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10.1126/science.1259802 http://scihub22266oqcxt.onion/10.1126/science.1259802 C4668018!4668018!25525245     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2014 ; 346 (6216): 1510-4 Nephropedia Template TP {{tp|p=25525245|t=2014. Extreme electric fields power catalysis in the active site of ketosteroid isomerase |pdf=|usr=}}{{25525245}} gab.com Text Extreme electric fields power catalysis in the active site of ketosteroid isomerase JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=25525245 #FOAvip Enzymes use protein architecture to impose specific electrostatic fields onto their bound substrates, but the magnitude and catalytic effect of these electric fields have proven difficult to quantify with standard experimental approaches. Using vibrational Stark effect spectroscopy, we found that the active site of the enzyme ketosteroid isomerase (KSI) exerts an extremely large electric field onto the C=O chemical bond that undergoes a charge rearrangement in KSI?s rate-determining step. Moreover, we found that the magnitude of the electric field exerted by the active site strongly correlates with the enzyme?s catalytic rate enhancement, enabling us to quantify the fraction of the catalytic effect that is electrostatic in origin. The measurements described here may help explain the role of electrostatics in many other enzymes and biomolecular systems. Twit Text FOAVip Extreme electric fields power catalysis in the active site of ketosteroid isomerase ????Science http://www.kidney.de/pget.php?&tw=1&pmid=25525245 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25525245 #FOAvip English Wikipedia <ref>{{Cite pmid|25525245}}</ref> Extreme electric fields power catalysis in the active site of ketosteroid isomerase #MMPMID25525245 Fried SD; Bagchi S; Boxer SG Science 2014[Dec]; 346 (6216): 1510-4 PMID25525245show ga Enzymes use protein architecture to impose specific electrostatic fields onto their bound substrates, but the magnitude and catalytic effect of these electric fields have proven difficult to quantify with standard experimental approaches. Using vibrational Stark effect spectroscopy, we found that the active site of the enzyme ketosteroid isomerase (KSI) exerts an extremely large electric field onto the C=O chemical bond that undergoes a charge rearrangement in KSI?s rate-determining step. Moreover, we found that the magnitude of the electric field exerted by the active site strongly correlates with the enzyme?s catalytic rate enhancement, enabling us to quantify the fraction of the catalytic effect that is electrostatic in origin. The measurements described here may help explain the role of electrostatics in many other enzymes and biomolecular systems. äExtreme electric fields power catalysis in the active site of ketoster(epmc).pdf DeepDyve Pubget Overpricing