Highly malleable haem-binding site of the haemoprotein HasA permits stable accommodation of bulky tetraphenylporphycenes-Reference-Cited by-同舟云学术

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Highly malleable haem-binding site of the haemoprotein HasA permits stable accommodation of bulky tetraphenylporphycenes

Published:2019 Issue:32 Volume:9 Page:18697-18702
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Sakakibara Erika¹²³⁴⁵^ORCID,Shisaka Yuma¹²³⁴⁵^ORCID,Onoda Hiroki¹²³⁴⁵^ORCID,Koga Daiki⁶⁷⁸⁹⁵,Xu Ning⁶⁷⁸⁹⁵,Ono Toshikazu⁶⁷⁸⁹⁵^ORCID,Hisaeda Yoshio⁶⁷⁸⁹⁵^ORCID,Sugimoto Hiroshi¹⁰¹¹¹²⁵¹³,Shiro Yoshitsugu¹⁴¹⁵¹⁶¹⁷⁵,Watanabe Yoshihito¹⁸³⁴⁵^ORCID,Shoji Osami¹²³⁴⁵^ORCID

Affiliation:

1. Department of Chemistry

2. Graduate School of Science

3. Nagoya University

4. Nagoya 464-0802

5. Japan

6. Department of Chemistry and Biochemistry

7. Graduate School of Engineering

8. Kyushu University

9. Fukuoka 819-0395

10. Core Research for Evolutional Science and Technology (CREST)

11. Japan Science and Technology Agency

12. Tokyo

13. RIKEN SPring-8 Center

14. Department of Life Science

15. Graduate School of Life Science

16. University of Hyogo

17. Akoh

18. Research Center for Materials Science

Abstract

Bulky metallo-tetraphenylporphycene was successfully incorporated into haemophore HasA which have flexible loops surrounding heme-binding site.

Funder

Japan Society for the Promotion of Science

Core Research for Evolutional Science and Technology

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2019/RA/C9RA02872B

Reference29 articles.

1. C(sp3)–H Bond Hydroxylation Catalyzed by Myoglobin Reconstituted with Manganese Porphycene

2. Abiological catalysis by artificial haem proteins containing noble metals in place of iron

3. Reconstitution of full-length P450BM3 with an artificial metal complex by utilising the transpeptidase Sortase A

4. Correction to “An Evolved Orthogonal Enzyme/Cofactor Pair”

5. Ru-Porphyrin Protein Scaffolds for Sensing O2

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1. Heme-substituted protein assembly bridged by synthetic porphyrin: achieving controlled configuration while maintaining rotational freedom;RSC Advances;2024

2. Diversifying the functions of heme proteins with non-porphyrin cofactors;Journal of Inorganic Biochemistry;2023-09

3. Heme-containing proteins: Structures, functions, and engineering;Comprehensive Inorganic Chemistry III;2023

4. Bridging the gap: Unveiling novel functions of a bacterial haem-acquisition protein capturing diverse synthetic porphyrinoids;Coordination Chemistry Reviews;2022-12

5. Tetraphenylporphyrin Enters the Ring: First Example of a Complex between Highly Bulky Porphyrins and a Protein**;ChemBioChem;2022-04-13

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