2WPN

Structure of the oxidised, as-isolated NiFeSe hydrogenase from D. vulgaris Hildenborough

2WPN の概要

• エントリーDOI: 10.2210/pdb2wpn/pdb
• 分子名称: PERIPLASMIC [NIFESE] HYDROGENASE, SMALL SUBUNIT, PERIPLASMIC [NIFESE] HYDROGENASE, LARGE SUBUNIT, SELENOCYSTEINE-CONTAINING, IRON/SULFUR CLUSTER, ... (10 entities in total)
• 機能のキーワード: hydrogenase, metal-binding, oxidoreductase, oxygen tolerance
• 由来する生物種: DESULFOVIBRIO VULGARIS; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 91438.76

構造登録者

Marques, M.C.,Coelho, R.,De Lacey, A.L.,Pereira, I.A.C.,Matias, P.M. (登録日: 2009-08-07, 公開日: 2010-01-12, 最終更新日: 2025-10-01)

主引用文献

Marques, M.C.,Coelho, R.,De Lacey, A.L.,Pereira, I.A.,Matias, P.M.
The three-dimensional structure of [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough: a hydrogenase without a bridging ligand in the active site in its oxidised, "as-isolated" state.
J.Mol.Biol., 396:893-907, 2010

PubMed Abstract: Hydrogen is a good energy vector, and its production from renewable sources is a requirement for its widespread use. [NiFeSe] hydrogenases (Hases) are attractive candidates for the biological production of hydrogen because they are capable of high production rates even in the presence of moderate amounts of O(2), lessening the requirements for anaerobic conditions. The three-dimensional structure of the [NiFeSe] Hase from Desulfovibrio vulgaris Hildenborough has been determined in its oxidised "as-isolated" form at 2.04-A resolution. Remarkably, this is the first structure of an oxidised Hase of the [NiFe] family that does not contain an oxide bridging ligand at the active site. Instead, an extra sulfur atom is observed binding Ni and Se, leading to a SeCys conformation that shields the NiFe site from contact with oxygen. This structure provides several insights that may explain the fast activation and O(2) tolerance of these enzymes.

PubMed: 20026074
DOI: 10.1016/j.jmb.2009.12.013

実験手法

X-RAY DIFFRACTION (2.04 Å)