Severity: Warning
Message: file_get_contents(https://...@gmail.com&api_key=61f08fa0b96a73de8c900d749fcb997acc09&a=1): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
Filename: helpers/my_audit_helper.php
Line Number: 176
Backtrace:
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 176
Function: file_get_contents
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 250
Function: simplexml_load_file_from_url
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3122
Function: getPubMedXML
File: /var/www/html/application/controllers/Detail.php
Line: 575
Function: pubMedSearch_Global
File: /var/www/html/application/controllers/Detail.php
Line: 489
Function: pubMedGetRelatedKeyword
File: /var/www/html/index.php
Line: 316
Function: require_once
Gel-electrophoretic assay revealed that the photosynthetic reaction center (RC) of Chromatium minutissimum, in contrast to the well-known RC Rhodopseudomonas viridis, consists of five rather than four subunits with molecular masses of 37, 34, 25, 19, and 17 kDa. The 37- and 19-kDa subunits are stained with tetramethylbenzidine for the cytochrome c hemes. Absorption spectra show that the concentration of reduced cytochromes in the C. minutissimum RC poised at redox potential of -150 mV (fully reduced pool of hemes) is about three times more than in the C. minutissimum RC poised at redox potential of +260 mV (only high-potential hemes are reduced). The results of redox titration of absorption changes at the cytochrome c alpha-band are most appropriately approximated by a six-component theoretical curve with the midpoint potentials of Em1 = 390 mV, Em2 = 320 mV, Em3 = 210 mV, Em4 = 100 mV, Em5 = 20 mV, and Em6 = -50 mV. Possible functions of the cytochromes with the midpoint potentials 210 and 100 mV, which have not been found in purple bacteria before, are discussed.
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Source |
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http://dx.doi.org/10.1016/s0014-5793(98)00013-1 | DOI Listing |
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