1OGY

Crystal structure of the heterodimeric nitrate reductase from Rhodobacter sphaeroides

1OGY の概要

• エントリーDOI: 10.2210/pdb1ogy/pdb
• 分子名称: PERIPLASMIC NITRATE REDUCTASE, DIHEME CYTOCHROME C NAPB MOLECULE: NITRATE REDUCTASE, IRON/SULFUR CLUSTER, ... (6 entities in total)
• 機能のキーワード: nitrate reductase, oxidoreductase
• 由来する生物種: RHODOBACTER SPHAEROIDES; 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 862965.86

構造登録者

Arnoux, P.,Sabaty, M.,Alric, J.,Frangioni, B.,Guigliarelli, B.,Adriano, J.-M.,Pignol, D. (登録日: 2003-05-19, 公開日: 2003-10-09, 最終更新日: 2024-10-23)

主引用文献

Arnoux, P.,Sabaty, M.,Alric, J.,Frangioni, B.,Guigliarelli, B.,Adriano, J.-M.,Pignol, D.
Structural and Redox Plasticity in the Heterodimeric Periplasmic Nitrate Reductase
Nat.Struct.Biol., 10:928-, 2003

PubMed Abstract: The structure of the respiratory nitrate reductase (NapAB) from Rhodobacter sphaeroides, the periplasmic heterodimeric enzyme responsible for the first step in the denitrification process, has been determined at a resolution of 3.2 A. The di-heme electron transfer small subunit NapB binds to the large subunit with heme II in close proximity to the [4Fe-4S] cluster of NapA. A total of 57 residues at the N- and C-terminal extremities of NapB adopt an extended conformation, embracing the NapA subunit and largely contributing to the total area of 5,900 A(2) buried in the complex. Complex formation was studied further by measuring the variation of the redox potentials of all the cofactors upon binding. The marked effects observed are interpreted in light of the three-dimensional structure and depict a plasticity that contributes to an efficient electron transfer in the complex from the heme I of NapB to the molybdenum catalytic site of NapA.

PubMed: 14528294
DOI: 10.1038/NSB994

実験手法

X-RAY DIFFRACTION (3.2 Å)