Cited by 189Hemoglobin structure and functionMetal-Catalyzed Oxygenation MechanismsHeme Oxygenase-1 and Carbon Monoxide

The DOI matches its Crossref record; 297 of the 297 references it cites were found in a registry or an index.

The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms

Reeder, Brandon J.·2010·Antioxidants & Redox Signaling

DOI 10.1089/ars.2009.2974

Open this paper in CoChat — free account

Abstract

Pentacoordinate respiratory hemoproteins such as hemoglobin and myoglobin have evolved to supply cells with oxygen. However, these respiratory heme proteins are also known to function as redox enzymes, reacting with compounds such as nitric oxide and peroxides. The recent discoveries of hexacoordinate hemoglobins in vertebrates and nonsymbiotic plants suggest that the redox activity of globins is inherent to the molecule. The uncontrolled formation of radical species resulting from such redox chemistry on respiratory hemoproteins can lead to oxidative damage and cellular toxicity. In this review, we examine the functions of various globins and the mechanisms by which these globins act as redox enzymes under physiologic conditions. Evidence that redox reactions also occur under disease conditions, leading to pathologic complications, also is examined, focusing on recent discoveries showing that the ferryl oxidation state of these hemoproteins is present in these disease states in vivo. In addition, we review the latest advances in the understanding of globin redox mechanisms and how they might affect cellular signaling pathways and how they might be controlled therapeutically or, in the case of hemoglobin-based blood substitutes, through rational design.

