¹H NMR Spectroscopy of [FeFe] Hydrogenase: Insight into the Electronic Structure of the Active Site.

ABSTRACT: The [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii has been studied using ¹H NMR spectroscopy identifying the paramagnetically shifted ¹H resonances associated with both the [4Fe-4S]_H and the [2Fe]_H subclusters of the active site "H-cluster". The signal pattern of the unmaturated HydA1 containing only [4Fe-4S]_H is reminiscent of bacterial-type ferredoxins. The spectra of maturated HydA1, with a complete H-cluster in the active H_ox and the CO-inhibited H_ox-CO state, reveal additional upfield and downfield shifted ¹H resonances originating from the four methylene protons of the azadithiolate ligand in the [2Fe]_H subsite. The two axial protons are affected by positive spin density, whil

SUBMITTER: Rumpel S 

PROVIDER: S-EPMC5765528 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature