The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Voltage-Gated Proton Channels and Other Proton Transfer Pathways
Abstract
Proton channels exist in a wide variety of membrane proteins where they transport protons rapidly and efficiently. Usually the proton pathway is formed mainly by water molecules present in the protein, but its function is regulated by titratable groups on critical amino acid residues in the pathway. All proton channels conduct protons by a hydrogen-bonded chain mechanism in which the proton hops from one water or titratable group to the next. Voltage-gated proton channels represent a specific subset of proton channels that have voltage- and time-dependent gating like other ion channels. However, they differ from most ion channels in their extraordinarily high selectivity, tiny conductance, strong temperature and deuterium isotope effects on conductance and gating kinetics, and insensitivity to block by steric occlusion. Gating of H+channels is regulated tightly by pH and voltage, ensuring that they open only when the electrochemical gradient is outward. Thus they function to extrude acid from cells. H+channels are expressed in many cells. During the respiratory burst in phagocytes, H+current compensates for electron extrusion by NADPH oxidase. Most evidence indicates that the H+channel is not part of the NADPH oxidase complex, but rather is a distinct and as yet unidentified molecule.
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Citations
Cites
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Cited by
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989
“Thus there is no doubt that there is a close relationship between NOX enzymes and proton channels; however, there are two different molecular interpretations: 1) NOX enzymes possess a proton channel domain, suggested to reside within the histidine-rich third transmembrane domain (55, 57, 365, 368, 592, 639), and 2) NO…”
BackgroundMyeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282
Proton-coupled electron transfer
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Proton Transfer 200 Years after von Grotthuss: Insights from Ab Initio Simulations
Marx, D. (2006) · ChemPhysChem · doi:10.1002/cphc.200600128 · Cited by 920
Anomalously Immobilized Water: A New Water Phase Induced by Confinement in Nanotubes
Mashl, R. J., Joseph, S., Aluru, N. R., & Jakobsson, E. (2003) · Nano Letters · doi:10.1021/nl0340226 · Cited by 447
Metadata
- Authors
- Decoursey, T. E.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2003-04-01
- Volume
- 83
- Issue
- 2
- Pages
- 475-579
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2103566186
- Cited by
- 737
- References
- 17
- FWCI
- 2.24
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
