The DOI matches its Crossref record; 98 of the 100 references it cites were found in a registry or an index.
Myoglobin function reassessed
Abstract
The heart and those striated muscles that contract for long periods, having available almost limitless oxygen, operate in sustained steady states of low sarcoplasmic oxygen pressure that resist change in response to changing muscle work or oxygen supply. Most of the oxygen pressure drop from the erythrocyte to the mitochondrion occurs across the capillary wall. Within the sarcoplasm, myoglobin, a mobile carrier of oxygen, is developed in response to mitochondrial demand and augments the flow of oxygen to the mitochondria. Myoglobin-facilitated oxygen diffusion, perhaps by virtue of reduction of dimensionality of diffusion from three dimensions towards two dimensions in the narrow spaces available between mitochondria, is rapid relative to other parameters of cell respiration. Consequently, intracellular gradients of oxygen pressure are shallow, and sarcoplasmic oxygen pressure is nearly the same everywhere. Sarcoplasmic oxygen pressure, buffered near 0.33 kPa (2.5 torr; equivalent to approximately 4 micro mol l(-1) oxygen) by equilibrium with myoglobin, falls close to the operational K(m) of cytochrome oxidase for oxygen, and any small increment in sarcoplasmic oxygen pressure will be countered by increased oxygen utilization. The concentration of nitric oxide within the myocyte results from a balance of endogenous synthesis and removal by oxymyoglobin-catalyzed dioxygenation to the innocuous nitrate. Oxymyoglobin, by controlling sarcoplasmic nitric oxide concentration, helps assure the steady state in which inflow of oxygen into the myocyte equals the rate of oxygen consumption.
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In the citing paper
“the high concentrations of hemoglobin and myoglobin in red blood cells (20 mM) and cardiac/skeletal muscle (300-900 μM) [31, 32], determines that the reaction between their hemes and NO will be fast and might inhibit NO-signaling.”
From Current perspectives and challenges in understanding the role of nitrite as an integral player in nitric oxide biology and therapy (2011) · cites this paper as [32]
In the citing paper
“In fact, the role of myoglobin as an NO scavenger in skeletal muscle to prevent its toxicity had been proposed [35; 36].”
From Skeletal muscle as an endogenous nitrate reservoir (2015) · cites this paper as [36]
Citations
Cites
Berg, H. C. (1984) · Princeton University Press eBooks · doi:10.1515/9780691279886 · Cited by 2,417
Keener, J. P., & Sneyd, J. (2009) · Interdisciplinary applied mathematics · doi:10.1007/978-0-387-75847-3 · Cited by 2,213
Structural chemistry and molecular biology
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Krogh, A. (1919) · The Journal of Physiology · doi:10.1113/jphysiol.1919.sp001839 · Cited by 1,433
Does nitric oxide modulate mitochondrial energy generation and apoptosis?
Moncada, S., & Erusalimsky, J. D. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm762 · Cited by 794
Leghemoglobin and Rhizobium Respiration
Appleby, C. A. (1984) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.pp.35.060184.002303 · Cited by 679
THE ULTRASTRUCTURE OF THE CAT MYOCARDIUM
Fawcett, D. W., & McNutt, N. S. (1969) · The Journal of Cell Biology · doi:10.1083/jcb.42.1.1 · Cited by 566
Myoglobin-facilitated oxygen diffusion: role of myoglobin in oxygen entry into muscle.
Wittenberg, J. B. (1970) · Physiological Reviews · doi:10.1152/physrev.1970.50.4.559 · Cited by 565
Self-citationThe supply of oxygen to the tissues and the regulation of the capillary circulation
Krogh, A. (1919) · The Journal of Physiology · doi:10.1113/jphysiol.1919.sp001844 · Cited by 530
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2 of the 100 references couldn’t be matched to a known paper.
Research works printed but not linked: 2
- Fawcett, D. W. (1966). An Atlas of Fine Structure. Philadelphia: W. B. Saunders.
- Klucas, R. V., Lee, K. K., Saari, L. and Erickson, B. K.(1985). Factors Effecting Functional Leghemoglobin in Legume Nodules. New York: Elsevier Science.
Cited by
Sorted by citations
Principles, Techniques, and Limitations of Near Infrared Spectroscopy
Ferrari, M., Mottola, L., & Quaresima, V. (2004) · Canadian Journal of Applied Physiology · doi:10.1139/h04-031 · Cited by 997
Myoglobin Chemistry and Meat Color
Suman, S. P., & Joseph, P. (2012) · Annual Review of Food Science and Technology · doi:10.1146/annurev-food-030212-182623 · Cited by 788
Shiva, S., Huang, Z., Grubina, R., Sun, J., Ringwood, L. A., MacArthur, P. H., Xu, X., Murphy, E., Darley-Usmar, V. M., & Gladwin, M. T. (2007) · Circulation Research · doi:10.1161/01.res.0000260171.52224.6b · Cited by 599
Myoglobin: an essential hemoprotein in striated muscle
Ordway, G. A., & Garry, D. J. (2004) · Journal of Experimental Biology · doi:10.1242/jeb.01172 · Cited by 445
Nitrite as Regulator of Hypoxic Signaling in Mammalian Physiology
van Faassen, E. E., Bahrami, S., Feelisch, M., Hogg, N., Kelm, M., Kim‐Shapiro, D. B., Kozlov, A. V., Li, H., Lundberg, J. O., Mason, R., et al. (2009) · Medicinal Research Reviews · doi:10.1002/med.20151 · Cited by 435
Metadata
- Authors
- Wittenberg, J. B., & Wittenberg, B. A.
- Affiliations
- Albert Einstein College of Medicine (US)
- Corresponding author
- Wittenberg, Jonathan B.
- Venue
- Journal of Experimental Biology
- Publisher
- The Company of Biologists
- Published
- 2003-06-15
- Volume
- 206
- Issue
- 12
- Pages
- 2011-2020
- ISSN
- 0022-0949 (ISSN-L)
- 1477-9145
- OpenAlex
- W2123971049
- Cited by
- 550
- References
- 100
- Citations by year
- 2026: 17 · 2025: 19 · 2024: 22 · 2023: 13 · 2022: 18 · 2021: 22 · 2020: 20 · 2019: 39 · 2018: 9 · 2017: 18 · 2016: 24 · 2015: 23 · 2014: 23 · 2013: 35 · 2012: 21
- FWCI
- 1.59
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Experimental Biology (publishedVersion)
- PubMed (publishedVersion)
- HighWire Press Open Archive (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Health Sciences › Medicine › Physiology (medical) › Cardiovascular and exercise physiology
- Health Sciences › Medicine › Physiology (medical) › Biomedical and Chemical Research
- Keywords
- myoglobin, oxygen diffusion, cytochrome c oxidase, nitric oxide, oxymyoglobin, nitrate, oxygen consumption, myocardium, skeletal muscle
- MeSH terms
- Animals, Electron Transport Complex IV, Diffusion, Heart, Myoglobin, Oxygen, Sarcolemma, Muscle, Skeletal
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