Characterization and evaluation of photolabile (µ-peroxo)(µ-hydroxo)bis[bis(bipyridyl)cobalt caged oxygen compounds to facilitate time-resolved crystallographic studies of cytochrome c oxidase
(2024) In Photochemical and Photobiological Sciences 23(5). p.839-851- Abstract
Photolabile (µ-peroxo)(µ-hydroxo)bis[bis(bipyridyl)-cobalt-based caged oxygen compounds have been synthesized and characterized by optical absorbance spectroscopy, X-ray crystallography. and the quantum yield and redox stability were investigated. Furthermore, conditions were established where redox incompatibilities encountered between caged oxygen compounds and oxygen-dependant cytochrome c oxidase (CcO) could be circumvented. Herein, we demonstrate that millimolar concentrations of molecular oxygen can be released from a caged oxygen compound with spatio-temporal control upon laser excitation, triggering enzymatic turnover in cytochrome c oxidase. Spectroscopic evidence confirms the attainment of a homogeneous reaction initiation at... (More)
Photolabile (µ-peroxo)(µ-hydroxo)bis[bis(bipyridyl)-cobalt-based caged oxygen compounds have been synthesized and characterized by optical absorbance spectroscopy, X-ray crystallography. and the quantum yield and redox stability were investigated. Furthermore, conditions were established where redox incompatibilities encountered between caged oxygen compounds and oxygen-dependant cytochrome c oxidase (CcO) could be circumvented. Herein, we demonstrate that millimolar concentrations of molecular oxygen can be released from a caged oxygen compound with spatio-temporal control upon laser excitation, triggering enzymatic turnover in cytochrome c oxidase. Spectroscopic evidence confirms the attainment of a homogeneous reaction initiation at concentrations and conditions relevant for further crystallography studies. This was demonstrated by the oxidizing microcrystals of reduced CcO by liberation of millimolar concentrations of molecular oxygen from a caged oxygen compound. We believe this will expand the scope of available techniques for the detailed investigation of oxygen-dependant enzymes with its native substrate and facilitate further time-resolved X-ray based studies such as wide/small angle X-ray scattering and serial femtosecond crystallography. Graphical abstract: (Figure presented.).
(Less)
- author
- Sandelin, Emil ; Johannesson, Jonatan ; Wendt, Ola LU ; Brändén, Gisela ; Neutze, Richard and Wallentin, Carl Johan LU
- organization
- publishing date
- 2024-05
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Caged oxygen, Cytochrome c oxidase, Time-resolved studies
- in
- Photochemical and Photobiological Sciences
- volume
- 23
- issue
- 5
- pages
- 13 pages
- publisher
- Royal Society of Chemistry
- external identifiers
-
- scopus:85190282658
- pmid:38615307
- ISSN
- 1474-905X
- DOI
- 10.1007/s43630-024-00558-x
- language
- English
- LU publication?
- yes
- id
- eef93282-c178-4298-afbf-ab280e13a272
- date added to LUP
- 2025-01-14 14:33:42
- date last changed
- 2025-07-16 05:31:05
@article{eef93282-c178-4298-afbf-ab280e13a272,
abstract = {{<p>Photolabile (µ-peroxo)(µ-hydroxo)bis[bis(bipyridyl)-cobalt-based caged oxygen compounds have been synthesized and characterized by optical absorbance spectroscopy, X-ray crystallography. and the quantum yield and redox stability were investigated. Furthermore, conditions were established where redox incompatibilities encountered between caged oxygen compounds and oxygen-dependant cytochrome c oxidase (CcO) could be circumvented. Herein, we demonstrate that millimolar concentrations of molecular oxygen can be released from a caged oxygen compound with spatio-temporal control upon laser excitation, triggering enzymatic turnover in cytochrome c oxidase. Spectroscopic evidence confirms the attainment of a homogeneous reaction initiation at concentrations and conditions relevant for further crystallography studies. This was demonstrated by the oxidizing microcrystals of reduced CcO by liberation of millimolar concentrations of molecular oxygen from a caged oxygen compound. We believe this will expand the scope of available techniques for the detailed investigation of oxygen-dependant enzymes with its native substrate and facilitate further time-resolved X-ray based studies such as wide/small angle X-ray scattering and serial femtosecond crystallography. Graphical abstract: (Figure presented.).</p>}},
author = {{Sandelin, Emil and Johannesson, Jonatan and Wendt, Ola and Brändén, Gisela and Neutze, Richard and Wallentin, Carl Johan}},
issn = {{1474-905X}},
keywords = {{Caged oxygen; Cytochrome c oxidase; Time-resolved studies}},
language = {{eng}},
number = {{5}},
pages = {{839--851}},
publisher = {{Royal Society of Chemistry}},
series = {{Photochemical and Photobiological Sciences}},
title = {{Characterization and evaluation of photolabile (µ-peroxo)(µ-hydroxo)bis[bis(bipyridyl)cobalt caged oxygen compounds to facilitate time-resolved crystallographic studies of cytochrome c oxidase}},
url = {{http://dx.doi.org/10.1007/s43630-024-00558-x}},
doi = {{10.1007/s43630-024-00558-x}},
volume = {{23}},
year = {{2024}},
}