Severity: Warning
Message: file_get_contents(https://...@gmail.com&api_key=61f08fa0b96a73de8c900d749fcb997acc09): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
Filename: helpers/my_audit_helper.php
Line Number: 143
Backtrace:
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 143
Function: file_get_contents
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 209
Function: simplexml_load_file_from_url
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 994
Function: getPubMedXML
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3134
Function: GetPubMedArticleOutput_2016
File: /var/www/html/application/controllers/Detail.php
Line: 574
Function: pubMedSearch_Global
File: /var/www/html/application/controllers/Detail.php
Line: 488
Function: pubMedGetRelatedKeyword
File: /var/www/html/index.php
Line: 316
Function: require_once
Hydrogenases, ferredoxins, and ferredoxin-NADP reductases (FNR) are redox proteins that mediate electron metabolism in vivo, and are also potential components for biological H production technologies. A high-throughput H production assay device (H PAD) is presented that enables simultaneous evaluation of 96 individual H production reactions to identify components that improve performance. Using a CCD camera and image analysis software, H PAD senses the chemo-optical response of Pd/WO thin films to the H produced. H PAD-enabled discovery of hydrogenase and FNR mutants that enhance biological H production is reported. From a library of 10 080 randomly mutated Clostridium pasteurianum [FeFe] hydrogenases, we found a mutant with nearly 3-fold higher H production specific activity. From a library of 400 semi-randomly mutated Oryza sativa FNR, the top hit enabled a 60 % increase in NADPH-driven H production rates. H PAD can also facilitate elucidation of fundamental biochemical mechanisms within these systems.
Download full-text PDF |
Source |
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http://dx.doi.org/10.1002/anie.201610260 | DOI Listing |
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