biochemistry · doi:10.1021/bi00296a001 · Cited by 191 · see citing works
Structural and Functional Effects of Apolar Mutations of the Distal Valine in Myoglobin
Quillin, M. L., Li, T., Olson, J. S., Phillips, G. N., Jr., Duo, Y., Ikeda‐Saito, M., Regan, R. M., Carlson, M. L., Gibson, Q. H., Li, H., et al. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.0034 · Cited by 190 · see citing works
Carver, T. E., Rohlfs, R. J., Olson, J. S., Gibson, Q. H., Blackmore, R. S., Springer, B. A., & Sligar, S. G. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)45475-5 · Cited by 182 · see citing works
Myoglobin and haemoglobin: role of distal residues in reactions with haem ligands
Perutz, M. F. (1989) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(89)90039-x · Cited by 178 · see citing works
Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K
Teng, T.-Y., Šrajer, V., & Moffat, K. (1994) · Nature Structural & Molecular Biology · doi:10.1038/nsb1094-701 · Cited by 170 · see citing works
Gibson, Q. H., Regan, R. M., Elber, R., Olson, J. S., & Carver, T. E. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41630-4 · Cited by 141 · see citing works
Jongeward, K. A., Magde, D., Taube, D. J., Marsters, J. C., Traylor, T. G., & Sharma, V. S. (1988) · Journal of the American Chemical Society · doi:10.1021/ja00210a011 · Cited by 133 · see citing works
Lim, M., Jackson, T. A., & Anfinrud, P. (1995) · The Journal of Chemical Physics · doi:10.1063/1.469484 · Cited by 133 · see citing works
Structure of myoglobin-ethyl isocyanide histidine as a swinging door for ligand entry
Johnson, K. A., Olson, J. S., & Phillips, G. N. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90269-6 · Cited by 126 · see citing works
Discovery of new ligand binding pathways in myoglobin by random mutagenesis
Huang, X. C., & Boxer, S. G. (1994) · Nature Structural & Molecular Biology · doi:10.1038/nsb0494-226 · Cited by 101 · see citing works
Tian, W.-N., Sage, J. T., & Champion, P. M. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1491 · Cited by 99 · see citing works
Reactivity of ferric Aplysia and sperm whale myoglobins towards imidazole
Bolognesi, M., Cannillo, E., Ascenzi, P., Giacometti, G. M., Merli, A., & Brunori, M. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90435-1 · Cited by 94 · see citing works
Orientation of carbon monoxide and structure-function relationship in carbonmonoxymyoglobin.
Ormos, P., Braunstein, D., Frauenfelder, H., Hong, M., Lin, S. L., Sauke, T. B., & Young, R. D. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.22.8492 · Cited by 93 · see citing works
Braunstein, D., Chu, K., Egeberg, K. D., Frauenfelder, H., Mourant, J. R., Nienhaus, G. U., Ormos, P., Sligar, S. G., Springer, B. A., & Young, R. D. (1993) · Biophysical Journal · doi:10.1016/s0006-3495(93)81310-9 · Cited by 91 · see citing works
Geminate Recombination of Diatomic Ligands CO, O2, and NO with Myoglobin
Walda, K. N., Liu, X. Y., Sharma, V. S., & Magde, D. (1994) · Biochemistry · doi:10.1021/bi00174a029 · Cited by 84 · see citing works
Smerdon, S. J., Dodson, G. G., Wilkinson, A. J., Gibson, Q. H., Blackmore, R. S., Carver, T. E., & Olson, J. S. (1991) · Biochemistry · doi:10.1021/bi00239a025 · Cited by 77 · see citing works
Carlson, M. L., Regan, R. M., Elber, R., Li, H., Phillips, G. N., Olson, J. S., & Gibson, Q. H. (1994) · Biochemistry · doi:10.1021/bi00201a005 · Cited by 73 · see citing works
