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Proton translocation in proteins

Copeland, Robert A. and Chan, Sunney I. (1989) Proton translocation in proteins. Annual Review of Physical Chemistry, 40 . pp. 671-698. ISSN 0066-426X. http://resolver.caltech.edu/CaltechAUTHORS:COParpc89

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Abstract

The active transport of protons across the low dielectric barrier imposed by biological membranes is accomplished by a plethora of proteins that span the ca. 40 Å of the phospholipid bilayer. The free energy derived from the proton electrochemical potential established by the translocation of these protons can subsequently be used to drive vital chemical reactions of the cell, such as ATP synthesis and cell locomotion. Membrane-bound proton translocating proteins have now been found for a variety of organisms and tissues (1). The driving force for proton pumping in these proteins is supplied by numerous mechanisms, including light absorption (e.g. bacteriorhodopsin) (2a,b), ligand binding (e.g. ATPase) (3), and electrochemistry (e.g. electron transfer through cytochrome c oxidase) (4). Thus nature has devised a variety of methods for supplying the energy required for proton pumping by these proteins. Such diversity notwithstanding, the proteins most likely share some common elements of structure and mechanism that allow them to function as proton pumps. A number of theoretical mechanisms have been put forth for both general proton translocation (5-7) and for energy coupling in specific proton pumps. However, despite almost three decades of intensive research, the details of the mechanism(s) and structural requirements for proton pumping remain largely unresolved. To some extent this is the result of the paucity of structural information available for integral membrane proteins. This situation may soon improve as a result of advances in protein methodologies that have allowed several integral membrane proteins to be successfully crystalized (8), and the increased use of genetic engineering to obtain recombinant proton translocating proteins that will offer an opportunity to assess the importance of specific amino acids for the proton translocation process (9).


Item Type:Article
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http://dx.doi.org/10.1146/annurev.pc.40.100189.003323DOIUNSPECIFIED
Additional Information:"Reprinted, with permission, from the Annual Review of Physical Chemistry, Volume 40 copyright 1989 by Annual Reviews, www.annualreviews.org" We wish to thank the many collaborators who have contributed to the work reported here. In particular we wish to thank P. M. Li, P. A. Smith, J. Gelles, D. F. Blair, S. N. Witt, J. Morgan, N. E. Gabriel, T. Nilsson, W. R. Ellis, Jr., H. B. Gray, H. Wang, M. Ma, R. Larsen, M. Ondrias, T. G. Spiro, and C. Martin. We also gratefully acknowledge helpful discussions with W. Woodruff, G. Babcock, B. Malmström, M. Wikström, M. Brunori, and P. Sarti. The work reported here from our laboratory was supported by grant GM22432 from the National Institute of General Medical Sciences, US Public Health Service to S.I.C. R.A.C. acknowledges support from a Chaim Weizmann Research Fellowship.
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Funding AgencyGrant Number
National Institute of General Medical SciencesGM22432
Public Health ServiceUNSPECIFIED
Chaim Weizmann Research FellowshipUNSPECIFIED
Record Number:CaltechAUTHORS:COParpc89
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:COParpc89
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ID Code:11624
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:17 Sep 2008 01:45
Last Modified:26 Dec 2012 10:17

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