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10.1007/s00775-014-1122-9 http://scihub22266oqcxt.onion/10.1007/s00775-014-1122-9 C4039383!4039383!24615282     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Inorg+Chem 2014 ; 19 (ä): 491-504 Nephropedia Template TP {{tp|p=24615282|t=2014. A two-electron shell game: Intermediates of the extradiol-cleaving catechol dioxygenases |pdf=|usr=}}{{24615282}} gab.com Text A two-electron shell game: Intermediates of the extradiol-cleaving catechol dioxygenases JO: J Biol Inorg Chem http://www.kidney.de/pget.php?&tw=1&pmid=24615282 #FOAvip Extradiol catechol ring-cleaving dioxygenases function by binding both the organic substrate and O2 at a divalent metal center in the active site. They have proven to be a particularly versatile group of enzymes with which to study the O2 activation process. Here, recent studies of homoprotocatechuate 2,3-dioxygenase (HPCD) are summarized with the objective of showing how Nature can utilize the enzyme structure and the properties of the metal and the substrate to select among many possible chemical paths to achieve both specificity and efficiency. Possible intermediates in the mechanism have been trapped by swapping active site metals, introducing active site amino acid substituted variants, and using substrates with different electron donating capacities. While each of these intermediates could form part of a viable reaction pathway, kinetic measurements significantly limit the likely candidates. Structural, kinetic, spectroscopic and computational analysis of the various intermediates shed light on how catalytic efficiency can be achieved. Twit Text FOAVip A two-electron shell game: Intermediates of the extradiol-cleaving catechol dioxygenases ????J Biol Inorg Chem http://www.kidney.de/pget.php?&tw=1&pmid=24615282 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24615282 #FOAvip English Wikipedia <ref>{{Cite pmid|24615282}}</ref> A two-electron shell game: Intermediates of the extradiol-cleaving catechol dioxygenases #MMPMID24615282 Fielding AJ; Lipscomb JD; Que L J Biol Inorg Chem 2014[Jun]; 19 (ä): 491-504 PMID24615282show ga Extradiol catechol ring-cleaving dioxygenases function by binding both the organic substrate and O2 at a divalent metal center in the active site. They have proven to be a particularly versatile group of enzymes with which to study the O2 activation process. Here, recent studies of homoprotocatechuate 2,3-dioxygenase (HPCD) are summarized with the objective of showing how Nature can utilize the enzyme structure and the properties of the metal and the substrate to select among many possible chemical paths to achieve both specificity and efficiency. Possible intermediates in the mechanism have been trapped by swapping active site metals, introducing active site amino acid substituted variants, and using substrates with different electron donating capacities. While each of these intermediates could form part of a viable reaction pathway, kinetic measurements significantly limit the likely candidates. Structural, kinetic, spectroscopic and computational analysis of the various intermediates shed light on how catalytic efficiency can be achieved. äA two-electron shell game: Intermediates of the extradiol-cleaving cat(epmc).pdf DeepDyve Pubget Overpricing