Cornelius, P. A., Steele, A. W., Chernoff, D. A., & Hochstrasser, R. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.12.7526 · Cited by 71 · see citing works
Tilton, R. F., Singh, U. C., Kuntz, I. D., & Kollman, P. A. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90389-0 · Cited by 68 · see citing works
Ultrafast Measurements of Geminate Recombination of NO with Site-specific Mutants of Human Myoglobin
Petrich, J. W., Lambry, J., Balasubramanian, S., Lambright, D. G., Boxer, S. G., & Martin, J. L. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1302 · Cited by 62 · see citing works
Distal Cavity Fluctuations in Myoglobin: Protein Motion and Ligand Diffusion
Carlson, M. L., Regan, R. M., & Gibson, Q. H. (1996) · Biochemistry · doi:10.1021/bi951767k · Cited by 59 · see citing works
Ikeda‐Saito, M., Dou, Y., Yonetani, T., Olson, J. S., Li, T., Regan, R. M., & Gibson, Q. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53115-x · Cited by 54 · see citing works
Lai, H. H., Li, T., Lyons, D. S., Phillips, G. N., Olson, J. S., & Gibson, Q. H. (1995) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340220404 · Cited by 44 · see citing works
Hemoproteins, Ligands, and Quanta
Gibson, Q. H. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47036-1 · Cited by 38 · see citing works
Simulation of carboxymyoglobin photodissociation.
Sassaroli, M., & Rousseau, D. L. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66562-7 · Cited by 23 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Riess, J. G. (2001) · Chemical Reviews · doi:10.1021/cr970143c · Cited by 772 · see citing works
Crystal Structures of Myoglobin-Ligand Complexes at Near-Atomic Resolution
Vojtechovsky, J., Chu, K., Berendzen, J., Sweet, R. M., & Schlichting, I. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77056-6 · Cited by 562 · see citing works
Mechanistic aspects of the reactions of nitric oxide with transition-metal complexes
Ford, P. C., & Lorkovic, I. M. (2002) · Chemical Reviews · doi:10.1021/cr0000271 · Cited by 525 · see citing works
Photoinduced Linkage Isomers of Transition-Metal Nitrosyl Compounds and Related Complexes
Coppens, P., Novozhilova, I. V., & Kovalevsky, A. Y. (2002) · Chemical Reviews · doi:10.1021/cr000031c · Cited by 427 · see citing works
Maia, L. B., & Moura, J. J. G. (2014) · Chemical Reviews · doi:10.1021/cr400518y · Cited by 401 · see citing works
Ligand binding and conformational motions in myoglobin
Ostermann, A., Waschipky, R., Parak, F., & Nienhaus, G. U. (2000) · Nature · doi:10.1038/35004622 · Cited by 368 · see citing works
Mapping the Pathways for O2 Entry Into and Exit from Myoglobin
Scott, E. E., Gibson, Q. H., & Olson, J. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008282200 · Cited by 351 · see citing works
Structure and function of haemoglobins
Gell, D. A. (2017) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2017.10.006 · Cited by 277 · see citing works
Gardner, P. R. (2004) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2004.10.003 · Cited by 272 · see citing works
Human Neuroglobin, a Hexacoordinate Hemoglobin That Reversibly Binds Oxygen
Trent, J. T., Watts, R. A., & Hargrove, M. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100300200 · Cited by 231 · see citing works
Infrared Probes for Studying the Structure and Dynamics of Biomolecules