Integrity signals

Registry

Crossref · 10.1089/ars.2009.2974

Cites

297 of 297 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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 obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine
Furchgott, R. F., & Zawadzki, J. V. (1980) · Nature · doi:10.1038/288373a0 · Cited by 12,064
Free Radicals in Biology and Medicine
Halliwell, B., & Gutteridge, J. M. C. (2015) · doi:10.1093/acprof:oso/9780198717478.001.0001 · Cited by 8,990
The global distribution of clinical episodes of Plasmodium falciparum malaria
Snow, R. W., Guerra, C. A., Noor, A. M., Myint, H. Y., & Hay, S. I. (2005) · Nature · doi:10.1038/nature03342 · Cited by 2,758
Strategies of antioxidant defense
SIES, H. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18025.x · Cited by 1,976
A series of prostaglandin F2-like compounds are produced in vivo in humans by a non-cyclooxygenase, free radical-catalyzed mechanism.
Morrow, J. D., Hill, K. E., Burk, R. F., Nammour, T., Badr, K. F., & Roberts, L. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.23.9383 · Cited by 1,898
Nitrite reduction to nitric oxide by deoxyhemoglobin vasodilates the human circulation
Cosby, K., Partovi, K. S., Crawford, J. H., Patel, R. P., Reiter, C. D., Martyr, S., Yang, B. K., Waclawiw, M. A., Zalos, G., Xu, X., et al. (2003) · Nature Medicine · doi:10.1038/nm954 · Cited by 1,807
Identification of the haemoglobin scavenger receptor
Kristiansen, M., Graversen, J. H., Jacobsen, C., Sonne, O., Hoffman, H.-J., Law, S. K. A., & Moestrup, S. K. (2001) · Nature · doi:10.1038/35051594 · Cited by 1,712
Subarachnoid haemorrhage
van Gijn, J., Kerr, R. S. C., & Rinkel, G. J. E. (2007) · The Lancet · doi:10.1016/s0140-6736(07)60153-6 · Cited by 1,703
S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
Jia, L., Bonaventura, C., Bonaventura, J., & Stamler, J. S. (1996) · Nature · doi:10.1038/380221a0 · Cited by 1,592
Low density lipoprotein undergoes oxidative modification in vivo.
Palinski, W., Rosenfeld, M. E., Ylä‐Herttuala, S., Gurtner, G. C., Socher, S. S., Butler, S. W., Parthasarathy, S., Carew, T. E., Steinberg, D. H., & Witztum, J. L. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.4.1372 · Cited by 1,514
Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide: Implications for neurodegenerative diseases
Cleeter, M. W. J., Cooper, J. M., Darley-Usmar, V. M., Moncada, S., & Schapira, A. H. V. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00424-2 · Cited by 1,241
Identification of Epoxyeicosatrienoic Acids as Endothelium-Derived Hyperpolarizing Factors
Campbell, W. B., Gebremedhin, D., Pratt, P. F., & Harder, D. R. (1996) · Circulation Research · doi:10.1161/01.res.78.3.415 · Cited by 1,221
Identification of nitric oxide synthase as a protective locus against tuberculosis
MacMicking, J. D., North, R. J., LaCourse, R., Mudgett, J. S., Shah, S. K., & Nathan, C. F. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.10.5243 · Cited by 1,180
4-Hydroxy-2-nonenal: a product and mediator of oxidative stress
Uchida, K. (2003) · Progress in Lipid Research · doi:10.1016/s0163-7827(03)00014-6 · Cited by 1,164
An introduction to free radical biochemistry
Cheeseman, K. H., & Slater, T. F. (1993) · British Medical Bulletin · doi:10.1093/oxfordjournals.bmb.a072625 · Cited by 1,156
Killing of virulent Mycobacterium tuberculosis by reactive nitrogen intermediates produced by activated murine macrophages.
Chan, J., Xing, Y., Magliozzo, R. S., & Bloom, B. R. (1992) · The Journal of Experimental Medicine · doi:10.1084/jem.175.4.1111 · Cited by 1,062
Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase
Brown, G. C., & Cooper, C. E. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01290-3 · Cited by 1,055
Blood Flow Regulation by S -Nitrosohemoglobin in the Physiological Oxygen Gradient
Stamler, J. S., Jia, L., Eu, J. P., McMahon, T. J., Demchenko, I. T., Bonaventura, J., Gernert, K., & Piantadosi, C. A. (1997) · Science · doi:10.1126/science.276.5321.2034 · Cited by 1,050
A vertebrate globin expressed in the brain
Burmester, T., Weich, B., Reinhardt, S., & Hankeln, T. (2000) · Nature · doi:10.1038/35035093 · Cited by 1,025
Measurement of F2-isoprostanes as an index of oxidative stress in vivo
Roberts, L. J., & Morrow, J. D. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00264-6 · Cited by 1,000
Biological and clinical significance of haptoglobin polymorphism in humans
Langlois, M. R., & Delanghe, J. R. (1996) · Clinical Chemistry · doi:10.1093/clinchem/42.10.1589 · Cited by 942
Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism
Baldwin, J. M., & Chothia, C. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90277-8 · Cited by 872
NO News Is Good News
Culotta, E., & Koshland, D. E. (1992) · Science · doi:10.1126/science.1361684 · Cited by 805
Singlet oxygen production in photosynthesis
Krieger‐Liszkay, A. (2004) · Journal of Experimental Botany · doi:10.1093/jxb/erh237 · Cited by 794
Identification of the NF-E2-related Factor-2-dependent Genes Conferring Protection against Oxidative Stress in Primary Cortical Astrocytes Using Oligonucleotide Microarray Analysis
Lee, J., Calkins, M. J., Chan, K., Kan, Y. W., & Johnson, J. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211558200 · Cited by 783
X-ray Diffraction Study of Binding of 2,3-Diphosphoglycerate to Human Deoxyhaemoglobin
Arnone, A. (1972) · Nature · doi:10.1038/237146a0 · Cited by 733
Oxidative Stress and Cell Signalling
Poli, G., Leonarduzzi, G., Biasi, F., & Chiarpotto, E. (2004) · Current Medicinal Chemistry · doi:10.2174/0929867043365323 · Cited by 721
Induction of heme oxygenase is a rapid, protective response in rhabdomyolysis in the rat.
Nath, K. A., Balla, G., Vercellotti, G. M., Balla, J., Jacob, H. S., Levitt, M. D., & Rosenberg, M. E. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115847 · Cited by 685
Prokaryotic Cells in the Hydrothermal Vent Tube Worm Riftia pachyptila Jones: Possible Chemoautotrophic Symbionts
Cavanaugh, C. M., Gardiner, S. L., Jones, M. L., Jannasch, H. W., & Waterbury, J. B. (1981) · Science · doi:10.1126/science.213.4505.340 · Cited by 677
Oxidative stress in malaria parasite-infected erythrocytes: host–parasite interactions
Becker, K., Tilley, L. M., Vennerstrom, J. L., Roberts, D. J., Rogerson, S. J., & Ginsburg, H. (2003) · International Journal for Parasitology · doi:10.1016/j.ijpara.2003.09.011 · Cited by 665
Cell-Free Hemoglobin-Based Blood Substitutes and Risk of Myocardial Infarction and Death
Natanson, C., Kern, S. J., Lurie, P. G., Banks, S. M., & Wolfe, S. M. (2008) · JAMA · doi:10.1001/jama.299.19.jrv80007 · Cited by 624
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
The emerging biology of the nitrite anion
Gladwin, M. T., Schechter, A. N., Kim-Shapiro, D. B., Patel, R. P., Hogg, N., Shiva, S., Cannon, R. O., Kelm, M., Wink, D. A., Espey, M. G., et al. (2005) · Nature Chemical Biology · doi:10.1038/nchembio1105-308 · Cited by 609
Early Management of Shock and Prophylaxis of Acute Renal Failure in Traumatic Rhabdomyolysis
Desforges, J. F., Better, O. S., & Stein, J. H. (1990) · New England Journal of Medicine · doi:10.1056/nejm199003223221207 · Cited by 596
Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products
Levonen, A., Landar, A. L., Ramachandran, A., CEASER, E. K., Dickinson, D. A., Zanoni, G., Morrow, J. D., & Darley-Usmar, V. M. (2004) · Biochemical Journal · doi:10.1042/bj20031049 · Cited by 569
