Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1990-3-14
pubmed:abstractText
The photochemical and the subsequent thermal behaviors of iodopsin (Cl(-)-bound form) and N-iodopsin (iodopsin whose Cl- was replaced by NO3-) in CHAPS-phosphatidylcholine (PC) were studied by low-temperature spectrophotometry. Irradiation of the iodopsin preparation at -185 degrees C produced a photo-steady-state mixture composed of iodopsin, bathoiodopsin, and isoiodopsin. Bathoiodopsin was thermally reverted to the original iodopsin. These results were almost the same as those reported previously [Yoshizawa, T., & Wald, G. (1967) Nature 214, 566-571] in which iodopsin was extracted with 2% digitonin. Therefore, photochemical and subsequent thermal behaviors of iodopsin were independent of the detergent to solubilize iodopsin. Irradiation of N-iodopsin at -185 degrees C produced the similar photo-steady-state mixture. However, N-bathoiodopsin was thermally converted to the next intermediate, presumably N-lumiiodopsin. These results suggest that the batho-lumi transition of iodopsin at low temperature is likely to be inhibited by the Cl- bound to the protein moiety of iodopsin, while at room temperature the Cl- bound to iodopsin could be released on the conversion process of batho- to lumiiodopsin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9412-6
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Effect of chloride ion on the thermal decay process of the batho intermediate of iodopsin at low temperature.
pubmed:affiliation
Department of Biophysics, Faculty of Science, Kyoto University, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't