Kim, H., & Cho, M. (2013) · Chemical Reviews · doi:10.1021/cr3005185 · Cited by 230 · see citing works
Møller, J. K. S., & Skibsted, L. H. (2002) · Chemical Reviews · doi:10.1021/cr000078y · Cited by 228 · see citing works
Yoon, S. S. (2006) · Journal of Clinical Investigation · doi:10.1172/jci24684 · Cited by 212 · see citing works
Nitric oxide and quality and safety of muscle based foods
Skibsted, L. H. (2011) · Nitric Oxide · doi:10.1016/j.niox.2011.03.307 · Cited by 201 · see citing works
Biological Chemistry of Carbon Monoxide
Piantadosi, C. A. (2002) · Antioxidants and Redox Signaling · doi:10.1089/152308602753666316 · Cited by 201 · see citing works
Spin-Forbidden Ligand Binding to the Ferrous−Heme Group: Ab Initio and DFT Studies
Strickland, N., & Harvey, J. N. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp064091j · Cited by 198 · see citing works
A molecular basis for NO selectivity in soluble guanylate cyclase
Boon, E. M., Huang, S. H., & Marletta, M. A. (2005) · Nature Chemical Biology · doi:10.1038/nchembio704 · Cited by 188 · see citing works
Picosecond time-resolved X-ray crystallography: probing protein function in real time
Schotte, F., Soman, J., Olson, J. S., Wulff, M., & Anfinrud, P. (2004) · Journal of Structural Biology · doi:10.1016/j.jsb.2004.06.009 · Cited by 169 · see citing works
Signal transduction by heme-containing PAS-domain proteins
Gilles‐Gonzalez, M., & Gonzalez, G. (2004) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00941.2003 · Cited by 168 · see citing works
Structure and reactivity of hexacoordinate hemoglobins
Kakar, S., Hoffman, F. G., Storz, J. F., Fabián, M., & Hargrove, M. S. (2010) · Biophysical Chemistry · doi:10.1016/j.bpc.2010.08.008 · Cited by 160 · see citing works
Schmidt, M., Nienhaus, K., Pahl, R., Krasselt, A., Anderson, S. M., Parak, F., Nienhaus, G. U., & Šrajer, V. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504932102 · Cited by 159 · see citing works
Plants, humans and hemoglobins
Kundu, S., Trent, J. T., & Hargrove, M. S. (2003) · Trends in Plant Science · doi:10.1016/s1360-1385(03)00163-8 · Cited by 159 · see citing works
Mechanisms of nitrite bioactivation
Kim-Shapiro, D. B., & Gladwin, M. T. (2014) · Nitric Oxide · doi:10.1016/j.niox.2013.11.002 · Cited by 157 · see citing works
Steady-state and Transient Kinetics of Escherichia coli Nitric-oxide Dioxygenase (Flavohemoglobin)
Gardner, A. M., Martin, L. A., & Gardner, P. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.17.12581 · Cited by 157 · see citing works
Hemoglobin-mediated nitric oxide signaling
Helms, C., & Kim-Shapiro, D. B. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.04.028 · Cited by 146 · see citing works
Probing Substates in Sperm Whale Myoglobin Using High-Pressure Crystallography
Urayama, P. K., Phillips, G. N., & Gruner, S. M. (2002) · Structure · doi:10.1016/s0969-2126(01)00699-2 · Cited by 144 · see citing works
Characterization of recombinant soybean leghemoglobin a and apolar distal histidine mutants
Hargrove, M. S., Barry, J. K., Brucker, E. A., Berry, M. B., Phillips, G. N., Olson, J. S., Arredondo‐Peter, R., Dean, J., Klucas, R. V., & Sarath, G. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0833 · Cited by 139 · see citing works
Reactions of NO and nitrite with heme models and proteins
Ford, P. C. (2010) · Inorganic Chemistry · doi:10.1021/ic902073z · Cited by 138 · see citing works
Is the CO Adduct of Myoglobin Bent, and Does It Matter?
