5 years ago

Structural and functional synthetic model of mono-iron hydrogenase featuring an anthracene scaffold

Structural and functional synthetic model of mono-iron hydrogenase featuring an anthracene scaffold
Junhyeok Seo, Michael J. Rose, Taylor A. Manes
Mono-iron hydrogenase was the third type of hydrogenase discovered. Its Lewis acidic iron(II) centre promotes the heterolytic cleavage of the H–H bond and this non-redox H2 activation distinguishes it from the well-studied dinuclear [FeFe] and [NiFe] hydrogenases. Cleavage of the H–H bond is followed by hydride transfer to the enzyme's organic substrate, H4MPT+, which serves as a CO2 ‘carrier’ in methanogenic pathways. Here we report a scaffold-based synthetic approach by which to model mono-iron hydrogenase using an anthracene framework, which supports a biomimetic fac-C,N,S coordination motif to an iron(II) centre. This arrangement includes the biomimetic and organometallic Fe–C σ bond, which enables bidirectional activity reminiscent of the native enzyme: the complex activates H2 under mild conditions, and catalyses C–H hydride abstraction plus H2 generation from a model substrate. Notably, neither H2 activation nor C–H hydride abstraction was observed in the analogous complex with a pincer-type mer-C,N,S ligation, emphasizing the importance of the fac-C,N,S-iron(II) motif in promoting enzyme-like reactivity.

Publisher URL: http://dx.doi.org/10.1038/nchem.2707

DOI: 10.1038/nchem.2707

You might also like
Discover & Discuss Important Research

Keeping up-to-date with research can feel impossible, with papers being published faster than you'll ever be able to read them. That's where Researcher comes in: we're simplifying discovery and making important discussions happen. With over 19,000 sources, including peer-reviewed journals, preprints, blogs, universities, podcasts and Live events across 10 research areas, you'll never miss what's important to you. It's like social media, but better. Oh, and we should mention - it's free.

  • Download from Google Play
  • Download from App Store
  • Download from AppInChina

Researcher displays publicly available abstracts and doesn’t host any full article content. If the content is open access, we will direct clicks from the abstracts to the publisher website and display the PDF copy on our platform. Clicks to view the full text will be directed to the publisher website, where only users with subscriptions or access through their institution are able to view the full article.