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Title of Journal: J Biol Inorg Chem

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Abbravation: JBIC Journal of Biological Inorganic Chemistry

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Springer-Verlag

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DOI

10.1007/bf00925220

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1432-1327

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Kinetic and structural studies on roles of the ser

Authors: Yasuaki Yamanaka Koichi Hashimoto Akashi Ohtaki Keiichi Noguchi Masafumi Yohda Masafumi Odaka
Publish Date: 2010/03/10
Volume: 15, Issue: 5, Pages: 655-665
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Abstract

Nitrile hydratases NHase which catalyze the hydration of nitriles to amides have an unusual Fe3+ or Co3+ center with two modified Cys ligands cysteine sulfininate CysSO2 − and either cysteine sulfenic acid or cysteine sulfenate CysSOH Two catalytic mechanisms have been proposed One is that the sulfenyl oxygen activates a water molecule enabling nucleophilic attack on the nitrile carbon The other is that the Ser ligand ionizes the strictly conserved Tyr activating a water molecule Here we characterized mutants of Fetype NHase from Rhodococcus erythropolis N771 replacing the Ser and Tyr residues αS113A and βY72F The αS113A mutation partially affected catalytic activity and did not change the pH profiles of the kinetic parameters UV–vis absorption spectra indicated that the electronic state of the Fe center was altered by the αS113A mutation but the changes could be prevented by a competitive inhibitor nbutyric acid The overall structure of the αS113A mutant was similar to that of the wild type but significant changes were observed around the catalytic cavity Like the UV–vis spectra the changes were compensated by the substrate or product The Ser ligand is important for the structure around the catalytic cavity but is not essential for catalysis The βY72F mutant exhibited no activity The structure of the βY72F mutant was highly conserved but was found to be the inactivated state with αCys114SOH oxidized to CysSO2 − suggesting that βTyr72 affected the electronic state of the Fe center The catalytic mechanism is discussed on the basis of the results obtained

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