Reactions between nitric oxide and haemoglobin under physiological conditions
Gow, A. J., & Stamler, J. S. (1998) · Nature · doi:10.1038/34402 · Cited by 562
Imaging the production of singlet oxygen in vivo using a new fluorescent sensor, Singlet Oxygen Sensor Green(R)
Flors, C. (2006) · Journal of Experimental Botany · doi:10.1093/jxb/erj181 · Cited by 516
Biochemistry of Plasmodium (malarial parasites)
Sherman, I. W. (1979) · Microbiological Reviews · doi:10.1128/mr.43.4.453-495.1979 · Cited by 510
Hemoglobin degradation in the malaria parasite Plasmodium falciparum: an ordered process in a unique organelle.
Goldberg, D. E., Slater, A. F. G., Cerami, A., & Henderson, G. B. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.8.2931 · Cited by 498
Cytoglobin: A Novel Globin Type Ubiquitously Expressed inVertebrate Tissues
Burmester, T., Ebner, B., Weich, B., & Hankeln, T. (2002) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a004096 · Cited by 496
CHEMICAL PHYSIOLOGY OF BLOOD FLOW REGULATION BY RED BLOOD CELLS: The Role of Nitric Oxide and S-Nitrosohemoglobin
Singel, D. J., & Stamler, J. S. (2005) · Annual Review of Physiology · doi:10.1146/annurev.physiol.67.060603.090918 · Cited by 481
Nitric oxide in the human respiratory cycle
McMahon, T., Moon, R. E., Luschinger, B. P., Carraway, M. S., Stone, A. E., Stolp, B. W., Gow, A. J., Pawloski, J. R., Watke, P., Singel, D. J., et al. (2002) · Nature Medicine · doi:10.1038/nm718 · Cited by 462
Diaspirin Cross-Linked Hemoglobin (DCLHb) in the Treatment of Severe Traumatic Hemorrhagic Shock A Randomized Controlled Efficacy Trial
Sloan, E. P. (1999) · JAMA · doi:10.1001/jama.282.19.1857 · Cited by 459
Role of circulating nitrite and S -nitrosohemoglobin in the regulation of regional blood flow in humans
Gladwin, M. T., Shelhamer, J. H., Schechter, A. N., Pease-Fye, M. E., Waclawiw, M. A., Panza, J. A., Ognibene, F. P., & Cannon, R. O. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.21.11482 · Cited by 441
Heme oxygenase and heme degradation
Kikuchi, G., Yoshida, T., & Noguchi, M. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.020 · Cited by 433
Rate of reaction with nitric oxide determines the hypertensive effect of cell-free hemoglobin
Doherty, D. H., Doyle, M. P., Curry, S. R., Vali, R. J., Fattor, T., Olson, J. S., & Lemon, D. D. (1998) · Nature Biotechnology · doi:10.1038/nbt0798-672 · Cited by 432
Formation of Isoprostane-like Compounds (Neuroprostanes) in Vivo from Docosahexaenoic Acid*
Roberts, L., Montine, T., Markesbery, W., Tapper, A. R., Hardy, P., Chemtob, S., Dettbarn, W., & Morrow, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13605 · Cited by 430
Transcription Factor Nrf2 Regulates Inflammation by Mediating the Effect of 15-Deoxy-Δ12,14-Prostaglandin J2
Itoh, K., Mochizuki, M., Ishii, Y., Ishii, T., Shibata, T., Kawamoto, Y., Kelly, V., Sekizawa, K., Uchida, K., & Yamamoto, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.1.36-45.2004 · Cited by 407
Symbiotic chemoautotrophic bacteria in marine invertebrates from sulphide-rich habitats
Cavanaugh, C. M. (1983) · Nature · doi:10.1038/302058a0 · Cited by 405
Nontraumatic Rhabdomyolysis and Acute Renal Failure
GROSSMAN, R. A., Hamilton, R. W., Morse, B. M., Penn, A. S., & Goldberg, M. (1974) · New England Journal of Medicine · doi:10.1056/nejm197410172911601 · Cited by 377
Truncated Hemoglobins: A New Family of Hemoglobins Widely Distributed in Bacteria, Unicellular Eukaryotes, and Plants
Wittenberg, J. B., Bolognesi, M., Wittenberg, B. A., & Guertin, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.r100058200 · Cited by 376
Non-traumatic rhabdomyolysis and acute renal failure.
Chang, C.-H., Fang, J., & Huang, C. (1996) · PubMed · Cited by 367
A clinical safety trial of stroma‐free hemoglobin
Savitsky, J. P., Doczi, J., Black, J., & Arnold, J. D. (1978) · Clinical Pharmacology & Therapeutics · doi:10.1002/cpt197823173 · Cited by 359
A Ubiquitously Expressed Human Hexacoordinate Hemoglobin
Trent, J. T., & Hargrove, M. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201934200 · Cited by 358
Arabidopsis Nonsymbiotic Hemoglobin AHb1 Modulates Nitric Oxide Bioactivity
Perazzolli, M., Dominici, P., Romero‐Puertas, M. C., Zago, E. D., Zeier, J., Sonoda, M., Lamb, C. J., & Delledonne, M. (2004) · The Plant Cell · doi:10.1105/tpc.104.025379 · Cited by 340
Characterization of a Stellate Cell Activation-associated Protein (STAP) with Peroxidase Activity Found in Rat Hepatic Stellate Cells
Kawada, N., Kristensen, D. B., Asahina, K., Nakatani, K., Minamiyama, Y., Seki, S., & Yoshizato, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102630200 · Cited by 339
Deep-Sea Hydrocarbon Seep Communities: Evidence for Energy and Nutritional Carbon Sources
Brooks, J. M., Kennicutt, M. C., Fisher, C. R., Macko, S. A., Cole, K., Childress, J. J., Bidigare, R. R., & Vetter, R. D. (1987) · Science · doi:10.1126/science.238.4830.1138 · Cited by 328
Biochemistry of Plasmodium (malarial parasites).
Sherman, I. W. (1979) · Microbiological Reviews · doi:10.1128/mmbr.43.4.453-495.1979 · Cited by 326
Lipid peroxidation in erythrocytes
Clemens, M. R., & Waller, H. D. (1987) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(87)90068-5 · Cited by 318
A human recombinant haemoglobin designed for use as a blood substitute
Looker, D. L., Abbott‐Brown, D., Cozart, P., Durfee, S. L., Hoffman, S. J., Mathews, A. J., Miller-Roehrkh, J., Shoemaker, S. A., Trimble, S., Fermi, G., et al. (1992) · Nature · doi:10.1038/356258a0 · Cited by 316
Erythrocytes: Oxygen Sensors and Modulators of Vascular Tone
Ellsworth, M. L., Ellis, C. G., Goldman, D., Stephenson, A. H., Dietrich, H. H., & Sprague, R. S. (2009) · Physiology · doi:10.1152/physiol.00038.2008 · Cited by 315
Accelerated autoxidation and heme loss due to instability of sickle hemoglobin.
Hebbel, R. P., Morgan, W. T., Eaton, J. W., & Hedlund, B. E. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.1.237 · Cited by 306
Neuroglobin and cytoglobin
Pesce, A., Bolognesi, M., Bocedi, A., Ascenzi, P., Dewilde, S., Moens, L. J., Hankeln, T., & Burmester, T. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf248 · Cited by 298
Nitric oxide's reactions with hemoglobin: a view through the SNO-storm
Gladwin, M. T., Lancaster, J. R., Freeman, B. Α., & Schechter, A. N. (2003) · Nature Medicine · doi:10.1038/nm0503-496 · Cited by 290
Discrimination between Oxygen and Carbon Monoxide and Inhibition of Autooxidation by Myoglobin
Springer, B. A., Egeberg, K. D., Sligar, S. G., Rohlfs, R. J., Mathews, A. J., & Olson, J. S. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94029-9 · Cited by 288
CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin
Schaer, D. J., Schaer, C. A., Buehler, P. W., Boykins, R. A., Schoedon, G., Alayash, A. I., & Schaffner, A. (2006) · Blood · doi:10.1182/blood-2005-03-1014 · Cited by 285
The reaction between metmyoglobin and hydrogen peroxide
George, P., & Irvine, D. H. (1952) · Biochemical Journal · doi:10.1042/bj0520511 · Cited by 278
Disruption of myoglobin in mice induces multiple compensatory mechanisms
Gödecke, A., Flögel, U., Zanger, K., Ding, Z., Hirchenhain, J., Decking, U. K. M., & Schrader, J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10495 · Cited by 277
A Causative Role for Redox Cycling of Myoglobin and Its Inhibition by Alkalinization in the Pathogenesis and Treatment of Rhabdomyolysis-induced Renal Failure
