6QII

Xenon derivatization of the F420-reducing [NiFe] hydrogenase complex from Methanosarcina barkeri

Summary for 6QII

• Entry DOI: 10.2210/pdb6qii/pdb
• Descriptor: Coenzyme F420 hydrogenase subunit gamma, FE (III) ION, MAGNESIUM ION, ... (13 entities in total)
• Functional Keywords: [nife] containing hydrogenase, reversible oxidation of dihydrogen, oxygen sensitive, methanogenic acetoclastic archaea, oxidoreductase
• Biological source: Methanosarcina barkeri MS; More
• Total number of polymer chains: 3
• Total formula weight: 115288.35

Authors

Ilina, Y.,Lorent, C.,Katz, S.,Jeoung, J.H.,Shima, S.,Horch, M.,Zebger, I.,Dobbek, H. (deposition date: 2019-01-19, release date: 2019-10-23, Last modification date: 2024-01-24)

Primary citation

Ilina, Y.,Lorent, C.,Katz, S.,Jeoung, J.H.,Shima, S.,Horch, M.,Zebger, I.,Dobbek, H.
X-ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases.
Angew.Chem.Int.Ed.Engl., 58:18710-18714, 2019

PubMed Abstract: [NiFe] hydrogenases are complex model enzymes for the reversible cleavage of dihydrogen (H ). However, structural determinants of efficient H binding to their [NiFe] active site are not properly understood. Here, we present crystallographic and vibrational-spectroscopic insights into the unexplored structure of the H -binding [NiFe] intermediate. Using an F -reducing [NiFe]-hydrogenase from Methanosarcina barkeri as a model enzyme, we show that the protein backbone provides a strained chelating scaffold that tunes the [NiFe] active site for efficient H binding and conversion. The protein matrix also directs H diffusion to the [NiFe] site via two gas channels and allows the distribution of electrons between functional protomers through a subunit-bridging FeS cluster. Our findings emphasize the relevance of an atypical Ni coordination, thereby providing a blueprint for the design of bio-inspired H -conversion catalysts.

PubMed: 31591784
DOI: 10.1002/anie.201908258

Experimental method

X-RAY DIFFRACTION (2.28 Å)