Published May 31, 2006
| Version v1
Journal article
Strongly hydrogen-bonded water molecule is observed only in the alkaline form of proteorhodopsin
- 1. Department of Materials Science and Engineering, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555 (Japan)
Description
Proteorhodopsin (PR), an archaeal-type rhodopsin found in marine bacteria, functions as a light-driven proton pump. The proton-pumping activity of PR is highly pH-dependent, its exact mechanism being still controversial. The present FTIR spectra are very similar at pH 10 and 5 in the 1800-900 cm-1 region, but significantly different in the 2700-2000 cm-1 region. This implies that the structure and structural changes are almost identical between the alkaline and acid forms of PR except for water-containing hydrogen-bonding network. In addition, different hydrogen-bonding strength of internal water molecule may be correlated with the pH-dependent proton-pumping activity of PR
Additional details
Identifiers
- DOI
- 10.1016/j.chemphys.2005.12.013;
- PII
- S0301-0104(05)00659-2;
Publishing Information
- Journal Title
- Chemical Physics
- Journal Volume
- 324
- Journal Issue
- 2-3
- Journal Page Range
- p. 705-708
- ISSN
- 0301-0104
- CODEN
- CMPHC2
INIS
- Country of Publication
- Netherlands
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 39096629
- Subject category
- S74: ATOMIC AND MOLECULAR PHYSICS;
- Descriptors DEI
- BACTERIA; CHEMICAL BONDS; FOURIER TRANSFORMATION; HYDROGEN; INFRARED SPECTRA; ISOMERIZATION; PH VALUE; PROTONS; PUMPING; RHODOPSIN; VISIBLE RADIATION; WATER
- Descriptors DEC
- BARYONS; CHEMICAL REACTIONS; ELECTROMAGNETIC RADIATION; ELEMENTARY PARTICLES; ELEMENTS; FERMIONS; HADRONS; HYDROGEN COMPOUNDS; INTEGRAL TRANSFORMATIONS; MICROORGANISMS; NONMETALS; NUCLEONS; ORGANIC COMPOUNDS; OXYGEN COMPOUNDS; PIGMENTS; PROTEINS; RADIATIONS; SPECTRA; TRANSFORMATIONS
Optional Information
- Copyright
- Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.