Literature DB >> 24231746

Spectroscopic studies on the interaction of Ga3+-hypocrellin A with myoglobin.

Wenli Xie1, Shaohua Wei1, Jihua Liu2, Xuefeng Ge1, Lin Zhou3, Jiahong Zhou4, Jian Shen1.   

Abstract

In this article, the interaction mechanism of Ga(3+)-hypocrellin A (Ga(3+)-HA) with myoglobin (Mb) is studied in detail through various spectroscopic technologies. UV-vis absorption and fluorescence spectra demonstrate the interaction process. The Stern-Volmer plot and the time-resolved fluorescence study suggest the fluorescence quenching mechanism of Mb by Ga(3+)-HA is a static quenching procedure, and the electronic transfer forces play a major role in binding Ga(3+)-HA to Mb. Furthermore, synchronous fluorescence studies and circular dichroism (CD) spectra reveal that the conformation of Mb is changed after its conjugation with Ga(3+)-HA.
Copyright © 2013 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Circular dichroism spectroscopy; Ga(3+)-hypocrellin A; Myoglobin; Steady state fluorescence spectroscopy; Time-resolved fluorescence spectroscopy; UV–vis absorption spectroscopy

Mesh:

Substances:

Year:  2013        PMID: 24231746     DOI: 10.1016/j.saa.2013.10.085

Source DB:  PubMed          Journal:  Spectrochim Acta A Mol Biomol Spectrosc        ISSN: 1386-1425            Impact factor:   4.098


  1 in total

1.  "Rigid" structure is a key determinant for the low digestibility of myoglobin.

Authors:  Qian Li; Di Zhao; Hui Liu; Miao Zhang; Shuai Jiang; Xinglian Xu; Guanghong Zhou; Chunbao Li
Journal:  Food Chem X       Date:  2020-06-10
  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.