Spiro, T. G., & Kozlowski, P. M. (2000) · Accounts of Chemical Research · doi:10.1021/ar000108j · Cited by 135 · see citing works
Ruscio, J. Z., Kumar, D., Shukla, M. P., Prisant, M. G., Murali, T. M., & Onufriev, A. V. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710825105 · Cited by 134 · see citing works
Rovira, C., Schulze, B. G., Eichinger, M., Evanseck, J. D., & Parrinello, M. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)75711-6 · Cited by 129 · see citing works
Internal dynamics and protein–matrix coupling in trehalose-coated proteins
Cordone, L., Cottone, G., Giuffrida, S., Palazzo, G., Venturoli, G., & Viappiani, C. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.03.004 · Cited by 121 · see citing works
Visualizing breathing motion of internal cavities in concert with ligand migration in myoglobin
Tomita, A., Sato, T., Ichiyanagi, K., Nozawa, S., Ichikawa, H., Chollet, M., Kawai, F., Park, S., Tsuduki, T., Yamato, T., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807774106 · Cited by 116 · see citing works
Ligand specificity of H-NOX domains: from sGC to bacterial NO sensors
Boon, E. M., & Marletta, M. A. (2005) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2004.12.016 · Cited by 113 · see citing works
A Cooperative Oxygen Binding Hemoglobin from Mycobacterium tuberculosis
Yeh, S., Couture, M., Ouellet, Y. H., Guertin, M., & Rousseau, D. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.3.1679 · Cited by 112 · see citing works
Birukou, I., Schweers, R. L., & Olson, J. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.053934 · Cited by 111 · see citing works
Controlling Ligand Binding in Myoglobin by Mutagenesis
Draghi, F., Miele, A. E., Travaglini‐Allocatelli, C., Vallone, B., Brunori, M., Gibson, Q. H., & Olson, J. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109206200 · Cited by 107 · see citing works
A “Sliding Scale Rule” for Selectivity among NO, CO, and O2 by Heme Protein Sensors
Tsai, A., Berka, V., Martin, E., & Olson, J. S. (2011) · Biochemistry · doi:10.1021/bi2015629 · Cited by 105 · see citing works
Andersen, J. F., Weichsel, A., Balfour, C. A., Champagne, D. E., & Montfort, W. R. (1998) · Structure · doi:10.1016/s0969-2126(98)00131-2 · Cited by 103 · see citing works
The Specificity of Nitroxyl Chemistry Is Unique Among Nitrogen Oxides in Biological Systems
Flores‐Santana, W., Salmon, D. J., Donzelli, S., Switzer, C., Basudhar, D., Ridnour, L. A., Cheng, R. Y. S., Glynn, S. A., Paolocci, N., Fukuto, J. M., et al. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3841 · Cited by 99 · see citing works
Wink, D. A., Miranda, K. M., Katori, T., Mancardi, D., Thomas, D. D., Ridnour, L. A., Espey, M. G., Feelisch, M., Colton, C. A., Fukuto, J. M., et al. (2003) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00531.2003 · Cited by 98 · see citing works
Protein dynamics and enzyme catalysis: Insights from simulations
McGeagh, J. D., Ranaghan, K. E., & Mulholland, A. J. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.12.002 · Cited by 95 · see citing works
Yi, J., Heinecke, J. L., Tan, H., Ford, P. C., & Richter-Addo, G. B. (2009) · Journal of the American Chemical Society · doi:10.1021/ja904726q · Cited by 96 · see citing works
Cherepanov, A. V., & de Vries, S. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.02.006 · Cited by 92 · see citing works
Protein ligand migration mapped by nonequilibrium 2D-IR exchange spectroscopy
Bredenbeck, J., Helbing, J., Nienhaus, K., Nienhaus, G. U., & Hamm, P. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607758104 · Cited by 92 · see citing works
Temperature-Dependent Studies of NO Recombination to Heme and Heme Proteins
Ionascu, D., Gruia, F., Xiong, Y., Yu, A., Rosca, F., Beck, C. M., Demidov, A., Olson, J. S., & Champion, P. M. (2005) · Journal of the American Chemical Society · doi:10.1021/ja054249y · Cited by 91 · see citing works
