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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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
Conformational Substates in Proteins
Frauenfelder, H., Parak, F., & Young, R. D. (1988) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.17.060188.002315 · Cited by 995
Mechanisms of Ligand Recognition in Myoglobin
Springer, B. A., Sligar, S. G., Olson, J. S., & Phillips, G. N. J. (1994) · Chemical Reviews · doi:10.1021/cr00027a007 · Cited by 755
Mechanism of NO-induced oxidation of myoglobin and hemoglobin
Eich, R. F., Li, T., Lemon, D. D., Doherty, D. H., Curry, S. R., Aitken, J. F., Mathews, A. J., Johnson, K. A., Smith, R. D., Phillips, et al. (1996) · Biochemistry · doi:10.1021/bi960442g · Cited by 613
Self-citationElber, R., & Karplus, M. (1990) · Journal of the American Chemical Society · doi:10.1021/ja00181a020 · Cited by 506
Cavities in proteins: structure of a metmyoglobin xenon complex solved to 1.9 .ANG.
Tilton, R. F., Kuntz, I. D., & Petsko, G. A. (1984) · Biochemistry · doi:10.1021/bi00308a002 · Cited by 476
High-Resolution Crystal Structures of Distal Histidine Mutants of Sperm Whale Myoglobin
Quillin, M. L., Arduini, R. M., Olson, J. S., & Phillips, G. N. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1569 · Cited by 385
Petrich, J. W., Poyart, C., & Martin, J. L. (1988) · Biochemistry · doi:10.1021/bi00411a022 · Cited by 364
Crystal Structures of CO−, Deoxy- and Met-myoglobins at Various pH Values
Yang, F., & Phillips, G. N., Jr. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0123 · Cited by 340
Crystal structure of photolysed carbonmonoxy-myoglobin
Schlichting, I., Berendzen, J., Phillips, G. N., Jr., & Sweet, R. M. (1994) · Nature · doi:10.1038/371808a0 · Cited by 329
Binding of CO to Myoglobin from a Heme Pocket Docking Site to Form Nearly Linear Fe-C-O
Lim, M., Jackson, T. A., & Anfinrud, P. (1995) · Science · doi:10.1126/science.7638619 · Cited by 280
Flagged first, then by citations
Cited by
Sorted by citations
Riess, J. G. (2001) · Chemical Reviews · doi:10.1021/cr970143c · Cited by 787
Crystal Structures of Myoglobin-Ligand Complexes at Near-Atomic Resolution
Vojtechovsky, J., Chu, K., Berendzen, J., Sweet, R. M., & Schlichting, I. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77056-6 · Cited by 562
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