Moore, K. P., Holt, S. G., Patel, R. P., Svistunenko, D. A., Zackert, W. E., Goodier, D., Reeder, B. J., Clozel, M., Anand, R., Cooper, C. E., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.48.31731 · Cited by 276
Self-citation
Heme oxygenase-1 affords protection against noncerebral forms of severe malaria
Seixas, E., Gozzelino, R., Chora, Â., Ferreira, A., Silva, G., Larsen, R., Rebelo, S., Penido, C., Smith, N. R., Coutinho, A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903419106 · Cited by 275
Two hemoglobin genes in Arabidopsis thaliana : The evolutionary origins of leghemoglobins
Trevaskis, B., Watts, R. A., Andersson, C. R., Llewellyn, D. J., Hargrove, M. S., Olson, J. S., Dennis, E. S., & Peacock, W. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.22.12230 · Cited by 269
Truncated hemoglobin HbN protects Mycobacterium bovis from nitric oxide
Ouellet, H., Ouellet, Y. H., Richard, C., Labarre, M., Wittenberg, B. A., Wittenberg, J. B., & Guertin, M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092017799 · Cited by 269
The Indispensability of Heme Oxygenase-1 in Protecting against Acute Heme Protein-Induced Toxicity in Vivo
Nath, K. A., Haggard, J. J., Croatt, A. J., Grande, J. P., Poss, K. D., & Alam, J. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65024-9 · Cited by 263
Neuroglobin, nitric oxide, and oxygen: Functional pathways and conformational changes
Brunori, M., Giuffrè, A., Nienhaus, K., Nienhaus, G. U., Scandurra, F. M., & Vallone, B. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408766102 · Cited by 261
Cell signaling by reactive nitrogen and oxygen species in atherosclerosis
Patel, R. P., Moellering, D. R., Murphy-Ullrich, J. E., Jo, H., Beckman, J. S., & Darley-Usmar, V. M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00235-5 · Cited by 243
Nitric Oxide Sensitivity of the Aconitases
Gardner, P. R., Costantino, G., Szabó, C., & Salzman, A. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.40.25071 · Cited by 237
Studies of mechanisms and protective maneuvers in myoglobinuric acute renal injury.
Zager, R. A. (1989) · PubMed · Cited by 234
A novel two‐over‐two α‐helical sandwich fold is characteristic of the truncated hemoglobin family
Pesce, A., Couture, M., Dewilde, S., Guertin, M., Yamauchi, K., Ascenzi, P., Moens, L., & Bolognesi, M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.11.2424 · Cited by 228
Catalytic generation of N2O3 by the concerted nitrite reductase and anhydrase activity of hemoglobin
Basu, S., Grubina, R., Huang, J., Conradie, J., Huang, Z., Jeffers, A., Jiang, A., He, X., Azarov, I., Seibert, R., et al. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.46 · Cited by 224
Controlled Safety Study of a Hemoglobin-Based Oxygen Carrier, DCLHb, in Acute Ischemic Stroke
Saxena, R. R., Wijnhoud, A. D., Carton, H., Hacke, W., Kaste, M., Przybelski, R. J., Stern, K. N., & Koudstaal, P. J. (1999) · Stroke · doi:10.1161/01.str.30.5.993 · Cited by 224
A novel antioxidant role for hemoglobin. The comproportionation of ferrylhemoglobin with oxyhemoglobin.
Giulivi, C., & Davies, K. J. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)45394-4 · Cited by 222
Radical Production and Scavenging in the Chloroplasts
Asada, K. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-48135-9_5 · Cited by 219
Nitric oxide moves myoglobin centre stage
Brunori, M. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01824-2 · Cited by 218
A Review of Blood Substitutes: Examining The History, Clinical Trial Results, and Ethics of Hemoglobin-Based Oxygen Carriers
Chen, J.-Y., Scerbo, M. H., & Kramer, G. C. (2009) · Clinics · doi:10.1590/s1807-59322009000800016 · Cited by 216
Increased Susceptibility in Hp Knockout Mice During Acute Hemolysis
Lim, S. K., Kim, H., Lim, S. K., bin Ali, A., Lim, Y. K., Wang, Y., Chong, S. M., Costantini, F. D., & Baumman, H. (1998) · Blood · doi:10.1182/blood.v92.6.1870 · Cited by 215
Clinical Experience with Hemoglobin-Saline Solutions
Amberson, W. R., Jennings, J. J., & Rhode, C. M. (1949) · Journal of Applied Physiology · doi:10.1152/jappl.1949.1.7.469 · Cited by 213
Current status of blood substitute research: towards a new paradigm
Winslow, R. M. (2003) · Journal of Internal Medicine · doi:10.1046/j.1365-2796.2003.01150.x · Cited by 208
The role of endothelium in the control of vascular tone
Busse, R., Trogisch, G., & Bassenge, E. (1985) · Basic Research in Cardiology · doi:10.1007/bf01907912 · Cited by 202
Reactions involving singlet oxygen and the superoxide anion
Koppenol, W. H. (1976) · Nature · doi:10.1038/262420a0 · Cited by 202
Sequestration of extracellular hemoglobin within a haptoglobin complex decreases its hypertensive and oxidative effects in dogs and guinea pigs
Boretti, F. S., Buehler, P. W., D’Agnillo, F., Kluge, K., Glaus, T. M., Butt, O. I., Jia, Y., Goede, J. S., Pereira, C. P., Maggiorini, M., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39115 · Cited by 198
Nitric oxide, cytochrome-c oxidase and myoglobin
Brunori, M. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01698-4 · Cited by 197
Pathogenesis of Renal Failure in Rhabdomyolysis: The Role of Myoglobin
Holt, S., & Moore, K. (2000) · Nephron Experimental Nephrology · doi:10.1159/000020651 · Cited by 197
Calcium Antagonists for Aneurysmal Subarachnoid Hemorrhage
Mees, S. M. D., Rinkel, G. J. E., Feigin, V. L., Algra, A., van den Bergh, W. M., Vermeulen, M., & van Gijn, J. (2008) · Stroke · doi:10.1161/strokeaha.107.496802 · Cited by 196
NAD(P)H Oxidase-Derived Reactive Oxygen Species as Mediators of Angiotensin II Signaling
Hanna, I. R., Taniyama, Y., Szöcs, K., Ročić, P., & Griendling, K. K. (2002) · Antioxidants and Redox Signaling · doi:10.1089/152308602762197443 · Cited by 195
Hemoglobins of the Lucina pectinata/bacteria symbiosis. I. Molecular properties, kinetics and equilibria of reactions with ligands.
Kraus, D. W., & Wittenberg, J. B. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46185-0 · Cited by 191
Oxidized Human Neuroglobin Acts as a Heterotrimeric Gα Protein Guanine Nucleotide Dissociation Inhibitor
Wakasugi, K., Nakano, T., & Morishima, I. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305519200 · Cited by 190
Reactions of the Protein Radical in Peroxide-treated Myoglobin
Catalano, C. E., Choe, Y., & de Montellano, P. R. O. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81654-4 · Cited by 185
Use of desferrioxamine as a ‘probe’ for iron-dependent formation of hydroxyl radicals
Halliwell, B. B. (1985) · Biochemical Pharmacology · doi:10.1016/0006-2952(85)90129-7 · Cited by 184
Acetaminophen inhibits hemoprotein-catalyzed lipid peroxidation and attenuates rhabdomyolysis-induced renal failure
Boutaud, O. G., Moore, K. P., Reeder, B. J., Harry, D. S., Howie, A. J., Wang, S., Carney, C. K., Masterson, T. S., Amin, T., Wright, D. W., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910174107 · Cited by 184
Self-citation
Nanotransducers in cellular redox signaling: modification of thiols by reactive oxygen and nitrogen species
Cooper, C. E., Patel, R. P., Brookes, P. S., & Darley-Usmar, V. M. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02191-6 · Cited by 180
Crystal structure of a nonsymbiotic plant hemoglobin
Hargrove, M. S., Brucker, E. A., Stec, B., Sarath, G., Arredondo‐Peter, R., Klucas, R. V., Olson, J. S., & Phillips, G. N. (2000) · Structure · doi:10.1016/s0969-2126(00)00194-5 · Cited by 175
Modulation of nitric oxide bioavailability by erythrocytes
