6QGR

The F420-reducing [NiFe] hydrogenase complex from Methanosarcina barkeri at the Nia-S state

6QGR の概要

• エントリーDOI: 10.2210/pdb6qgr/pdb
• 分子名称: Coenzyme F420 hydrogenase subunit gamma, FE (III) ION, MAGNESIUM ION, ... (13 entities in total)
• 機能のキーワード: [nife] containing hydrogenase, reversible oxidation of dihydrogen, oxygen sensitive, methanogenic acetoclastic archaea, metal binding protein, oxidoreductase
• 由来する生物種: Methanosarcina barkeri MS; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 112717.69

構造登録者

Ilina, Y.,Lorent, C.,Katz, S.,Jeoung, J.H.,Shima, S.,Horch, M.,Zebger, I.,Dobbek, H. (登録日: 2019-01-12, 公開日: 2019-10-23, 最終更新日: 2024-01-24)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.839 Å)