The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
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.
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“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]
Citations
Cites
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Crystal Structures of Myoglobin-Ligand Complexes at Near-Atomic Resolution
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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
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
Maia, L. B., & Moura, J. J. G. (2014) · Chemical Reviews · doi:10.1021/cr400518y · Cited by 401
Metadata
- 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 › Biochemistry › 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
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