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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

10.1002/bbpc.19100160715

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1432-1327

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Protein stability and mutations in the axial methi

Authors: Ilaria Bartalesi Ivano Bertini Giulia Di Rocco Antonio Ranieri Antonio Rosato Murugendra Vanarotti Paul R Vasos Maria Silvia Viezzoli
Publish Date: 2004/06/03
Volume: 9, Issue: 5, Pages: 600-608
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Abstract

The minimal monoheme ferricytochrome c from Bacillus pasteurii containing 71 amino acids has been further investigated through mutagenesis of different positions in the loop containing the iron ligand Met71 These mutations have been designed to sample different aspects of the loop structure in order to obtain insights into the determinants of the stability of the ironIII environment In particular positions 68 72 and 75 have been essayed Gln68 has been mutated to Lys to provide a suitable alternate ligand that can displace Met71 under denaturing conditions Pro72 has been mutated to Gly and Ala to modify the range of allowed backbone conformations Ile75 which is in van der Waals contact with Met71 and partly shields a longlived water molecule in a protein cavity has been substituted by Val and Ala to affect the network of interresidue interactions around the metal site The different contributions of the above amino acids to protein parameters such as structure redox potential and the overall stability against unfolding with guanidinium hydrochloride are analyzed While the structure remains essentially the same the stability decreases with mutations The comparison with mitochondrial ctype cytochromes is instructive

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