Spectroscopic Investigations of [FeFe] Hydrogenase Maturated with [57Fe2(adt)(CN)2(CO)4]2-

Ryan Gilbert-Wilson, Judith F. Siebel, Agnieszka Adamska-Venkatesh, Cindy C. Pham, Edward Reijerse, Hongxin Wang, Stephen P. Cramer, Wolfgang Lubitz, Thomas B. Rauchfuss

Research output: Contribution to journalArticlepeer-review

Abstract

The preparation and spectroscopic characterization of a CO-inhibited [FeFe] hydrogenase with a selectively 57Fe-labeled binuclear subsite is described. The precursor [57Fe2(adt)(CN)2(CO)4]2- was synthesized from the 57Fe metal, S8, CO, (NEt4)CN, NH4Cl, and CH2O. (Et4N)2[57Fe2(adt)(CN)2(CO)4] was then used for the maturation of the [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii, to yield the enzyme selectively labeled at the [2Fe]H subcluster. Complementary 57Fe enrichment of the [4Fe-4S]H cluster was realized by reconstitution with 57FeCl3 and Na2S. The Hox-CO state of [257Fe]H and [457Fe-4S]H HydA1 was characterized by Mössbauer, HYSCORE, ENDOR, and nuclear resonance vibrational spectroscopy. (Chemical Equation Presented).

Original languageEnglish (US)
Pages (from-to)8998-9005
Number of pages8
JournalJournal of the American Chemical Society
Volume137
Issue number28
DOIs
StatePublished - Jul 22 2015

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Fingerprint

Dive into the research topics of 'Spectroscopic Investigations of [FeFe] Hydrogenase Maturated with [<sup>57</sup>Fe<sub>2</sub>(adt)(CN)<sub>2</sub>(CO)<sub>4</sub>]<sup>2-</sup>'. Together they form a unique fingerprint.

Cite this