Ultrafast dynamics of ligands within heme proteins
Vos, M. H. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.10.004 · Cited by 89 · see citing works
Kim, S., Jin, G., & Lim, M. (2004) · The Journal of Physical Chemistry B · doi:10.1021/jp0489020 · Cited by 86 · see citing works
Reaction mechanisms relevant to the formation of iron and ruthenium nitric oxide complexes
Ford, P. C., & Laverman, L. E. (2004) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2004.04.006 · Cited by 86 · see citing works
Watts, R., Ponka, P., & Richardson, D. R. (2003) · Biochemical Journal · doi:10.1042/bj20021302 · Cited by 84 · see citing works
Graves, P. E., Henderson, D. P., Horstman, M. J., Solomon, B. J., & Olson, J. S. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.04.012 · Cited by 82 · see citing works
Evidence for dynamics in proteins as a mechanism for ligand dissociation
Carroll, M. J., Mauldin, R. V., Gromova, A. V., Singleton, S. F., Collins, E. J., & Lee, A. L. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.769 · Cited by 81 · see citing works
Ligand Binding and Hexacoordination in SynechocystisHemoglobin
Hvitved, A. N., Trent, J. T., Premer, S. A., & Hargrove, M. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105175200 · Cited by 81 · see citing works
Tejero, J., Sparacino-Watkins, C. E., Ragireddy, V., Frizzell, S. A., & Gladwin, M. T. (2015) · Biochemistry · doi:10.1021/bi501196k · Cited by 77 · see citing works
Plant Hemoglobins: A Molecular Fossil Record for the Evolution of Oxygen Transport
Hoy, J. A., Robinson, H. H., Trent, J. T., Kakar, S., Smagghe, B. J., & Hargrove, M. S. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.05.029 · Cited by 78 · see citing works
Sakakura, M., Yamaguchi, S., Hirota, N., & Terazima, M. (2001) · Journal of the American Chemical Society · doi:10.1021/ja9944655 · Cited by 75 · see citing works
Structural Dynamics of Myoglobin
Lamb, D. C., Nienhaus, K., Arcovito, A., Draghi, F., Miele, A. E., Brunori, M., & Nienhaus, G. U. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109892200 · Cited by 75 · see citing works
Trapping intermediates in the crystal: ligand binding to myoglobin
Schlichting, I., & Chu, K. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00158-5 · Cited by 75 · see citing works
Structural Dynamics of Myoglobin
Nienhaus, K., Deng, P., Olson, J. S., Warren, J. J., & Nienhaus, G. U. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306888200 · Cited by 74 · see citing works
Brunori, M., Cutruzzolà, F., Savino, C., Travaglini‐Allocatelli, C., Vallone, B., & Gibson, Q. H. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77289-9 · Cited by 74 · see citing works
Structural dynamics of myoglobin
Brunori, M. (2000) · Biophysical Chemistry · doi:10.1016/s0301-4622(00)00142-3 · Cited by 73 · see citing works
Theoretical study of the discrimination between O2 and CO by myoglobin
Sigfridsson, E., & Ryde, U. (2002) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(02)00426-9 · Cited by 72 · see citing works
The leghemoglobin proximal heme pocket directs oxygen dissociation and stabilizes bound heme
Kundu, S., Snyder, B., Das, K., Chowdhury, P. K., Park, J., Petrich, J. W., & Hargrove, M. S. (2002) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10048 · Cited by 72 · see citing works
Su, J., & Groves, J. T. (2009) · Journal of the American Chemical Society · doi:10.1021/ja902473r · Cited by 71 · see citing works
Lu, C., Egawa, T., Wainwright, L. M., Poole, R. K., & Yeh, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609397200 · Cited by 71 · see citing works
Oxygen affinity and amino acid sequence of myoglobins from endothermic and ectothermic fish
Marcinek, D. J., Bonaventura, J., Wittenberg, J. B., & Block, B. A. (2001) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.2001.280.4.r1123 · Cited by 66 · see citing works
