Severity: Warning
Message: file_get_contents(https://...@pubfacts.com&api_key=b8daa3ad693db53b1410957c26c9a51b4908&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: 1034
Function: getPubMedXML
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3152
Function: GetPubMedArticleOutput_2016
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
The absorption spectrum and fluorescence emission spectrum of RS601 were found to keep the typical characteristics of those of the purple nonsulfide bacteria Rb. sphaeroides. Under illumination, methyl viologen was reduced by RS601 chromatophores in the presence of DCPIPH(2) as the electron donor, setting up a standard noncyclic electron transport. o-phenanthroline with I(50) of 1.0 mM inhibited the DCPIPH(2) right curved arrow MV electron transport. Antimycin A did not inhibit the DCPIPH(2) right curved arrow MV electron transport and had no I(50). The results suggested that the exact site where methyl viologen accepted electron should locate between the secondary electron acceptor, Q(B), and cyt b, but not at the Q(A) binding site as indicated before. The difference of electron transport between reduced sides of reaction centers of Rb. sphaeroides and Rs. rubrum was discussed.
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