A designed heme-[4Fe-4S] metalloenzyme catalyzes sulfite reduction like the native enzyme

Evan N. Mirts, Igor D. Petrik, Parisa Hosseinzadeh, Mark J. Nilges, Yi Lu

Research output: Contribution to journalArticle

Abstract

Multielectron redox reactions often require multicofactor metalloenzymes to facilitate coupled electron and proton movement,but it is challenging to design artificial enzymes to catalyze these important reactions,owing to their structural and functional complexity.We report a designed heteronuclear heme-[4Fe-4S] cofactor in cytochrome c peroxidase as a structural and functional model of the enzyme sulfite reductase. The initial model exhibits spectroscopic and ligand-binding properties of the native enzyme, and sulfite reduction activity was improved-through rational tuning of the secondary sphere interactions around the [4Fe-4S] and the substrate-binding sites-to be close to that of the native enzyme. By offering insight into the requirements for a demanding six-electron, seven-proton reaction that has so far eluded synthetic catalysts,this study provides strategies for designing highly functional multicofactor artificial enzymes.

Original languageEnglish (US)
Pages (from-to)1098-1101
Number of pages4
JournalScience
Volume361
Issue number6407
DOIs
StatePublished - Sep 14 2018

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'A designed heme-[4Fe-4S] metalloenzyme catalyzes sulfite reduction like the native enzyme'. Together they form a unique fingerprint.

  • Cite this