4CVT

Structure of Apobacterioferritin Y58F variant

4CVT の概要

• エントリーDOI: 10.2210/pdb4cvt/pdb
• 関連するPDBエントリー: 4CVP 4CVR 4CVS
• 分子名称: BACTERIOFERRITIN, ZINC ION (3 entities in total)
• 機能のキーワード: oxidoreductase, electron transfer
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18872.82

構造登録者

Hingorani, K.,Pace, R.,Whitney, S.,Murray, J.W.,Wydrzynski, T.,Cheah, M.H.,Smith, P.,Hillier, W. (登録日: 2014-03-29, 公開日: 2014-08-20, 最終更新日: 2023-12-20)

主引用文献

Hingorani, K.,Pace, R.,Whitney, S.,Murray, J.W.,Smith, P.,Cheah, M.H.,Wydrzynski, T.,Hillier, W.
Photo-Oxidation of Tyrosine in a Bio-Engineered Bacterioferritin 'Reaction Centre'-A Protein Model for Artificial Photosynthesis.
Biochim.Biophys.Acta, 1837:1821-, 2014

PubMed Abstract: The photosynthetic reaction centre (RC) is central to the conversion of solar energy into chemical energy and is a model for bio-mimetic engineering approaches to this end. We describe bio-engineering of a Photosystem II (PSII) RC inspired peptide model, building on our earlier studies. A non-photosynthetic haem containing bacterioferritin (BFR) from Escherichia coli that expresses as a homodimer was used as a protein scaffold, incorporating redox-active cofactors mimicking those of PSII. Desirable properties include: a di-nuclear metal binding site which provides ligands for bivalent metals, a hydrophobic pocket at the dimer interface which can bind a photosensitive porphyrin and presence of tyrosine residues proximal to the bound cofactors, which can be utilised as efficient electron-tunnelling intermediates. Light-induced electron transfer from proximal tyrosine residues to the photo-oxidised ZnCe6(•+), in the modified BFR reconstituted with both ZnCe6 and Mn(II), is presented. Three site-specific tyrosine variants (Y25F, Y58F and Y45F) were made to localise the redox-active tyrosine in the engineered system. The results indicate that: presence of bound Mn(II) is necessary to observe tyrosine oxidation in all BFR variants; Y45 the most important tyrosine as an immediate electron donor to the oxidised ZnCe6(•+) and that Y25 and Y58 are both redox-active in this system, but appear to function interchangebaly. High-resolution (2.1Å) crystal structures of the tyrosine variants show that there are no mutation-induced effects on the overall 3-D structure of the protein. Small effects are observed in the Y45F variant. Here, the BFR-RC represents a protein model for artificial photosynthesis.

PubMed: 25107631
DOI: 10.1016/J.BBABIO.2014.07.019

実験手法

X-RAY DIFFRACTION (1.794 Å)