Huang, K., Han, T. H., Hyduke, D. R., Vaughn, M. W., Herle, H. M.-L. V., Hein, T. W., Zhang, C., Kuo, L., & Liao, J. C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.201276698 · Cited by 172
Hemoglobin and Myoglobin Associated Oxidative Stress: from Molecular Mechanisms to Disease States
Reeder, B. J., & Wilson, M. T. (2005) · Current Medicinal Chemistry · doi:10.2174/092986705774463021 · Cited by 169
Self-citation
Thioredoxin as a Molecular Target of Cyclopentenone Prostaglandins
Shibata, T., Yamada, T., Ishii, T., Kumazawa, S., Nakamura, H., Masutani, H., Yodoi, J., & Uchida, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303690200 · Cited by 160
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
Hemoglobin in a Nonleguminous Plant, Parasponia : Possible Genetic Origin and Function in Nitrogen Fixation
Appleby, C. A., Tjepkema, J. D., & Trinick, M. J. (1983) · Science · doi:10.1126/science.220.4600.951 · Cited by 158
SNO-hemoglobin is not essential for red blood cell–dependent hypoxic vasodilation
Isbell, T. S., Sun, C.-W., Wu, L.-C., Teng, X., Vitturi, D. A., Branch, B. G., Kevil, C. G., Peng, N., Wyss, J. M., Ambalavanan, N., et al. (2008) · Nature Medicine · doi:10.1038/nm1771 · Cited by 157
Reaction of haem containing proteins and enzymes with hydroperoxides: The radical view
Svistunenko, D. A. (2005) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2005.01.004 · Cited by 155
Formation of Reactive Cyclopentenone Compounds in Vivo as Products of the Isoprostane Pathway
Chen, Y., Morrow, J. D., & Roberts, L. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.16.10863 · Cited by 155
Mechanisms of compound I formation in heme peroxidases
Hiner, A. N. P., Raven, E. L., THORNELEY, R. N. F., Garcı́a-Cánovas, F., & Rodríguez‐López, J. N. (2002) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(02)00390-2 · Cited by 151
Structural Basis of Peroxide-mediated Changes in Human Hemoglobin
Jia, Y., Buehler, P. W., Boykins, R. A., Venable, R. M., & Alayash, A. I. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609955200 · Cited by 151
Malaria-parasitized erythrocytes and hemozoin nonenzymatically generate large amounts of hydroxy fatty acids that inhibit monocyte functions
Schwarzer, E., Kühn, H., Valente, E., & Arese, P. (2002) · Blood · doi:10.1182/blood-2002-03-0979 · Cited by 147
Diaspirins that crosslink .beta. chains of hemoglobin: bis(3,5-dibromosalicyl) succinate and bis(3,5-dibromosalicyl) fumarate
Walder, J. A., Zaugg, R. H., Walder, R. Y., Steele, J. M., & Klotz, I. M. (1979) · Biochemistry · doi:10.1021/bi00587a001 · Cited by 144
Reactions of ferrous neuroglobin and cytoglobin with nitrite under anaerobic conditions
Petersen, M. G., Dewilde, S., & Fago, A. (2008) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2008.05.008 · Cited by 144
Biphasic Effects of 15-Deoxy-Δ 12,14 -Prostaglandin J 2 on Glutathione Induction and Apoptosis in Human Endothelial Cells
Levonen, A., Dickinson, D. A., Moellering, D. R., Mulcahy, R., Forman, H. J., & Darley-Usmar, V. M. (2001) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq1101.098488 · Cited by 141
Lipid Peroxyl Radical Intermediates in the Peroxidation of Polyunsaturated Fatty Acids by Lipoxygenase
Chamulitrat, W., & Mason, R. P. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)30031-6 · Cited by 140
Molecular Characterization of the Haptoglobin·Hemoglobin Receptor CD163
Madsen, M. M., Møller, H. J., Nielsen, M. J., Jacobsen, C. B., Graversen, J. H., van den Berg, T. K., & Moestrup, S. K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409629200 · Cited by 140
The oxidation of myoglobin to metmyoglobin by oxygen. 2. The relation between the first order rate constant and the partial pressure of oxygen
George, P., & Stratmann, C. J. (1952) · Biochemical Journal · doi:10.1042/bj0510418 · Cited by 140
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
Phase I study of the safety and pharmacologic effects of diaspirin cross-linked hemoglobin solution
Przybelski, R. J., Daily, E. K., Kisicki, J. C., Mattia‐Goldberg, C., Bounds, M. J., & Colburn, W. A. (1996) · Critical Care Medicine · doi:10.1097/00003246-199612000-00011 · Cited by 138
Cytoglobin/STAP, its unique localization in splanchnic fibroblast-like cells and function in organ fibrogenesis
Nakatani, K., Okuyama, H., Shimahara, Y., Saeki, S., Kim, D.-H., Nakajima, Y., Seki, S., Kawada, N., & Yoshizato, K. (2004) · Laboratory Investigation · doi:10.1038/labinvest.3700013 · Cited by 137
Site-specific spin trapping of tyrosine radicals in the oxidation of metmyoglobin by hydrogen peroxide
GUNTHER, R. M., Tschirret-Guth, R. A., Witkowska, H. E., FANN, C. Y., BARR, P. D., de Montellano, P. R. O., & Mason, R. P. (1998) · Biochemical Journal · doi:10.1042/bj3301293 · Cited by 136
Increased lipid peroxidation in patients with rhabdomyolysis
Holt, S., Reeder, B. J., Wilson, M., Harvey, S. E., Morrow, J. D., Roberts, L. J., & Moore, K. P. (1999) · The Lancet · doi:10.1016/s0140-6736(98)05768-7 · Cited by 135
Self-citation
Oxidative stress in malaria; implications for prevention and therapy
Postma, N. S., Zuidema, J., Momm�rs, E. C., & Eling, W. M. C. (1996) · Pharmacy World & Science · doi:10.1007/bf00717727 · Cited by 134
Intrarenal Hemodynamics in Glycerol-Induced Myohemoglobinuric Acute Renal Failure in the Rat
Ayer, G., Grandchamp, A., Wyler, T., & Truniger, B. (1971) · Circulation Research · doi:10.1161/01.res.29.2.128 · Cited by 132
Effects of neuroglobin overexpression on mitochondrial function and oxidative stress following hypoxia/reoxygenation in cultured neurons
Liu, J., Yu, Z., Guo, S., Lee, S., Xing, C., Zhang, C., Gao, Y., Nicholls, D. G., Lo, E. H., & Wang, X. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21826 · Cited by 131
Effects of Chloroquine on the Feeding Mechanism of the Intraerythrocytic Human Malarial Parasite Plasmodium falciparum1
Yayon, A., Timberg, R., Friedman, S., & Ginsburg, H. (1984) · The Journal of Protozoology · doi:10.1111/j.1550-7408.1984.tb02981.x · Cited by 130
The biochemistry of the isoprostane, neuroprostane, and isofuran pathways of lipid peroxidation
Roberts, L. J., & Fessel, J. P. (2003) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2003.09.016 · Cited by 129
Neuroglobin and cytoglobin expression in mice
Fordel, E., Thijs, L., Moens, L. J., & Dewilde, S. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05679.x · Cited by 126
Iron and 8-isoprostane levels in acute and chronic wounds
Yeoh-Ellerton, S., & Stacey, M. C. (2003) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2003.12471.x · Cited by 125
Tyrosine Residues as Redox Cofactors in Human Hemoglobin
Reeder, B. J., Grey, M., Silaghi-Dumitrescu, R. L., Svistunenko, D. A., Bülow, L., Cooper, C. E., & Wilson, M. T. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804709200 · Cited by 124
Self-citation
Free Radical produced in the Reaction of Metmyoglobin with Hydrogen Peroxide
Gibson, J. F., Ingram, D. J. E., & Nicholls, P. J. (1958) · Nature · doi:10.1038/1811398a0 · Cited by 121
Soluble dextran-hemoglobin complex as a potential blood substitute.
Tam, S., Blumenstein, J., & Wong, J. T.-F. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.6.2128 · Cited by 119
Sulfide binding is mediated by zinc ions discovered in the crystal structure of a hydrothermal vent tubeworm hemoglobin
Flores, J. F., Fisher, C. R., Carney, S. L., Green, B. N., Freytag, J. K., Schaeffer, S. W., & Royer, W. E. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407455102 · Cited by 119
p38 MAP kinase pathway regulates angiotensin II-induced contraction of rat vascular smooth muscle
Meloche, S., Landry, J., Huot, J., Houle, F., Marceau, F., & Giasson, E. (2000) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2000.279.2.h741 · Cited by 119
Myoglobin as a model system for designing heme protein based blood substitutes
Dou, Y., Maillett, D. H., Eich, R. F., & Olson, J. S. (2002) · Biophysical Chemistry · doi:10.1016/s0301-4622(02)00090-x · Cited by 118
The Globin-based Free Radical of Ferryl Hemoglobin Is Detected in Normal Human Blood
Svistunenko, D. A., Patel, R. P., Voloshchenko, S. V., & Wilson, M. T. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.11.7114 · Cited by 117
Heme degradation and oxidative stress in murine models for hemoglobinopathies: Thalassemia, sickle cell disease and hemoglobin C disease
Nagababu, E., Fabry, M. E., Nagel, R. L., & Rifkind, J. M. (2008) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2007.12.003 · Cited by 114
Mechanisms of Cell Signaling by Nitric Oxide and Peroxynitrite: From Mitochondria to MAP Kinases
Levonen, A., Patel, R. P., Brookes, P. S., Go, Y., Jo, H., Parthasarathy, S., Anderson, P. G., & Darley-Usmar, V. M. (2001) · Antioxidants and Redox Signaling · doi:10.1089/152308601300185188 · Cited by 113
Effect of ferritin-containing fractions with different iron loading on lipid peroxidation
Gutteridge, J. M. C., Halliwell, B. B., Treffry, A., Harrison, P. M., & Blake, D. R. (1983) · Biochemical Journal · doi:10.1042/bj2090557 · Cited by 113
The enzymatic oxidation of Desferal to a nitroxide free radical
Morehouse, K. M., Flitter, W. D., & Mason, R. P. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)80379-4 · Cited by 112
Iron Chelation Therapy for Malaria
Mabeza, G. F., Loyevsky, M., Gordeuk, V. R., & Weiss, G. (1999) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(98)00037-0 · Cited by 111
The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: a role for the protonated ferryl species
Reeder, B. J., & Wilson, M. T. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00534-2 · Cited by 109
Self-citation
Structural hierarchy in erythrocruorin, the giant respiratory assemblage of annelids
Royer, W. E., Strand, K., van Heel, M., & Hendrickson, W. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.13.7107 · Cited by 108
Toxicological Consequences of Extracellular Hemoglobin: Biochemical and Physiological Perspectives
Buehler, P. W., & D’Agnillo, F. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2799 · Cited by 107
Accumulation of 15-deoxy-Δ12,14-prostaglandin J2 adduct formation with Keap1 over time: effects on potency for intracellular antioxidant defence induction
Oh, J. Y., Giles, N. M., Landar, A. L., & Darley-Usmar, V. M. (2008) · Biochemical Journal · doi:10.1042/bj20071189 · Cited by 106
Current status of oxygen carriers (‘blood substitutes’): 2006
Winslow, R. M. (2006) · Vox Sanguinis · doi:10.1111/j.1423-0410.2006.00789.x · Cited by 105
Hemoglobin-Mediated, Hypoxia-Induced Vasodilation via Nitric Oxide
Robinson, J. M., & Lancaster, J. R. (2005) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.f292 · Cited by 104
Toxicity of myoglobin and haemoglobin: oxidative stress in patients with rhabdomyolysis and subarachnoid haemorrhage
Reeder, B. J., Sharpe, M. A., Kay, A. D., Kerr, M., Moore, K. P., & Wilson, M. T. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300745 · Cited by 104
Self-citation
The Role of Phospholipases, Cyclooxygenases, and Lipoxygenases in Cerebral Ischemic/Traumatic Injuries
Phillis, J. W., & O’Regan, M. H. (2003) · Critical Reviews in Neurobiology · doi:10.1615/critrevneurobiol.v15.i1.30 · Cited by 102
Oxygen‐binding haem proteins
Wilson, M. T., & Reeder, B. J. (2007) · Experimental Physiology · doi:10.1113/expphysiol.2007.039735 · Cited by 101
Self-citation
Haptoglobin Phenotypes Differ in Their Ability To Inhibit Heme Transfer from Hemoglobin to LDL
Bamm, V. V., Tsemakhovich, V., Shaklai, M., & Shaklai, N. (2004) · Biochemistry · doi:10.1021/bi0362626 · Cited by 101
The oxidation of myoglobin to metmyoglobin by oxygen. 1
George, P., & Stratmann, C. J. (1952) · Biochemical Journal · doi:10.1042/bj0510103 · Cited by 98
Cytoglobin Up-regulated by Hydrogen Peroxide Plays a Protective Role in Oxidative Stress
Li, D., Chen, X., Li, W.-J., Yang, Y., Wang, J., & Yu, A. C. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9317-x · Cited by 97
Peroxidase Activity of Hemoglobin·Haptoglobin Complexes
Kapralov, A., Vlasova, I. I., Feng, W., Maeda, A., Walson, K., Tyurin, V. A., Huang, Z., Aneja, R. K., Carcillo, J., Bayır, H., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.045567 · Cited by 96
Kinetics of the reactions of nitrogen monoxide and nitrite with ferryl hemoglobin
Herold, S., & Rehmann, F. K. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01355-2 · Cited by 95
A Model for Ligand Binding to Hexacoordinate Hemoglobins
Trent, J. T., Hvitved, A. N., & Hargrove, M. S. (2001) · Biochemistry · doi:10.1021/bi0100790 · Cited by 92
Characteristics and Mechanism of Formation of Peroxide-Induced Heme to Protein Cross-Linking in Myoglobin
Reeder, B. J., Svistunenko, D. A., Sharpe, M. A., & Wilson, M. T. (2001) · Biochemistry · doi:10.1021/bi011335b · Cited by 92
Self-citation
Constitutive and Adaptive Detoxification of Nitric Oxide in Escherichia coli
Gardner, P. R., Costantino, G., & Salzman, A. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.41.26528 · Cited by 89
Mechanisms of signal transduction mediated by oxidized lipids: the role of the electrophile-responsive proteome
CEASER, E. K., Moellering, D. R., Shiva, S., Ramachandran, A., Landar, A. L., Venkartraman, A., Crawford, J., Patel, R. P., Dickinson, D. A., Ulasova, E., et al. (2004) · Biochemical Society Transactions · doi:10.1042/bst0320151 · Cited by 87
Ferryl haem protonation gates peroxidatic reactivity in globins
Silaghi-Dumitrescu, R. L., Reeder, B. J., Nicholls, P. J., Cooper, C. E., & Wilson, M. T. (2007) · Biochemical Journal · doi:10.1042/bj20061421 · Cited by 85
Self-citation
Review Lecture - Stereochemical mechanism of oxygen transport by haemoglobin
Perutz, M. F. (1980) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.1980.0047 · Cited by 83
Interaction between hemoglobin subunits in the hemoglobin . haptoglobin complex.
Hwang, P. K., & Greer, J. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85848-9 · Cited by 82
Hypoxia/Ischemia and the Regulation of Neuroglobin and Cytoglobin Expression
Fordel, E., Geuens, E., Dewilde, S., Coen, W. D., & Moens, L. J. (2004) · IUBMB Life · doi:10.1080/15216540500037406 · Cited by 82
Increase in plasma esterified F2-isoprostanes following intravenous iron infusion in patients on hemodialysis
Salahudeen, A. K., Oliver, B. L., Bower, J. D., & Roberts, L. J. (2001) · Kidney International · doi:10.1046/j.1523-1755.2001.00976.x · Cited by 82
Nitric oxide and cellular respiration
Brunori, M., Giuffr�, A., Sarti, P., Stubauer, G., & Wilson, M. T. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050452 · Cited by 81
Mitochondrial free radical production induces lipid peroxidation during myohemoglobinuria
Zager, R. A. (1996) · Kidney International · doi:10.1038/ki.1996.103 · Cited by 81
Expression of NO scavenging hemoglobin is involved in the timing of bolting in Arabidopsis thaliana
Hebelstrup, K. H., & Jensen, E. Ø. (2007) · Planta · doi:10.1007/s00425-007-0667-z · Cited by 79
Iron chelators can protect against oxidative stress through ferryl heme reduction
Reeder, B. J., Hider, R. C., & Wilson, M. T. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.08.006 · Cited by 79
Self-citation
Reactions of Sperm Whale Myoglobin with Hydrogen Peroxide
Alayash, A. I., Ryan, B. A. B., Eich, R. F., Olson, J. S., & Cashon, R. E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.4.2029 · Cited by 79
Effects of polymerization on the hypertensive action of diaspirin cross-linked hemoglobin in rats
Abassi, Z. A., Kotob, S., Pieruzzi, F., Abouassali, M., Keiser, H. R., Fratantoni, J. C., & Alayash, A. I. (1997) · Journal of Laboratory and Clinical Medicine · doi:10.1016/s0022-2143(97)90194-3 · Cited by 79
Structural Bases for Sulfide Recognition inLucina pectinataHemoglobin I
Rizzi, M., Wittenberg, J. B., Coda, A., Ascenzi, P., & Bolognesi, M. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0228 · Cited by 78
Ectopic Expression of the Cotton Non-symbiotic Hemoglobin Gene GhHbd1 Triggers Defense Responses and Increases Disease Tolerance in Arabidopsis
Qu, Z.-L., Zhong, N., Wang, H., Chen, A., Jian, G., & Xia, G. (2006) · Plant and Cell Physiology · doi:10.1093/pcp/pcj076 · Cited by 76
Modification of human hemoglobin with polyethylene glycol: A new candidate for blood substitute
Ajisaka, K., & Iwashita, Y. (1980) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(80)91485-0 · Cited by 75
Blood Components Prevent Sulfide Poisoning of Respiration of the Hydrothermal Vent Tube Worm Riftia pachyptila
Powell, M. A., & Somero, G. N. (1983) · Science · doi:10.1126/science.219.4582.297 · Cited by 75
Redox cycling of diaspirin cross-linked hemoglobin induces G2/M arrest and apoptosis in cultured endothelial cells
D’Agnillo, F., & Alayash, A. I. (2001) · Blood · doi:10.1182/blood.v98.12.3315 · Cited by 75
A Study of the Effectiveness of the Iron-Chelating Agent Deferoxamine as Vasospasm Prophylaxis in a Rabbit Model of Subarachnoid Hemorrhage
Vollmer, D. G., Hongo, K., Ogawa, H., Tsukahara, T., & Kassell, N. F. (1991) · Neurosurgery · doi:10.1227/00006123-199101000-00005 · Cited by 75
Cytoglobin is upregulated by tumour hypoxia and silenced by promoter hypermethylation in head and neck cancer
Shaw, R., Omar, M. M., Rokadiya, S., Kogera, F., Lowe, D., Hall, G. L., Woolgar, J. A., Homer, J. J., Liloglou, T., Field, J. K., et al. (2009) · British Journal of Cancer · doi:10.1038/sj.bjc.6605121 · Cited by 74
Hemoglobin Can Attenuate Hydrogen Peroxide–Induced Oxidative Stress by Acting as an Antioxidative Peroxidase
Widmer, C. C., Pereira, C. P., Gehrig, P., Vallelian, F., Schoedon, G., Buehler, P. W., & Schaer, D. J. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2826 · Cited by 73
Multiple wavelength analysis of the reaction between hydrogen peroxide and metmyoglobin
Fox, J. B., Nicholas, R. A., Ackerman, S. A., & Swift, C. E. (1974) · Biochemistry · doi:10.1021/bi00722a020 · Cited by 73
A new sensitive assay reveals that hemoglobin is oxidatively modified in vivo
Vollaard, N. B. J., Reeder, B. J., Shearman, J., Menu, P., Wilson, M. T., & Cooper, C. E. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.06.012 · Cited by 72
Self-citation
A role for neuroglobin: Resetting the trigger level for apoptosis in neuronal and retinal cells
Fago, A., Mathews, A. J., & Brittain, T. (2008) · IUBMB Life · doi:10.1002/iub.35 · Cited by 72
Hemodynamic effect of the nitroxide superoxide dismutase mimics
Hahn, S. M., Sullivan, F. J., DeLuca, A. M., Bacher, J. D., Liebmann, J., Krishna, M. C., Coffin, D., & Mitchell, J. B. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00099-4 · Cited by 72
Oxidative modification by low levels of HOOH can transform myoglobin to an oxidase.
Osawa, Y., & Korzekwa, K. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.16.7081 · Cited by 71
Cell-free oxygen carriers: Scientific foundations, clinical development, and new directions
Winslow, R. M. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.04.032 · Cited by 71
Mechanism of reaction of myoglobin with the lipid hydroperoxide hydroperoxyoctadecadienoic acid
Reeder, B. J., & Wilson, T. (1998) · Biochemical Journal · doi:10.1042/bj3301317 · Cited by 69
Self-citation
Autoxidation of Native Oxymyoglobin. Kinetic Analysis of the pH Profile
Shikama, K., & Sugawara, Y. (1978) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1978.tb12693.x · Cited by 67
Tyrosine as a redox-active center in electron transfer to ferryl heme in globins
Reeder, B. J., Cutruzzolà, F., Bigotti, M. G., Hider, R. C., & Wilson, M. T. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.06.030 · Cited by 67
Self-citation
Heme oxygenase-1 gene therapy for prevention of vasospasm in rats
Ono, S., Komuro, T., & Macdonald, R. L. (2002) · Journal of neurosurgery · doi:10.3171/jns.2002.96.6.1094 · Cited by 66
Processing of Excitation Energy by Antenna Pigments
Owens, T. G. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-48135-9_1 · Cited by 64
Oxidation and Reduction of Leghemoglobin in Root Nodules of Leguminous Plants
Becana, M., & Klucas, R. V. (1992) · PLANT PHYSIOLOGY · doi:10.1104/pp.98.4.1217 · Cited by 64
Reactivity and endogenous modification by nitrite and hydrogen peroxide: does human neuroglobin act only as a scavenger?
Nicolis, S., Monzani, E., Ciaccio, C., Ascenzi, P., Moens, L., & Casella, L. (2007) · Biochemical Journal · doi:10.1042/bj20070372 · Cited by 63
Role of Pre-A Motif in Nitric Oxide Scavenging by Truncated Hemoglobin, HbN, of Mycobacterium tuberculosis
Lama, A., Pawaria, S., Bidon‐Chanal, A., Anand, A., Gelpí, J. L., Arya, S., Marti, M. A., Estrin, D. A., Luque, F. J., & Dikshit, K. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807436200 · Cited by 63
The Role of a Zinc-Based, Serum-Borne Sulphide-Binding Component in the Uptake and Transport of Dissolved Sulphide by the Chemoautotrophic Symbiont-Containing Clam Calyptogena Elongata
Childress, J. J., Fisher, C. R., Favuzzi, J. A., Arp, A. J., & Oros, D. R. (1993) · Journal of Experimental Biology · doi:10.1242/jeb.179.1.131 · Cited by 62
Quaternary Structure of Rice Nonsymbiotic Hemoglobin
Goodman, M. D., & Hargrove, M. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009254200 · Cited by 60
Functional Modulation by Lactate of Myoglobin
Giardina, B., Ascenzi, P., Clementi, M. E., Sanctis, G. D., Rizzi, M., & Coletta, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.29.16999 · Cited by 59
The freeze-dried preservation of liposome encapsulated hemoglobin: A potential blood substitute
Rudolph, A. S. (1988) · Cryobiology · doi:10.1016/0011-2240(88)90036-3 · Cited by 57
The binding of cytochrome c to neuroglobin: A docking and surface plasmon resonance study
Bønding, S. H., Henty, K., Dingley, A. J., & Brittain, T. (2008) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2008.07.003 · Cited by 57
Free fatty acids in human cerebrospinal fluid following subarachnoid hemorrhage and their potential role in vasospasm: a preliminary observation
Pilitsis, J. G., Coplin, W. M., O’Regan, M. H., Wellwood, J. M., Diaz, F. G., Fairfax, M. R., Michael, D. B., & Phillis, J. W. (2002) · Journal of neurosurgery · doi:10.3171/jns.2002.97.2.0272 · Cited by 56
ROLE OF REDOX POTENTIAL OF HEMOGLOBIN-BASED OXYGEN CARRIERS ON METHEMOGLOBIN REDUCTION BY PLASMA COMPONENTS
Dorman, S. C., Kenny, C. F., Miller, L., Hirsch, R. E., & Harrington, J. P. (2002) · Artificial Cells Blood Substitutes and Biotechnology · doi:10.1081/bio-120002726 · Cited by 56

