波紋
Online ISSN : 1884-636X
Print ISSN : 1349-046X
ISSN-L : 1349-046X
サイエンス記事
ビリン還元酵素PcyAの二つの変異体の吸収スペクトルおよび反応の変化とプロトン化状態との相関
海野 昌喜城塚 達也杉島 正一和田 啓萩原 義徳矢野 直峰Andreas Ostermann日下 勝弘
著者情報
ジャーナル フリー

2023 年 33 巻 4 号 p. 151-156

詳細
抄録

PcyA is an enzyme that biosynthesizes phycocyanobilin, a pigment used in photosynthesis and photosensing from the heme metabolite biliverdin. A single residue mutation of key amino acids within PcyA alters the electronic absorption spectra in the state in complex with biliverdin. The differences in the spectra have been proposed to reflect differences in the protonation states of the biliverdin bound to the PcyA mutants, however, to date, there have been no examples of the protonation states of the biliverdin bound to the PcyA mutants being visualized. In this study, the protonation states near the biliverdin-binding site of the two mutants was successfully visualized and proved the hypothesis by a combination of neutron crystallography and computational chemistry.

著者関連情報
© 2023 日本中性子科学会
前の記事
feedback
Top