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

Kinetic pathways and barriers for ligand binding to myoglobin

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

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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Registry

Crossref · 10.1074/jbc.271.30.17593

Cites

38 of 38 references verified0 citation errors · 0 not checkable

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  • The k0 for Ngb is 500 fold faster than for Hb and approaching a rate constant characteristic of that which is rate-limited by how fast nitrite can get to the heme pocket.

    “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]

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Authors
Olson, J. S., & Phillips, G. N.
Affiliations
Rice University (US)
Corresponding author
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
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 › Cell Biology › 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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