Structure and reactivity of chlorite dismutase nitrosyls.

ABSTRACT: Ferric nitrosyl ({FeNO}⁶) and ferrous nitrosyl ({FeNO}⁷) complexes of the chlorite dismutases (Cld) from Klebsiella pneumoniae and Dechloromonas aromatica have been characterized using UV-visible absorbance and Soret-excited resonance Raman spectroscopy. Both of these Clds form kinetically stable {FeNO}⁶ complexes and they occupy a unique region of ν(Fe-NO)/ν(N-O) correlation space for proximal histidine liganded heme proteins, characteristic of weak Fe-NO and N-O bonds. This location is attributed to admixed Fe^III-NO character of the {FeNO}⁶ ground state. Cld {FeNO}⁶ complexes undergo slow reductive nitrosylation to yield {FeNO}⁷ complexes. The effects of proximal and distal environment on reductive nitroylsation

SUBMITTER: Geeraerts Z 

PROVIDER: S-EPMC7749827 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature