ArticlePhysical chemistry chemical physics : PCCP2010
Kinetic spectroscopy of heme hydration and ligand binding in myoglobin and isolated hemoglobin chains: an optical window into heme pocket water dynamics.
Article in Physical chemistry chemical physics : PCCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Changes in Water Dynamics by Osmolytes Regulate Enzyme Activity.The journal of physical chemistry. B · 2026Article
- Kinetic mechanisms for OMolecular aspects of medicine · 2022Review
- X-ray snapshots reveal conformational influence on active site ligation during metalloprotein folding.Chemical science · 2019Article
- Do Osmolytes Impact the Structure and Dynamics of Myoglobin?Molecules (Basel, Switzerland) · 2018Article
- Role of Heme Pocket Water in Allosteric Regulation of Ligand Reactivity in Human Hemoglobin.Biochemistry · 2016Article
- Internal water and microsecond dynamics in myoglobin.The journal of physical chemistry. B · 2013Article
- Development of recombinant hemoglobin-based oxygen carriers.Antioxidants & redox signaling · 2013Review
- Modulating distal cavities in the α and β subunits of human HbA reveals the primary ligand migration pathway.Biochemistry · 2011Article
- Blocking the gate to ligand entry in human hemoglobin.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The entry of a water molecule into the distal heme pocket of pentacoordinate heme proteins such as myoglobin and the alpha,beta chains of hemoglobin can be detected by time-resolved spectroscopy in the heme visible bands after photolysis of the CO complex. Reviewing the evidence from spectrokinetic studies of Mb variants, we find that this optical method measures the occupancy of non(heme)coordinated water in the distal pocket, n(w), with high fidelity. This evidence further suggests that perturbation of the kinetic barrier presented by distal pocket water is often the dominant mechanism by which active site mutations affect the bimolecular rate constant for CO binding. Water entry into the heme pockets of isolated hemoglobin subunits was detected by optical methods. Internal hydration is higher in the native alpha chains than in the beta chains, in agreement with previous crystallographic results for the subunits within Hb tetramers. The kinetic parameters obtained from modeling of the water entry and ligand rebinding in Mb mutants and native Hb chains are consistent with an inverse dependence of the bimolecular association rate constant on the water occupancy factor. This correlation suggests that water and ligand mutually exclude one another from the distal pockets of both types of hemoglobin chains and myoglobin.
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Registered trials
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