Cited by 259Hemoglobin structure and functionProtein Structure and DynamicsMetal-Catalyzed Oxygenation Mechanisms

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Kinetic Pathways and Barriers for Ligand Binding to Myoglobin

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Olson, John S., Phillips, George N.·1996·Journal of Biological Chemistry

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Abstract

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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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)
DOI: 10.1074/jbc.271.30.17593
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 8871 d)
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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Kinetic Pathways and Barriers for Ligand Binding to Myoglobin

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