Research works printed but not linked: 10

Antonini E, 1971, Frontiers in Biology, 13
Boretti FS, 2009, J Clin Invest, 119, 2271
Delacollette C, 1995, Ann Soc Belg Med Trop, 75, 51
Destro Bisol G, 1999, Parasitologia, 41, 203
Goldman DW, 1998, Am J Physiol, 275, H1046
McLeod LL, 1999, Am J Physiol, 277, H92
Palasuwan A, 2005, Southeast Asian J Trop Med Public Health, 36, 271
Palasuwan A, 2006, Southeast Asian J Trop Med Public Health, 37, 184
Styblo K, 1980, Adv Tuberc Res, 20, 1
Zager RA, 1989, Lab Invest, 60, 619

Sorted by citations

Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release
Zorov, D. B., Juhaszova, M., & Sollott, S. J. (2014) · Physiological Reviews · doi:10.1152/physrev.00026.2013 · Cited by 5,383
Hemolysis and free hemoglobin revisited: exploring hemoglobin and hemin scavengers as a novel class of therapeutic proteins
Schaer, D. J., Buehler, P. W., Alayash, A. I., Belcher, J. D., & Vercellotti, G. M. (2013) · Blood · doi:10.1182/blood-2012-11-451229 · Cited by 754
Intravascular hemolysis and the pathophysiology of sickle cell disease
Kato, G. J., Steinberg, M. H., & Gladwin, M. T. (2017) · Journal of Clinical Investigation · doi:10.1172/jci89741 · Cited by 748
Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia
Kuhn, V., Diederich, L., Keller, T. C. S., Kramer, C. M., Lückstädt, W., Panknin, C., Suvorava, T., Isakson, B. E., Kelm, M., & Cortese-Krott, M. M. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6954 · Cited by 469
Protective Role for Antioxidants in Acute Kidney Disease
Dennis, J. M., & Witting, P. K. (2017) · Nutrients · doi:10.3390/nu9070718 · Cited by 298

See all 189

Authors: Reeder, B. J.
Affiliations: University of Essex (GB)
Corresponding author: Reeder, Brandon J.
ORCID: Reeder, Brandon J.
Venue: Antioxidants & Redox Signaling
Publisher: SAGE Publications
Published: 2010-10
Volume: 13
Issue: 7
Pages: 1087-1123
ISSN: 1523-0864 (ISSN-L)
1557-7716
DOI: 10.1089/ars.2009.2974
OpenAlex: W2024968752
Cited by: 189
References: 294
Citations by year: 2026: 9 · 2025: 5 · 2024: 7 · 2023: 11 · 2022: 11 · 2021: 11 · 2020: 12 · 2019: 11 · 2018: 7 · 2017: 20 · 2016: 19 · 2015: 15 · 2014: 13 · 2013: 14 · 2012: 13
FWCI: 1.06
Type: journal article
Language: en
Open access: closed
Locations: Antioxidants and Redox Signaling (publishedVersion)
PubMed (publishedVersion)
Open Access at Essex (University of Essex) (submittedVersion)
Funders: Biotechnology and Biological Sciences Research Council
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
Keywords: hemoglobin, myoglobin, globin, oxidative enzymes, heme proteins, nitric oxide, peroxides, ferryl hemoglobin, oxidative damage, cytotoxicity, signal transduction, hemoglobin-based blood substitutes, plant hemoglobin
MeSH terms: Neuroglobin, Cytoglobin, Animals, Blood Substitutes, Globins, Heme, Hemeproteins, Hemoglobins, Humans, Myoglobin, Nerve Tissue Proteins, Nitric Oxide, Oxidation-Reduction, Oxygen, Peroxides, Signal Transduction

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

The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks