1DE0

MODULATING THE MIDPOINT POTENTIAL OF THE [4FE-4S] CLUSTER OF THE NITROGENASE FE PROTEIN

1DE0 の概要

• エントリーDOI: 10.2210/pdb1de0/pdb
• 関連するPDBエントリー: 1NIP
• 分子名称: NITROGENASE IRON PROTEIN, IRON/SULFUR CLUSTER (3 entities in total)
• 機能のキーワード: redox proteins, [fes] clusters, fe protein, oxidoreductase
• 由来する生物種: Azotobacter vinelandii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63263.81

構造登録者

Jang, S.B.,Seefeldt, L.C.,Peters, J.W. (登録日: 1999-11-12, 公開日: 2000-02-09, 最終更新日: 2024-02-07)

主引用文献

Jang, S.B.,Seefeldt, L.C.,Peters, J.W.
Modulating the midpoint potential of the [4Fe-4S] cluster of the nitrogenase Fe protein.
Biochemistry, 39:641-648, 2000

PubMed Abstract: Protein-bound [FeS] clusters function widely in biological electron-transfer reactions, where their midpoint potentials control both the kinetics and thermodynamics of these reactions. The polarity of the protein environment around [FeS] clusters appears to contribute largely to modulating their midpoint potentials, with local protein dipoles and water dipoles largely defining the polarity. The function of the [4Fe-4S] cluster containing Fe protein in nitrogenase catalysis is, at least in part, to serve as the nucleotide-dependent electron donor to the MoFe protein which contains the sites for substrate binding and reduction. The ability of the Fe protein to function in this manner is dependent on its ability to adopt the appropriate conformation for productive interaction with the MoFe protein and on its ability to change redox potentials to provide the driving force required for electron transfer. Phenylalanine at position 135 is located near the [4Fe-4S] cluster of nitrogenase Fe protein and has been suggested by amino acid substitution studies to participate in defining both the midpoint potential and the nucleotide-induced changes in the [4Fe-4S] cluster. In the present study, the crystal structure of the Azotobacter vinelandii nitrogenase Fe protein variant having phenylalanine at position 135 substituted by tryptophan has been determined by X-ray diffraction methods and refined to 2.4 A resolution. A comparison of available Fe protein structures not only provides a structural basis for the more positive midpoint potential observed in the tryptophan substituted variant but also suggests a possible general mechanism by which the midpoint potential could be controlled by nucleotide interactions and nitrogenase complex formation.

PubMed: 10651628
DOI: 10.1021/bi991694v

実験手法

X-RAY DIFFRACTION (2.4 Å)