Heme: From quantum spin crossover to oxygen manager of life
Kepp, K. P. (2016) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2016.08.008 · Cited by 64 · see citing works
From curiosity to applications. A personal perspective on inorganic photochemistry
Ford, P. C. (2016) · Chemical Science · doi:10.1039/c6sc00188b · Cited by 63 · see citing works
Ultrafast Proteinquake Dynamics in Cytochromec
Zang, C., Stevens, J. A., Link, J. J., Guo, L., Wang, L., & Zhong, D. (2009) · Journal of the American Chemical Society · doi:10.1021/ja8057293 · Cited by 62 · see citing works
Cooper, H. L. R., Mishra, G., Huang, X., Pender‐Cudlip, M., Austin, R. N., Shanklin, J., & Groves, J. T. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3059149 · Cited by 61 · see citing works
Tsai, A.-L., Martin, E., Berka, V., & Olson, J. S. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4564 · Cited by 60 · see citing works
Spectroscopic and Mechanistic Investigations of Dehaloperoxidase B fromAmphitrite ornata
D’Antonio, J., D'Antonio, E. L., Thompson, M. K., Bowden, E. F., Franzen, S., Smirnova, T. I., & Ghiladi, R. A. (2010) · Biochemistry · doi:10.1021/bi100407v · Cited by 58 · see citing works
Goldbeck, R. A., Bhaskaran, S. S., Ortega, C., Mendoza, J. L., Olson, J. S., Soman, J., Kliger, D. S., & Esquerra, R. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507840103 · Cited by 58 · see citing works
Finding Gas Migration Pathways in Proteins Using Implicit Ligand Sampling
Cohen, J., Olsen, K. W., & Schulten, K. J. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)37022-5 · Cited by 58 · see citing works
Ishigami, I., Zatsepin, N. A., Hikita, M., Conrad, C. E., Nelson, G., Coe, J. D., Basu, S., Grant, T. D., Seaberg, M., Sierra, R. G., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1705628114 · Cited by 58 · see citing works
Halder, P., Trent, J. T., & Hargrove, M. S. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21210 · Cited by 56 · see citing works
Nienhaus, K., Deng, P., Kriegl, J. M., & Nienhaus, G. U. (2003) · Biochemistry · doi:10.1021/bi034787s · Cited by 56 · see citing works
Role of Heme Distortion on Oxygen Affinity in Heme Proteins: The Protoglobin Case
Bikiel, D. E., Forti, F., Boechi, L., Nardini, M., Luque, F. J., Marti, M. A., & Estrin, D. A. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp102135p · Cited by 54 · see citing works
Influence of Histidine Tag Attachment on Picosecond Protein Dynamics
Thielges, M. C., Chung, J. K., Axup, J. Y., & Fayer, M. D. (2011) · Biochemistry · doi:10.1021/bi2003923 · Cited by 54 · see citing works
Bianchetti, C. M., Blouin, G. C., Bitto, E., Olson, J. S., & Phillips, G. N. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22617 · Cited by 54 · see citing works
Sato, A., Sasakura, Y., Sugiyama, S., Sagami, I., Shimizu, T., Mizutani, Y., & Kitagawa, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204559200 · Cited by 52 · see citing works
Underbakke, E. S., Sürmeli, N. B., Smith, B. C., Wynia‐Smith, S. L., & Marletta, M. A. (2013) · Elsevier eBooks · doi:10.1016/b978-0-08-097774-4.00320-x · Cited by 51 · see citing works
Møller, J. K. S., & Skibsted, L. H. (2004) · Chemistry - A European Journal · doi:10.1002/chem.200305368 · Cited by 51 · see citing works
Brittain, T., Baker, A. R., Butler, C. S., Little, R. H., LOWE, D. J., Greenwood, C., & Watmough, N. J. (1997) · Biochemical Journal · doi:10.1042/bj3260109 · Cited by 50 · see citing works
Internal Water and Microsecond Dynamics in Myoglobin
Kaieda, S., & Halle, B. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp409234g · Cited by 49 · see citing works
Denaturation of a Protein Monitored by Diffusion Coefficients: Myoglobin
Choi, J., & Terazima, M. (2002) · The Journal of Physical Chemistry B · doi:10.1021/jp0256802 · Cited by 48 · see citing works
