ATP-Triggered Fe(CN)₂CO Synthon Transfer from the Maturase HypCD to the Active Site of Apo-[NiFe]-Hydrogenase.

ABSTRACT: [NiFe]-hydrogenases catalyze the reversible activation of H₂ using a unique NiFe(CN)₂CO metal site, which is assembled by a sophisticated multiprotein machinery. The [4Fe-4S] cluster-containing HypCD complex, which possesses an ATPase activity with a hitherto unknown function, serves as the hub for the assembly of the Fe(CN)₂CO subfragment. HypCD is also thought to be responsible for the subsequent transfer of the iron fragment to the apo-form of the catalytic hydrogenase subunit, but the underlying mechanism has remained unexplored. Here, we performed a thorough spectroscopic characterization of different HypCD preparations using infrared, Mössbauer, and NRVS spectroscopy, revealing molecular details of the coordination of the Fe(CN)₂CO fragment

SUBMITTER: Kwiatkowski A 

PROVIDER: S-EPMC11565642 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature