Photothermal Conversion and Temperature Elevation by a Minimal Heme Protein

Ooto, Shima; Ishikawa, Haruto; Urui, Taito et al.

The Journal of Physical Chemistry B, 2026, 130(27), 6807-6815

Number of Access:63（2026-08-17 10:52 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/105233

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Title
Photothermal Conversion and Temperature Elevation by a Minimal Heme Protein
Creator
CreatorName
Ooto, Shima
NRID
1000040551338 1000040551338
ORCID
0000-0001-6362-5719 0000-0001-6362-5719
researchmap permalink
haruto haruto
Scopus Author ID
7404013908 7404013908
CreatorName
Ishikawa, Haruto
NRID
1000081013943 1000081013943
ORCID
0009-0009-1970-8256 0009-0009-1970-8256
researchmap permalink
uruitaito uruitaito
Scopus Author ID
57226073766 57226073766
CreatorName
Urui, Taito
NRID
1000060270469 1000060270469
ORCID
0000-0002-3754-5720 0000-0002-3754-5720
researchmap permalink
read0182663 read0182663
Scopus Author ID
7202969842 7202969842
CreatorName
Mizutani, Yasuhisa
Description
Ooto Shima, Ishikawa Haruto, Urui Taito, et al. Photothermal Conversion and Temperature Elevation by a Minimal Heme Protein. The Journal of Physical Chemistry B 130, 6807 (2026); https://doi.org/10.1021/acs.jpcb.6c02792.
Abstract
Heat plays a crucial role in biological systems, functioning both as an energy source and as a signaling stimulus. However, precise intracellular heating tools remain limited. Small, biocompatible molecular heaters capable of localized photothermal conversion are therefore essential for advancing cellular thermobiology. Here, we investigated the photothermal conversion ability of cytochrome b5 from Hadesarchaea archaeon YNP_N21 (HaCytb5), a minimal heme protein. Temperature changes in aqueous solution under 532 nm laser irradiation were monitored using Raman spectroscopy. HaCytb5 exhibits exceptional thermal stability attributed in part to a covalent heme-polypeptide linkage. Upon irradiation, it induced a temperature increase up to 7.0 K, sufficient to activate thermosensitive proteins. Importantly, His-tagging did not significantly alter the thermal stability or heating ability of HaCytb5, indicating that organelle-localization signals can be incorporated without sacrificing its molecular heater function. Furthermore, thermal diffusion modeling reasonably aligns with experimental data, confirming efficient photothermal heating. These findings highlight HaCytb5 as a potent, minimally perturbative thermogenic agent, offering a promising nanoscale tool for localized intracellular heating and potential investigation of temperature heterogeneity within living cells.
Publisher
American Chemical Society (ACS)
Source Title
The Journal of Physical Chemistry B
Volume (Issue)
130(27)
Page
6807-6815
Date of Issued
2026-06-25
Handle URL
https://hdl.handle.net/11094/105233
PISSN
15206106
eISSN
15205207
Relation.isVersionOf
DOI (Publisher Version)
https://doi.org/10.1021/acs.jpcb.6c02792
Access Rights
embargoed access
CopyRight
This document is the Accepted Manuscript version of a Published Work that appeared in final form in The Journal of Physical Chemistry B, © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.jpcb.6c02792.
The full-text file will be made open to the public on 25 June 2027 in accordance with the publisher's policy.
oaire:version
Accepted Manuscript
Category
学術雑誌論文 Journal Article