Normal and Abnormal Protein Subunit Interactions in Hemoglobins
Manning, J. M., Dumoulin, A., Li, X., & Manning, L. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.31.19359 · Cited by 48 · see citing works
Kumazaki, S., Nakajima, H., Sakaguchi, T., Nakagawa, E., Shinohara, H., Yoshihara, K., & Aono, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005533200 · Cited by 48 · see citing works
Bobofchak, K. M., Mito, T., Texel, S. J., Bellelli, A., Nemoto, M., Traystman, R. J., Koehler, R. C., Brinigar, W. S., & Fronticelli, C. (2003) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00037.2003 · Cited by 47 · see citing works
Hendgen-Cotta, U. B., Kelm, M., & Rassaf, T. (2010) · Nitric Oxide · doi:10.1016/j.niox.2009.10.003 · Cited by 46 · see citing works
Protein Engineering Strategies for Designing More Stable Hemoglobin-based Blood Substitutes
Olson, J. S., Eich, R. F., Smith, L. P., Warren, J. J., & Knowles, B. C. (1997) · Artificial Cells Blood Substitutes and Biotechnology · doi:10.3109/10731199709118912 · Cited by 46 · see citing works
Harmonic and Anharmonic Dynamics of Fe–CO and Fe–O2 in Heme Models
Rovira, C., & Parrinello, M. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76575-1 · Cited by 46 · see citing works
Searching for Neuroglobin's role in the brain
Nienhaus, K., & Nienhaus, G. U. (2007) · IUBMB Life · doi:10.1080/15216540601188538 · Cited by 44 · see citing works
An Atomistic View on Human Hemoglobin Carbon Monoxide Migration Processes
Lucas, M. F., & Guallar, V. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.01.011 · Cited by 44 · see citing works
Free-Energy Barriers in MbCO Rebinding
Banushkina, P. V., & Meuwly, M. (2005) · The Journal of Physical Chemistry B · doi:10.1021/jp051938n · Cited by 44 · see citing works
Harada, K., Makino, M., Sugimoto, H., Hirota, S., Matsuo, T., Shiro, Y., Hisaeda, Y., & Hayashi, T. (2007) · Biochemistry · doi:10.1021/bi7007068 · Cited by 44 · see citing works
Molecular Basis for Nitric Oxide Dynamics and Affinity with Alcaligenes xylosoxidans Cytochrome c´
Kruglik, S. G., Lambry, J., Cianetti, S., Martin, J. L., Eady, R. R., Andrew, C. R., & Négrerie, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604327200 · Cited by 44 · see citing works
Blocking the Gate to Ligand Entry in Human Hemoglobin
Birukou, I., Soman, J., & Olson, J. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.176271 · Cited by 43 · see citing works
Time resolved thermodynamics of ligand binding to heme proteins
Larsen, R. W., & Mikšovská, J. (2006) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2006.08.018 · Cited by 42 · see citing works
Structural and functional properties of class 1 plant hemoglobins
Igamberdiev, A. U., Bykova, N. V., & Hill, R. D. (2011) · IUBMB Life · doi:10.1002/iub.439 · Cited by 42 · see citing works
- Authors
- Olson, J. S., & Phillips, G. N.
- Affiliations
- Rice University (US)
- Corresponding author
- Olson, John S.
- ORCID
- Olson, John S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1996-07
- Volume
- 271
- Issue
- 30
- Pages
- 17593-17596
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2075917539
- Cited by
- 259
- References
- 38
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 4 · 2023: 1 · 2022: 2 · 2021: 2 · 2020: 2 · 2019: 3 · 2018: 2 · 2017: 8 · 2016: 8 · 2015: 8 · 2014: 3 · 2013: 10 · 2012: 12
- FWCI
- 0.44
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (7r01ar040252-11)
- National Heart, Lung, and Blood Institute (HL47020, R01HL047020)
- National Institute of General Medical Sciences (GM35649, R01GM035649)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR 40252)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- myoglobin, ligand binding, binding kinetics, heme proteins, oxygen binding, carbon monoxide binding, nitric oxide binding, protein tertiary structure
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review