Binding sites of quinones in photosynthetic bacterial reaction centers investigated by light-induced FTIR difference spectroscopy: Binding of chainless symmetrical quinones to the QA site of Rhodobacter sphaeroides.
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00207a007
Cited by 57 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Time-resolved FTIR difference spectroscopy for the study of photosystem I with high potential naphthoquinones incorporated into the A1 binding site 2: Identification of neutral state quinone bands;Photosynthesis Research;2023-07-21
2. Calculated vibrational properties of pigments in protein binding sites 2: Semiquinones in photosynthetic proteins;Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy;2023-07
3. Time-resolved FTIR Difference Spectroscopy for the Study of Photosystem I with High Potential Naphthoquinones Incorporated into the A 1 Binding Site. Identification of Neutral State Quinone Bands;2023-04-17
4. Time-resolved FTIR difference spectroscopy for the study of photosystem I with high potential naphthoquinones incorporated into the A1 binding site;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2023-01
5. Resolving the Impact of Hydrogen Bonding on the Phylloquinone Cofactor through Two-Dimensional Infrared Spectroscopy;J PHYS CHEM B;2022
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