Distinguishing Active Site Characteristics of Chlorite Dismutases with Their Cyanide Complexes.

ABSTRACT: O₂-evolving chlorite dismutases (Clds) efficiently convert chlorite (ClO₂^-) to O₂ and Cl^-. Dechloromonas aromatica Cld ( DaCld) is a highly active chlorite-decomposing homopentameric enzyme, typical of Clds found in perchlorate- and chlorate-respiring bacteria. The Gram-negative, human pathogen Klebsiella pneumoniae contains a homodimeric Cld ( KpCld) that also decomposes ClO₂^-, albeit with an activity 10-fold lower and a turnover number lower than those of DaCld. The interactions between the distal pocket and heme ligand of the DaCld and KpCld active sites have been probed via kinetic, thermodynamic, and spectroscopic behaviors of their cyanide complexes for insight into active site characteristics that are deter

SUBMITTER: Geeraerts Z 

PROVIDER: S-EPMC5849076 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature