Conformation, co-operativity and ligand binding in human hemoglobin
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Both ferrous deoxy and oxyheme react relatively rapidly with NO to produce nitrosyl heme or nitrate respectively.
“both ferrous deoxy and oxyheme react relatively rapidly (rate constants ~107 M-1s-1) with NO to produce nitrosyl heme (Scheme 1) or nitrate respectively [29, 30].”
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 [29]
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- Authors
- Cassoly, R., & Gibson, Q. H.
- Affiliations
- Institut de Biologie Physico-Chimique (FR)
- Cornell University (US)
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1975-01
- Volume
- 91
- Issue
- 3
- Pages
- 301-313
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2007942188
- Cited by
- 259
- References
- 18
- Citations by year
- 2024: 2 · 2023: 1 · 2022: 3 · 2021: 4 · 2019: 3 · 2018: 3 · 2017: 5 · 2016: 5 · 2015: 5 · 2014: 10 · 2013: 8 · 2012: 8
- FWCI
- 2.50
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Health Sciences › Medicine › Genetics › Hemoglobinopathies and Related Disorders
- Keywords
- human hemoglobin, nitric oxide binding, carbon monoxide binding, ligand binding kinetics, ligand competition, conformational change
- MeSH terms
- Arylsulfonates, Carbon Monoxide, Chemistry, Hemoglobins, Humans, Kinetics, Ligands, Nitric Oxide, Protein Binding, Protein Conformation, Pyrenes, Chemical Phenomena
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