Work

Synthesis and vibrational spectroscopy of 57 Fe-labeled models of [NiFe] hydrogenase: first direct observation of a nickel–iron interaction

Year: 2014

Type: article

Abstract: A new route to iron carbonyls has enabled synthesis of (57)Fe-labeled [NiFe] hydrogenase mimic (OC)3(57)Fe(pdt)Ni(dppe). Its study by nuclear resonance vibrational spectroscopy revealed Ni-(57)Fe vibrations, as confirmed by calculations. The modes are absent for [(OC)3(57)Fe(pdt)Ni(dppe)](+), which lacks Ni-(57)Fe bonding, underscoring the utility of the analyses in identifying metal-metal interactions.

Source: Chemical Communications

DOI: 10.1039/c4cc04572f

Authors: David Schilter, Vladimir Pelmenschikov, Hongxin Wang, Florian Meier, Leland B. Gee, Yoshitaka Yoda, Martin Kaupp, Thomas B. Rauchfuss, Stephen P. Cramer

Institutions: University of Illinois Urbana-Champaign, Technische Universität Berlin, Lawrence Berkeley National Laboratory, University of California System, University of California, Davis, SPring-8, Japan Synchrotron Radiation Research Institute, Spring-8 (Japan)

Language: English

Topic: Metalloenzymes and iron-sulfur proteins

Subfield: Renewable Energy, Sustainability and the Environment

Field: Energy

Domain: Physical Sciences

Open Access status: hybrid

Funders: U.S. Department of Energy, National Institutes of Health, National Institute of General Medical Sciences

Awards: G143921860, G2386843879, Biosynthesis and Reactivity of the Active Site of the FeFe Hydrogenases, Spectroscopy of Fe-S Cluster Proteins -- Information for Structure and Function

OpenAlex ID: W1990557410

FWCI: 0.659

Cites: 35

Cited by: 12

Related to: 10