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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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“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]
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“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]
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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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